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1. Hoffmann K, Mehrle S, Schmidt J, Büchler MW, Märten A: Interferon-alpha restitutes the chemosensitivity in pancreatic cancer. Anticancer Res; 2008 May-Jun;28(3A):1499-507
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Interferon-alpha restitutes the chemosensitivity in pancreatic cancer.
  • BACKGROUND: Multidrug resistance is a major obstacle in the treatment of pancreatic cancer.
  • Immunochemotherapy including interferon-alpha increases response rates and survival.
  • MATERIALS AND METHODS: Pancreatic cancer was induced in an orthotopic mouse model.
  • Animals received standard chemotherapy or combinative treatment with interferon-alpha.
  • Immunological phenotyping, cytotoxic activity assays and analysis of T-cell activation status were performed.
  • RESULTS: Addition of interferon-alpha to chemotherapeutic regimes significantly reduced chemotherapy-induced expression of multidrug resistance proteins and drug efflux activity of cancer cells.
  • Tumor size and metastatic seeding decreased significantly upon combination therapy and survival was prolonged.
  • A significantly higher proportion of activated and cytotoxic active CD8+ tumor infiltrating lymphocytes was detectable after induction of drug resistance.
  • CONCLUSION: Restitution of chemosensitivity by the addition of interferon alpha to chemotherapy was demonstrated in experimental pancreatic cancer for the first time.
  • Since drug-resistance proteins may function as tumor antigens, our data support immunochemotherapy as an encouraging new approach.
  • [MeSH-major] Antineoplastic Combined Chemotherapy Protocols / pharmacology. Carcinoma, Pancreatic Ductal / therapy. Interferon-alpha / pharmacology. Pancreatic Neoplasms / therapy
  • [MeSH-minor] Cell Line, Tumor. Cisplatin / administration & dosage. Combined Modality Therapy. Deoxycytidine / administration & dosage. Deoxycytidine / analogs & derivatives. Drug Resistance, Multiple. Drug Resistance, Neoplasm. Drug Synergism. Fluorouracil / administration & dosage. Humans. P-Glycoprotein / biosynthesis. P-Glycoprotein / metabolism

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  • (PMID = 18630504.001).
  • [ISSN] 0250-7005
  • [Journal-full-title] Anticancer research
  • [ISO-abbreviation] Anticancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Greece
  • [Chemical-registry-number] 0 / Interferon-alpha; 0 / P-Glycoprotein; 0W860991D6 / Deoxycytidine; B76N6SBZ8R / gemcitabine; Q20Q21Q62J / Cisplatin; U3P01618RT / Fluorouracil
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2. Walsh N, Clynes M, Crown J, O'Donovan N: Alterations in integrin expression modulates invasion of pancreatic cancer cells. J Exp Clin Cancer Res; 2009;28:140
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  • [Title] Alterations in integrin expression modulates invasion of pancreatic cancer cells.
  • BACKGROUND: Factors mediating the invasion of pancreatic cancer cells through the extracellular matrix (ECM) are not fully understood.
  • METHODS: In this study, sub-populations of the human pancreatic cancer cell line, MiaPaCa-2 were established which displayed differences in invasion, adhesion, anoikis, anchorage-independent growth and integrin expression.
  • Integrins beta 1, alpha 5 and alpha 6 were over-expressed in Clone #8.
  • Using small interfering RNA (siRNA), integrin beta1 knockdown in Clone #8 cells increased invasion through matrigel and fibronectin, increased motility, decreased adhesion and anoikis.
  • Integrin alpha 5 and alpha 6 knockdown also resulted in increased motility, invasion through matrigel and decreased adhesion.
  • Analysis of these clonal populations of MiaPaCa-2 provides a model for investigations into the invasive properties of pancreatic carcinoma.
  • [MeSH-major] Integrins / biosynthesis. Neoplasm Invasiveness / pathology. Pancreatic Neoplasms / pathology
  • [MeSH-minor] Anoikis / genetics. Blotting, Western. Cell Adhesion / genetics. Cell Line, Tumor. Cell Movement / genetics. Gene Expression. Humans. RNA, Small Interfering. Transfection

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  • (PMID = 19825166.001).
  • [ISSN] 1756-9966
  • [Journal-full-title] Journal of experimental & clinical cancer research : CR
  • [ISO-abbreviation] J. Exp. Clin. Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Integrins; 0 / RNA, Small Interfering
  • [Other-IDs] NLM/ PMC2765436
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3. Chen Y, Yu G, Yu D, Zhu M: PKCalpha-induced drug resistance in pancreatic cancer cells is associated with transforming growth factor-beta1. J Exp Clin Cancer Res; 2010;29:104
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  • [Title] PKCalpha-induced drug resistance in pancreatic cancer cells is associated with transforming growth factor-beta1.
  • BACKGROUND: Drug resistance remains a great challenge in the treatment of pancreatic cancer.
  • The goal of this study was to determine whether TGF-beta1 is associated with drug resistance in pancreatic cancer.
  • METHODS: Pancreatic cancer BxPC3 cells were stably transfected with TGF-beta1 cDNA.
  • Cellular morphology and cell cycle were determined and the suppressive subtracted hybridization (SSH) assay was performed to identify differentially expressed genes induced by TGF-beta1.
  • Western blotting and immunohistochemistry were used to detect expression of TGF-beta1-related genes in the cells and tissue samples.
  • After that, the cells were further treated with an anti-cancer drug (e.g., cisplatin) after pre-incubated with the recombinant TGF-beta1 plus PKCalpha inhibitor Gö6976.
  • TGF-beta1 type II receptor, TbetaRII was also knocked down using TbetaRII siRNA to assess the effects of these drugs in the cells.
  • Cell viability was assessed by MTT assay.
  • RESULTS: Overexpression of TGF-beta1 leads to a markedly increased invasion potential but a reduced growth rate in BxPC3 cells.
  • Recombinant TGF-beta1 protein increases expression of PKCalpha in BxPC3 cells, a result that we confirmed by SSH.
  • Moreover, TGF-beta1 reduced the sensitivity of BxPC3 cells to cisplatin treatment, and this was mediated by upregulation of PKCalpha.
  • However, blockage of PKCalpha with Gö6976 and TbetaRII with siRNA reversed the resistance of BxPC3 cells to gemcitabine, even in the presence of TGF-beta1.
  • Immunohistochemical data show that pancreatic cancers overexpress TGF-beta1 and P-gp relative to normal tissues.
  • In addition, TGF-beta1 expression is associated with P-gp and membranous PKCalpha expression in pancreatic cancer.
  • CONCLUSIONS: TGF-beta1-induced drug resistance in pancreatic cancer cells was associated with PKCalpha expression.
  • The PKCalpha inhibitor Gö6976 could be a promising agent to sensitize pancreatic cancer cells to chemotherapy.
  • [MeSH-major] Antineoplastic Combined Chemotherapy Protocols / pharmacology. Drug Resistance, Neoplasm. Extracellular Matrix Proteins / metabolism. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / metabolism. Protein Kinase C-alpha / pharmacology. Transforming Growth Factor beta / metabolism
  • [MeSH-minor] Apoptosis / drug effects. Blotting, Western. Cell Cycle / drug effects. Cell Movement / drug effects. Cell Proliferation / drug effects. Humans. Immunoenzyme Techniques. Protein-Serine-Threonine Kinases / antagonists & inhibitors. Protein-Serine-Threonine Kinases / genetics. Protein-Serine-Threonine Kinases / metabolism. RNA, Messenger / genetics. RNA, Small Interfering / pharmacology. Receptors, Transforming Growth Factor beta / antagonists & inhibitors. Receptors, Transforming Growth Factor beta / genetics. Receptors, Transforming Growth Factor beta / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Subtraction Technique. Tumor Cells, Cultured

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  • (PMID = 20684793.001).
  • [ISSN] 1756-9966
  • [Journal-full-title] Journal of experimental & clinical cancer research : CR
  • [ISO-abbreviation] J. Exp. Clin. Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Extracellular Matrix Proteins; 0 / RNA, Messenger; 0 / RNA, Small Interfering; 0 / Receptors, Transforming Growth Factor beta; 0 / Transforming Growth Factor beta; 148710-76-3 / betaIG-H3 protein; EC 2.7.11.1 / Protein-Serine-Threonine Kinases; EC 2.7.11.13 / Protein Kinase C-alpha; EC 2.7.11.30 / transforming growth factor-beta type II receptor
  • [Other-IDs] NLM/ PMC2924847
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4. Yu R, Nissen NN, Dhall D, Heaney AP: Nesidioblastosis and hyperplasia of alpha cells, microglucagonoma, and nonfunctioning islet cell tumor of the pancreas: review of the literature. Pancreas; 2008 May;36(4):428-31
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  • [Title] Nesidioblastosis and hyperplasia of alpha cells, microglucagonoma, and nonfunctioning islet cell tumor of the pancreas: review of the literature.
  • We report a rare case of nesidioblastosis and hyperplasia of alpha cells, microglucagonoma, and nonfunctioning islet cell tumor of the pancreas.
  • The patient's clinical presentation, diagnosis, treatment, pancreas pathology, and follow-up are reviewed.
  • A 60-year-old patient was incidentally found to harbor a pancreatic mass with markedly elevated glucagon levels but without glucagonoma syndrome.
  • She was initially diagnosed with glucagonoma, and the tumor was resected.
  • Pathological examination demonstrated that the tumor was a nonfunctioning islet cell tumor and revealed nesidioblastosis and hyperplasia of alpha cells and microglucagonoma in the apparently normal surgical margin.
  • No pancreatic tumors recurred 36 months after surgery.
  • This is the third case of alpha-cell nesidioblastosis reported in the English literature.
  • Nesidioblastosis and hyperplasia of alpha cells should be considered in the differential diagnosis of hyperglucagonemia.
  • Somatostatin analog may be used to suppress glucagon secretion in alpha-cell hyperplasia.
  • [MeSH-major] Adenoma, Islet Cell / pathology. Carcinoma, Islet Cell / pathology. Glucagonoma / pathology. Islets of Langerhans / pathology. Nesidioblastosis / pathology. Pancreatic Neoplasms / pathology

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  • (PMID = 18437091.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
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5. Lobo I, Carvalho A, Amaral C, Machado S, Carvalho R: Glucagonoma syndrome and necrolytic migratory erythema. Int J Dermatol; 2010 Jan;49(1):24-9
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  • The glucagonoma syndrome is a rare disorder, characterized by necrolytic migratory erythema, elevated serum glucagon levels, abnormal glucose tolerance, weight loss, and anemia in association with a glucagon-secreting alpha-cell tumor of the pancreas.
  • The clinical investigation revealed a pancreatic glucagonoma with resolution of the cutaneous and systemic features after surgical removal.
  • Early recognition and treatment may prevent metastatic disease and ensure its cure with resolution of the cutaneous and catabolic manifestations.
  • [MeSH-major] Erythema / etiology. Erythema / pathology. Glucagonoma / complications. Pancreatic Neoplasms / complications. Skin / pathology
  • [MeSH-minor] Aged. Biopsy. Glucagon / blood. Humans. Male. Necrosis. Pancreatectomy. Tomography, X-Ray Computed

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  • (PMID = 20465606.001).
  • [ISSN] 1365-4632
  • [Journal-full-title] International journal of dermatology
  • [ISO-abbreviation] Int. J. Dermatol.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 9007-92-5 / Glucagon
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6. Kahlert C, Weber H, Mogler C, Bergmann F, Schirmacher P, Kenngott HG, Matterne U, Mollberg N, Rahbari NN, Hinz U, Koch M, Aigner M, Weitz J: Increased expression of ALCAM/CD166 in pancreatic cancer is an independent prognostic marker for poor survival and early tumour relapse. Br J Cancer; 2009 Aug 4;101(3):457-64
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Increased expression of ALCAM/CD166 in pancreatic cancer is an independent prognostic marker for poor survival and early tumour relapse.
  • BACKGROUND: ALCAM (activated leucocyte cell adhesion molecule, synonym CD166) is a cell adhesion molecule, which belongs to the Ig superfamily.
  • Disruption of the ALCAM-mediated adhesiveness by proteolytic sheddases such as ADAM17 has been suggested to have a relevant impact on tumour invasion.
  • Although the expression of ALCAM is a valuable prognostic and predictive marker in several types of epithelial tumours, its role as a prognostic marker in pancreatic cancer has not yet been reported.
  • METHODS: In this study, paraffin-embedded samples of 97 patients with pancreatic cancer undergoing potentially curative resection were immunostained against ALCAM, ADAM17 and CK19.
  • RESULTS: We could show that in normal pancreatic tissue, ALCAM is predominantly expressed at the cellular membrane, whereas in pancreatic tumour cells, it is mainly localised in the cytoplasm.
  • Overexpression of ADAM17 in pancreatic cancer, however, failed to be a significant prognostic marker and was not coexpressed with ALCAM.
  • CONCLUSIONS: Our findings support the hypothesis that the disruption of ALCAM-mediated adhesiveness is a relevant step in pancreatic cancer progression.
  • Moreover, ALCAM overexpression is a relevant independent prognostic marker for poor survival and early tumour relapse in pancreatic cancer.
  • [MeSH-major] Antigens, CD / analysis. Biomarkers, Tumor / analysis. Cell Adhesion Molecules, Neuronal / analysis. Fetal Proteins / analysis. Neoplasm Recurrence, Local / chemistry. Pancreatic Neoplasms / chemistry
  • [MeSH-minor] ADAM Proteins / analysis. Adult. Aged. Aged, 80 and over. Cell Adhesion. Female. Humans. Immunohistochemistry. Male. Middle Aged. Pancreas / chemistry. Prognosis

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  • (PMID = 19603023.001).
  • [ISSN] 1532-1827
  • [Journal-full-title] British journal of cancer
  • [ISO-abbreviation] Br. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / ALCAM protein, human; 0 / Antigens, CD; 0 / Biomarkers, Tumor; 0 / Cell Adhesion Molecules, Neuronal; 0 / Fetal Proteins; EC 3.4.24.- / ADAM Proteins; EC 3.4.24.- / tumor necrosis factor-alpha convertase
  • [Other-IDs] NLM/ PMC2720248
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7. Chow JY, Ban M, Wu HL, Nguyen F, Huang M, Chung H, Dong H, Carethers JM: TGF-beta downregulates PTEN via activation of NF-kappaB in pancreatic cancer cells. Am J Physiol Gastrointest Liver Physiol; 2010 Feb;298(2):G275-82
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  • [Title] TGF-beta downregulates PTEN via activation of NF-kappaB in pancreatic cancer cells.
  • TGF-beta utilizes receptor-activated SMAD signaling to mediate growth suppression; however, non-SMAD signaling that modulates the TGF-beta response in epithelial cells become apparent when the SMAD signaling is abrogated, a common occurrence in pancreatic cancers.
  • Here, we examined whether TGF-beta utilized NF-kappaB to downregulate PTEN, a gene that is rarely mutated in pancreatic cancers.
  • SMAD4-null BxPc3 and CAPAN-1 pancreatic cancer cells were treated with TGF-beta (10 ng/ml) and lysed, and cellular proteins were analyzed by Western blots using p-IkappaB, p65, and PTEN antibodies.
  • Dominant negative p-IkappaB-alpha-M (NF-kappaB superrepressor) was used to block activation of NF-kappaB.
  • Cell motility was assessed by Boyden chamber migration assay.
  • TGF-beta induced IkappaB-alpha phosphorylation followed by NF-kappaB p65 subunit nuclear translocation and increased NF-kappaB activity.
  • IkappaB-alpha-M blocked TGF-beta-induced NF-kappaB activity, reversed downregulated PTEN promoter activity and PTEN expression, and prevented augmentation of cell motility induced by TGF-beta.
  • Thus TGF-beta suppresses PTEN in pancreatic cancer cells through NF-kappaB activation and enhances cell motility and invasiveness in a SMAD4-independent manner that can be counteracted when TGF-beta-SMAD signaling is restored.
  • The TGF-beta/NF-kappaB/PTEN cascade may be a critical pathway for pancreatic cancer cells to proliferate and metastasize.

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  • (PMID = 19940030.001).
  • [ISSN] 1522-1547
  • [Journal-full-title] American journal of physiology. Gastrointestinal and liver physiology
  • [ISO-abbreviation] Am. J. Physiol. Gastrointest. Liver Physiol.
  • [Language] ENG
  • [Grant] United States / NIDDK NIH HHS / DK / R01 DK067287; United States / NIDDK NIH HHS / DK / R01 DK067287-02; United States / NIDDK NIH HHS / DK / DK-067287; United States / NIDDK NIH HHS / DK / R24 DK080506; United States / NIDDK NIH HHS / DK / DK-073090; United States / NIDDK NIH HHS / DK / DK067287-02; United States / NIDDK NIH HHS / DK / R24 DK080506-01; United States / NIDDK NIH HHS / DK / DK-080506
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / I-kappa B Proteins; 0 / SMAD2 protein, human; 0 / SMAD3 protein, human; 0 / SMAD4 protein, human; 0 / Smad2 Protein; 0 / Smad3 Protein; 0 / Smad4 Protein; 0 / Transcription Factor RelA; 0 / Transforming Growth Factor beta; 139874-52-5 / NF-kappaB inhibitor alpha; EC 3.1.3.48 / PTEN protein, human; EC 3.1.3.67 / PTEN Phosphohydrolase
  • [Other-IDs] NLM/ PMC3774494
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8. Yue T, Goldstein IJ, Hollingsworth MA, Kaul K, Brand RE, Haab BB: The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays. Mol Cell Proteomics; 2009 Jul;8(7):1697-707
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  • [Title] The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays.
  • Changes to the glycan structures of proteins secreted by cancer cells are known to be functionally important and to have potential diagnostic value.
  • Here we report the use of a previously developed antibody-lectin sandwich array method to characterize both the protein and glycan levels of specific mucins and carcinoembryonic antigen-related proteins captured from the sera of pancreatic cancer patients (n = 23) and control subjects (n = 23).
  • The MUC16 protein was frequently elevated in the cancer patients (65% of the patients) but showed no glycan alterations, whereas the MUC1 and MUC5AC proteins were less frequently elevated (30 and 35%, respectively) and showed highly prevalent (up to 65%) and distinct glycan alterations.
  • An unexpected increase in the exposure of alpha-linked mannose also was observed on MUC1 and MUC5ac, indicating possible N-glycan modifications.
  • Because glycan alterations occurred independently from the protein levels, improved identification of the cancer samples was achieved using glycan measurements on specific proteins relative to using the core protein measurements.
  • The most significant elevation was the cancer antigen 19-9 on MUC1, occurring in 19 of 23 (87%) of the cancer patients and one of 23 (4%) of the control subjects.
  • This work gives insight into the prevalence and protein carriers of glycan alterations in pancreatic cancer and points to the potential of using glycan measurements on specific proteins for highly effective biomarkers.

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  • (PMID = 19377061.001).
  • [ISSN] 1535-9484
  • [Journal-full-title] Molecular & cellular proteomics : MCP
  • [ISO-abbreviation] Mol. Cell Proteomics
  • [Language] ENG
  • [Grant] United States / NIGMS NIH HHS / GM / R01 GM029470; United States / NCI NIH HHS / CA / R21 CA122890; United States / NCI NIH HHS / CA / R33 CA122890; United States / NIGMS NIH HHS / GM / GM 29470
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antibodies; 0 / Antigens, Neoplasm; 0 / Biomarkers, Tumor; 0 / Glycoproteins; 0 / Lectins; 0 / MUC5AC protein, human; 0 / Mucin 5AC; 0 / Polysaccharides
  • [Other-IDs] NLM/ PMC2709194
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9. Ito T, Kawabe K, Arita Y, Hisano T, Igarashi H, Funakoshi A, Sumii T, Yamanaka T, Takayanagi R: Evaluation of pancreatic endocrine and exocrine function in patients with autoimmune pancreatitis. Pancreas; 2007 Mar;34(2):254-9
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  • [Title] Evaluation of pancreatic endocrine and exocrine function in patients with autoimmune pancreatitis.
  • OBJECTIVES: Up to now, the characteristics of pancreatic endocrine and exocrine functions in autoimmune pancreatitis (AIP) are still unclear.
  • The aim of this study is to evaluate pancreatic functions in AIP compared with those of chronic pancreatitis (CP).
  • METHODS: Twelve patients with AIP and 25 patients with CP were examined for exocrine and endocrine pancreas.
  • Concerning endocrine function, insulin secretion (C-peptide response) was examined with the glucagon tolerance test and glucagon secretion was examined with the arginine tolerance test.
  • Pathological examination of pancreatic tissues was done on the operative specimens of AIP and CP that could not be clinically excluded from pancreatic cancer.
  • Autoimmune pancreatitis accompanied with diabetes mellitus showed a reduction both in DeltaC-peptide response (beta-cell response) and Deltaglucagon (alpha-cell response).
  • Histologically, AIP showed lymphoplasmatic cells infiltration surrounding the pancreatic ducts, but basement membranes were intact.
  • Furthermore, islet cells in AIP were revealed as almost intact even though they were surrounded by fibrosis.
  • CONCLUSIONS: These findings indicate that exocrine dysfunction with AIP is different from CP because AIP induces stenosis of the pancreatic ducts, but ductal cells that possess the function of bicarbonate secretion are intact, and that endocrine dysfunction with AIP was secondary pancreatic diabetes.
  • [MeSH-major] Autoimmune Diseases / physiopathology. Islets of Langerhans / physiology. Pancreas, Exocrine / physiology. Pancreatitis, Chronic / physiopathology
  • [MeSH-minor] Adult. Aged. Bicarbonates / metabolism. Constriction, Pathologic. Diabetes Mellitus / pathology. Diabetes Mellitus / physiopathology. Female. Fibrosis. Glucagon / secretion. Glucose Intolerance / pathology. Glucose Intolerance / physiopathology. Humans. Insulin / secretion. Male. Middle Aged. Pancreatic Ducts / pathology. Pancreatic Ducts / physiology. Secretin / metabolism

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  • (PMID = 17312466.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bicarbonates; 0 / Insulin; 1393-25-5 / Secretin; 9007-92-5 / Glucagon
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10. Chang Q, Qin R, Huang T, Gao J, Feng Y: Effect of antisense hypoxia-inducible factor 1alpha on progression, metastasis, and chemosensitivity of pancreatic cancer. Pancreas; 2006 Apr;32(3):297-305
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  • [Title] Effect of antisense hypoxia-inducible factor 1alpha on progression, metastasis, and chemosensitivity of pancreatic cancer.
  • OBJECTIVES: The aim of the study was to observe the effect of antisense hypoxia-inducible factor 1alpha (HIF-1alpha) on progression, metastasis, and chemosensitivity of pancreatic cancer.
  • METHODS: BxPc-3 cells transfected with antisense HIF-1alpha plasmid were exposed to 0.5% O2 for 4 hours.
  • Growth inhibition rates and apoptosis rates of BxPc-3 cells under different dosages of chemotherapy agents (5-fluorouracil, doxorubicin, and gemcitabine) were measured by MTT colorimetric assay and flow cytometry.
  • The migration of BxPc-3 cells was assayed using transwell cell culture chambers.
  • Subcutaneous transplantation of BxPc-3 cells in nude mice for 8 weeks was to assess progression and metastasis of pancreatic cancer.
  • The number of migrated BxPc-3 cells in the experimental group was far less than in control (P < 0.05).
  • In vivo, the tumor size and weight in the experimental group were significantly lower than those in control (P < 0.05).
  • CONCLUSION: Our data demonstrate that antisense HIF-1alpha inhibits expressions of survivin and beta1 integrin, enhancing apoptosis in human pancreatic cancer cells and restraining the progression and metastasis of pancreatic cancer.
  • Therefore, HIF-1alpha may play a very important role in progression, metastasis, and chemosensitivity of human pancreatic cancer.
  • Blocking HIF-1alpha in pancreatic cancer cells may offer an avenue for gene therapy.
  • [MeSH-major] Antisense Elements (Genetics) / pharmacology. Hypoxia-Inducible Factor 1, alpha Subunit / antagonists & inhibitors. Pancreatic Neoplasms / drug therapy
  • [MeSH-minor] Animals. Antigens, CD29 / analysis. Antigens, CD29 / genetics. Apoptosis. Cell Line, Tumor. Cell Movement. Colorimetry. Disease Progression. Flow Cytometry. Genetic Therapy. Humans. Inhibitor of Apoptosis Proteins. Male. Mice. Mice, Inbred BALB C. Mice, Nude. Microtubule-Associated Proteins / analysis. Microtubule-Associated Proteins / genetics. Neoplasm Metastasis. Neoplasm Proteins / analysis. Neoplasm Proteins / genetics. Neoplasm Transplantation. Transplantation, Heterologous

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  • (PMID = 16628086.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antigens, CD29; 0 / Antisense Elements (Genetics); 0 / BIRC5 protein, human; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Inhibitor of Apoptosis Proteins; 0 / Microtubule-Associated Proteins; 0 / Neoplasm Proteins
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11. Wei HY, Chen LB, Wang CY: [Correlation of mRNA expression of hypoxia inducible factor-1alpha to biological features of pancreatic cancer]. Ai Zheng; 2005 Feb;24(2):184-8
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  • [Title] [Correlation of mRNA expression of hypoxia inducible factor-1alpha to biological features of pancreatic cancer].
  • BACKGROUND & OBJECTIVE: Hypoxia inducible factor-1alpha(HIF-1alpha) is universally expressed in many types of cells, and plays a key role in modulation of tumor related genes under hypoxia.
  • Our research was to detect mRNA expression of HIF-1alpha,and explore its relationship with biological characteristics of pancreatic cancer, such as tumor angiogenesis, tumor cell proliferation, differentiation, and metastasis.
  • METHODS: Reverse transcription-polymerase chain reaction (RT-PCR) was used to detect mRNA expression of HIF-1alpha in 50 specimens of pancreatic cancer tissues and relevant adjacent tissues.
  • Expressions of Survivin, proliferating cell nuclear antigen (PCNA), and CD34 were measured by SP immunohistochemistry.
  • RESULTS: mRNA level of HIF-1alpha in pancreatic cancer tissues was significantly higher than that in adjacent tissues (0.77+/-0.04 vs. 0.56+/-0.01, P < 0.01).
  • No significant difference in mRNA expression of HIF-1alpha was observed among tumor tissues of different pathologic grades (P > 0.05).
  • mRNA level of HIF-1alpha in pancreatic cancer tissues of stages I-II was significantly higher than that in cancer tissues of stages III-IV (0.79+/-0.05 vs. 0.76+/-0.04, P < 0.05).
  • CONCLUSION: mRNA expression of HIF-1alpha has significant correlations with tumor angiogenesis, cell proliferation, apoptosis, and metastasis of pancreatic cancer.
  • [MeSH-major] Antigens, CD34 / metabolism. Hypoxia-Inducible Factor 1, alpha Subunit / biosynthesis. Microtubule-Associated Proteins / metabolism. Neoplasm Proteins / metabolism. Pancreatic Neoplasms / metabolism. Proliferating Cell Nuclear Antigen / metabolism
  • [MeSH-minor] Adult. Aged. Apoptosis. Cell Proliferation. Female. Humans. Inhibitor of Apoptosis Proteins. Male. Middle Aged. Neoplasm Staging. Neovascularization, Pathologic. Pancreas / metabolism. RNA, Messenger / biosynthesis. RNA, Messenger / genetics

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  • (PMID = 15694030.001).
  • [Journal-full-title] Ai zheng = Aizheng = Chinese journal of cancer
  • [ISO-abbreviation] Ai Zheng
  • [Language] chi
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] China
  • [Chemical-registry-number] 0 / Antigens, CD34; 0 / BIRC5 protein, human; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Inhibitor of Apoptosis Proteins; 0 / Microtubule-Associated Proteins; 0 / Neoplasm Proteins; 0 / Proliferating Cell Nuclear Antigen; 0 / RNA, Messenger
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12. Ripka S, Neesse A, Riedel J, Bug E, Aigner A, Poulsom R, Fulda S, Neoptolemos J, Greenhalf W, Barth P, Gress TM, Michl P: CUX1: target of Akt signalling and mediator of resistance to apoptosis in pancreatic cancer. Gut; 2010 Aug;59(8):1101-10
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  • [Title] CUX1: target of Akt signalling and mediator of resistance to apoptosis in pancreatic cancer.
  • BACKGROUND AND AIMS: The transcription factor CUX1 is known as a regulator of cell differentiation and cell cycle progression.
  • Previously, CUX1 was identified as a modulator of invasiveness in various cancers.
  • Based on expression profiles suggesting a role for CUX1 in mediating chemoresistance, the aim of this study was to characterise the effect of CUX1 on apoptosis as well as its regulation by signalling pathways modulating drug resistance in pancreatic cancer.
  • METHODS: The effect of CUX1 on TRAIL- (tumour necrosis factor-related apoptosis-inducing ligand) and drug-induced apoptosis was analysed using overexpression and knock-down strategies.
  • Furthermore, CUX1 RNA and protein expression was evaluated in human pancreatic cancer and adjacent normal tissues.
  • The antiapoptotic effect of CUX1 was associated with upregulation of BCL2 and downregulation of tumour necrosis factor alpha.
  • CUX1 was significantly overexpressed in pancreatic cancers, as analysed by in situ hybridisation and immunohistochemistry.
  • In vivo, silencing of CUX1 by intratumourally administered polyethylenimine-complexed siRNA led to reduced tumour growth and increased apoptosis in pancreatic cancer xenografts.
  • CONCLUSION: CUX1 was identified as an important mediator of tumour cell survival in pancreatic cancer in vitro and in vivo.
  • [MeSH-major] Apoptosis / physiology. Homeodomain Proteins / physiology. Nuclear Proteins / physiology. Pancreatic Neoplasms / pathology. Proto-Oncogene Proteins c-akt / physiology. Repressor Proteins / physiology
  • [MeSH-minor] Animals. Caspases, Effector / metabolism. Cell Survival / physiology. Gene Expression Profiling. Gene Expression Regulation, Neoplastic. Gene Knockdown Techniques. Genetic Therapy / methods. Humans. Mice. Neoplasm Proteins / physiology. Neoplasm Transplantation. Poly(ADP-ribose) Polymerases / metabolism. RNA, Small Interfering / genetics. Signal Transduction / physiology. TNF-Related Apoptosis-Inducing Ligand / physiology. Transplantation, Heterologous. Tumor Cells, Cultured

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  • [CommentIn] Gut. 2010 Aug;59(8):1014-5 [20639245.001]
  • (PMID = 20442202.001).
  • [ISSN] 1468-3288
  • [Journal-full-title] Gut
  • [ISO-abbreviation] Gut
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / CUX1 protein, human; 0 / Homeodomain Proteins; 0 / Neoplasm Proteins; 0 / Nuclear Proteins; 0 / RNA, Small Interfering; 0 / Repressor Proteins; 0 / TNF-Related Apoptosis-Inducing Ligand; 0 / TNFSF10 protein, human; EC 2.4.2.30 / Poly(ADP-ribose) Polymerases; EC 2.7.11.1 / Proto-Oncogene Proteins c-akt; EC 3.4.22.- / Caspases, Effector
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13. Diamantidis M, Tsapournas G, Kountouras J, Zavos C: New aspects of regulatory signaling pathways and novel therapies in pancreatic cancer. Curr Mol Med; 2008 Feb;8(1):12-37
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  • [Title] New aspects of regulatory signaling pathways and novel therapies in pancreatic cancer.
  • Pancreatic cancer is an exceptionally devastating and incurable disease, the treatment of which has largely been unsuccessful due to higher resistance of pancreatic tumor cells to conventional approaches including surgery, radiation and/or chemotherapy.
  • Therefore, there is a need for development of new and effective chemotherapeutic agents which can target multiple signaling pathways to induce responsiveness of pancreatic cancer cells to death signals.
  • Although crucial advances in our understanding of the molecular pathogenesis of the disease have been made, the exceptional aggressiveness of pancreatic cancer remains largely unexplained.
  • Pancreatic tumor cells have developed remarkable defense mechanisms to evade apoptosis and to increase their resistance to several drugs.
  • Understanding these complex mechanisms has created new hopes concerning pancreatic cancer in the last years and has evoked new therapeutic approaches, many of which undergo clinical trials with promising results to date.
  • The present review provides a comprehensive description of the molecular signaling mainly of the apoptotic pathways implicated in the pathogenesis of pancreatic cancer, an incentive on the potential pathogenetic role of Helicobacter pylori infection and an appraisal of the most recent therapeutic strategies aiming at the repair of molecular lesions and applied at a cell biochemical level.
  • [MeSH-major] Pancreatic Neoplasms. Signal Transduction / physiology
  • [MeSH-minor] Antigens, CD95 / metabolism. Apoptosis / physiology. Caveolin 1 / metabolism. Cyclins / metabolism. Cyclooxygenase 1 / metabolism. Cyclooxygenase 2 / metabolism. Estradiol / analogs & derivatives. Estradiol / metabolism. Fas Ligand Protein / metabolism. Granzymes / metabolism. Humans. Intercellular Signaling Peptides and Proteins / metabolism. Intracellular Signaling Peptides and Proteins / metabolism. Mitochondrial Proteins / metabolism. Mitogen-Activated Protein Kinases / metabolism. Mucins / metabolism. Neuropeptides / metabolism. Perforin / metabolism. Phosphatidylinositol 3-Kinases / metabolism. Proto-Oncogene Proteins c-akt / metabolism. Receptors, Notch / metabolism. TNF-Related Apoptosis-Inducing Ligand / metabolism. Tumor Necrosis Factor-alpha / metabolism

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  • (PMID = 18289011.001).
  • [ISSN] 1566-5240
  • [Journal-full-title] Current molecular medicine
  • [ISO-abbreviation] Curr. Mol. Med.
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Antigens, CD95; 0 / CAV1 protein, human; 0 / Caveolin 1; 0 / Cyclins; 0 / DIABLO protein, human; 0 / Fas Ligand Protein; 0 / Intercellular Signaling Peptides and Proteins; 0 / Intracellular Signaling Peptides and Proteins; 0 / Mitochondrial Proteins; 0 / Mucins; 0 / Neuropeptides; 0 / Receptors, Notch; 0 / TNF-Related Apoptosis-Inducing Ligand; 0 / TNFSF10 protein, human; 0 / Tumor Necrosis Factor-alpha; 126465-35-8 / Perforin; 4TI98Z838E / Estradiol; 6I2QW73SR5 / 2-methoxyestradiol; EC 1.14.99.1 / Cyclooxygenase 1; EC 1.14.99.1 / Cyclooxygenase 2; EC 1.14.99.1 / PTGS2 protein, human; EC 2.7.1.- / Phosphatidylinositol 3-Kinases; EC 2.7.11.1 / Proto-Oncogene Proteins c-akt; EC 2.7.11.24 / Mitogen-Activated Protein Kinases; EC 3.4.21.- / Granzymes
  • [Number-of-references] 226
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14. Neesse A, Wagner M, Ellenrieder V, Bachem M, Gress TM, Buchholz M: Pancreatic stellate cells potentiate proinvasive effects of SERPINE2 expression in pancreatic cancer xenograft tumors. Pancreatology; 2007;7(4):380-5
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  • [Title] Pancreatic stellate cells potentiate proinvasive effects of SERPINE2 expression in pancreatic cancer xenograft tumors.
  • We have previously reported that inducible overexpression of the serine protease inhibitor nexin 2 (SERPINE2) significantly increases local invasiveness of subclones of the pancreatic cancer cell-line SUIT-2 in nude mouse xenografts.
  • This was associated with a striking increase of extracellular matrix deposition in the invasive tumors.
  • Pancreatic stellate cells (PSCs) have recently been identified as the major source of fibrosis in pancreatic adenocarcinomas.
  • Here we report that co-injection of PSCs and tumor cells dramatically enhances the invasive potential of serine protease inhibitor Nexin 2 (SERPINE2)-expressing SUIT-2 cells.
  • 100% (24 of 24) of the SERPINE2-expressing tumors with PSCs grew aggressively invasive, as compared to 39% of SERPINE2-negative tumors with PSCs and 27% of SERPINE2-expressing tumors without PSCs.
  • In contrast to pure cancer cell preparations, SERPINE2 overexpression in the presence of PSCs also resulted in increased tumor growth.
  • Histological evaluation demonstrated the presence of large amounts of ECM deposits co-localizing with cells staining positive for the PSC marker alpha-SMA.
  • We conclude that PSCs actively proliferate in pancreatic cancer xenograft tumors and significantly contribute to the local invasive potential of the tumors.
  • Presence of PSCs enhances the pro-invasive effects of SERPINE2 expression, and SERPINE2 influences tumor growth (as opposed to invasiveness) only in the presence of PSCs.
  • Our data thus suggest that SERPINE2 is an important modulator of tumor cell/host interactions in pancreatic cancer.
  • [MeSH-major] Amyloid beta-Protein Precursor / metabolism. Pancreas / cytology. Receptors, Cell Surface / metabolism
  • [MeSH-minor] Animals. Gene Expression Regulation, Neoplastic. Mice. Mice, Nude. Neoplasm Invasiveness. Neoplasms, Experimental. Pancreatic Neoplasms. Protease Nexins. Transplantation, Heterologous

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  • [Copyright] 2007 S. Karger AG, Basel and IAP
  • (PMID = 17703087.001).
  • [ISSN] 1424-3911
  • [Journal-full-title] Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.]
  • [ISO-abbreviation] Pancreatology
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Switzerland
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor; 0 / Protease Nexins; 0 / Receptors, Cell Surface
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15. Nortier JW, Ogilvie A: A phase II study of early up-front red blood cell transfusion followed by maintenance epoetin-alpha subcutaneously support during chemotherapy. J Clin Oncol; 2009 May 20;27(15_suppl):e20719

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  • [Title] A phase II study of early up-front red blood cell transfusion followed by maintenance epoetin-alpha subcutaneously support during chemotherapy.
  • : e20719 Background: To determine in patients with cancer related anaemia (Hb<11,3 g/d) starting with their chemotherapy the efficacy and safety of up-front red blood cell transfusion and subsequently maintenance epoetin-alpha (Epo) administration.
  • The study target was the range of low-normal Hb levels of 11,3 to 12,9 g/dL aiming at improving tumor oxygenation.
  • All eligible patients with metastatic solid cancers received around their first or second chemotherapy cycle a transfusion of 1-3 units of erythrocytes depending on their Hb level.
  • An intention-to-treatment analysis was performed for the primary objectives in 16 patients (8 with breast-, 4 with colorectal-, 1 with ovarian- and 1 with pancreatic cancer) and reported here.
  • Grade 3/4 adverse events and serious adverse events that occurred were found to be all chemotherapy or progressive disease related.
  • This was presumably related to the lesser than projected yield of the red blood cell transfusion.

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  • (PMID = 27962027.001).
  • [ISSN] 1527-7755
  • [Journal-full-title] Journal of clinical oncology : official journal of the American Society of Clinical Oncology
  • [ISO-abbreviation] J. Clin. Oncol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
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16. Wei H, Wang C, Chen L: Proliferating cell nuclear antigen, survivin, and CD34 expressions in pancreatic cancer and their correlation with hypoxia-inducible factor 1alpha. Pancreas; 2006 Mar;32(2):159-63
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  • [Title] Proliferating cell nuclear antigen, survivin, and CD34 expressions in pancreatic cancer and their correlation with hypoxia-inducible factor 1alpha.
  • OBJECTIVE: Hypoxia-inducible factor 1alpha (HIF-1alpha) has been universally detected in many types of cells and plays a key role in modulation of tumor-related genes.
  • The purpose of this study was to explore the relationship between HIF-1alpha messenger RNA (mRNA) expression and biologic characteristics in pancreatic cancer, such as tumor angiogenesis, tumor cell proliferation, differentiation, apoptosis, and metastasis.
  • The expressions of survivin, proliferating cell nuclear antigen (PCNA), and CD34 proteins were measured immunohistochemically.
  • RESULTS: There was very significant difference in the expression of HIF-1alpha between the pancreatic cancer tissue and adjacent normal tissue (P < 0.01), but no significant difference was found among tumor histopathologic grades (P > 0.05).
  • There was significant difference in the expression of HIF-1alpha mRNA between Japanese Pancreatic Society stages I to II and stages III to IV (P < 0.05).
  • CONCLUSION: The expression level of HIF-1alpha mRNA is surmised to have a significant correlation with tumor angiogenesis, cell proliferation, apoptosis, and metastasis.
  • Inhibition of HIF-1alpha may be an important and approachable therapeutic target for pancreatic cancer.
  • [MeSH-major] Antigens, CD34 / genetics. Microtubule-Associated Proteins / genetics. Neoplasm Proteins / genetics. Pancreatic Neoplasms / genetics. Proliferating Cell Nuclear Antigen / genetics
  • [MeSH-minor] DNA Primers. Humans. Hypoxia-Inducible Factor 1, alpha Subunit / genetics. Inhibitor of Apoptosis Proteins. Neoplasm Staging. RNA, Messenger / genetics. RNA, Neoplasm / genetics. Reverse Transcriptase Polymerase Chain Reaction. Survival Analysis

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  • (PMID = 16552335.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antigens, CD34; 0 / BIRC5 protein, human; 0 / DNA Primers; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Inhibitor of Apoptosis Proteins; 0 / Microtubule-Associated Proteins; 0 / Neoplasm Proteins; 0 / Proliferating Cell Nuclear Antigen; 0 / RNA, Messenger; 0 / RNA, Neoplasm
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17. Stolzenberg-Solomon RZ, Weinstein S, Pollak M, Tao Y, Taylor PR, Virtamo J, Albanes D: Prediagnostic adiponectin concentrations and pancreatic cancer risk in male smokers. Am J Epidemiol; 2008 Nov 1;168(9):1047-55
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  • [Title] Prediagnostic adiponectin concentrations and pancreatic cancer risk in male smokers.
  • The authors conducted a nested case-control study in the Alpha-Tocopherol, Beta-Carotene Cancer Prevention Study cohort, a cohort of male Finnish smokers aged 50-69 years at baseline, to test whether prediagnostic adiponectin concentrations are associated with pancreatic cancer.
  • Between January 1985 and October 2004, 311 incident exocrine pancreatic cancer cases were diagnosed among cohort participants with serum samples.
  • Controls (n = 510) were alive and free of cancer at the time the case was diagnosed and were matched to the cases by age and date of blood drawing.
  • The authors used conditional logistic regression adjusted for smoking, blood pressure, and C-peptide level to calculate odds ratios and 95% confidence intervals for pancreatic cancer.
  • Higher adiponectin concentrations were inversely associated with pancreatic cancer (for highest quintile (> 9.8 microg/mL) vs. lowest (< or =4.6 microg/mL), odds ratio = 0.65, 95% confidence interval: 0.39, 1.07; P-trend = 0.04).
  • These results support the hypothesis that higher adiponectin concentrations may be inversely associated with the development of pancreatic cancer.

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  • (PMID = 18801887.001).
  • [ISSN] 1476-6256
  • [Journal-full-title] American journal of epidemiology
  • [ISO-abbreviation] Am. J. Epidemiol.
  • [Language] ENG
  • [Grant] United States / CCR NIH HHS / RC / N01-RC-45035; United States / CCR NIH HHS / RC / N01-RC-37004; United States / Intramural NIH HHS / / ; United States / NCI NIH HHS / CN / N01-CN-45165; United States / CCR NIH HHS / RC / N01RC37004; United States / NCI NIH HHS / CN / N01 CN045165
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Adiponectin
  • [Other-IDs] NLM/ PMC2720773
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18. Abe Y, Ito T, Baba E, Nagafuji K, Kawabe K, Choi I, Arita Y, Miyamoto T, Teshima T, Nakano S, Harada M: Nonmyeloablative allogeneic hematopoietic stem cell transplantation as immunotherapy for pancreatic cancer. Pancreas; 2009 Oct;38(7):815-9
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  • [Title] Nonmyeloablative allogeneic hematopoietic stem cell transplantation as immunotherapy for pancreatic cancer.
  • OBJECTIVE: Advanced unresectable pancreatic cancer has an extremely poor prognosis despite intensive chemotherapy.
  • As a new therapeutic modality, we investigated nonmyeloablative allogeneic hematopoietic stem cell transplantation from a related donor.
  • METHODS: Five patients with chemotherapy-resistant pancreatic cancer received allogeneic peripheral blood stem cell transplantation after a conditioning regimen consisting of low-dose total body irradiation and fludarabine.
  • The prophylaxis for graft-versus-host disease consisted of mycophenolate mofetil and cyclosporine.
  • RESULTS: The median age of the 5 patients was 54 years, and the median duration from diagnosis to nonmyeloablative allogeneic hematopoietic stem cell transplantation was 10 months.
  • Three of the 5 patients achieved complete donor chimerism of peripheral T cells, at a median time of day 42.
  • Acute graft-versus-host disease developed in 3 patients: grade 2 in 2 patients and grade 1 in 1.
  • Tumor reduction was observed in 2 patients: 1 patient showed disappearance of the pancreatic tumor, and the other patient showed approximately 20% reduction of the tumor.
  • Marked elevation of tumor necrosis factor alpha was observed as the tumor regressed.
  • CONCLUSIONS: Although advanced pancreatic cancer progresses rapidly, some graft-versus-tumor effects and pivotal role of tumor necrosis factor alpha were suggested.
  • [MeSH-major] Hematopoietic Stem Cell Transplantation / methods. Immunotherapy / methods. Pancreatic Neoplasms / therapy
  • [MeSH-minor] Adult. Antineoplastic Agents / administration & dosage. Antineoplastic Combined Chemotherapy Protocols / therapeutic use. Cyclosporine / administration & dosage. Female. Graft vs Host Disease / metabolism. Graft vs Host Disease / prevention & control. Humans. Male. Middle Aged. Mycophenolic Acid / administration & dosage. Mycophenolic Acid / analogs & derivatives. Time Factors. Transplantation Conditioning. Transplantation, Homologous. Tumor Necrosis Factor-alpha / metabolism. Vidarabine / administration & dosage. Vidarabine / analogs & derivatives. Whole-Body Irradiation

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  • (PMID = 19696692.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antineoplastic Agents; 0 / Tumor Necrosis Factor-alpha; 83HN0GTJ6D / Cyclosporine; 9242ECW6R0 / mycophenolate mofetil; FA2DM6879K / Vidarabine; HU9DX48N0T / Mycophenolic Acid; P2K93U8740 / fludarabine
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19. Billadeau DD, Chatterjee S, Bramati P, Sreekumar R, Shah V, Hedin K, Urrutia R: Characterization of the CXCR4 signaling in pancreatic cancer cells. Int J Gastrointest Cancer; 2006;37(4):110-9
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  • [Title] Characterization of the CXCR4 signaling in pancreatic cancer cells.
  • CXCL12 and its receptor, CXCR4, are emerging as promising targets for modulating growth, angiogenesis, and metastasis in several human cancers.
  • Indeed, blocking the receptor is sufficient to prevent metastasis and angiogenesis in experimental breast cancer xenografts.
  • Recently, the biological effect of the CXCR4 in pancreatic cancer, one of the most deadly neoplastic diseases, has been reported.
  • In this paper, we characterize the signaling pathways activated by CXCR4 in pancreatic cancer.
  • Analysis of this cascade in pancreatic cancer cells revealed that the ERK-mediated pathway regulates genes involved in angiogenesis, such as VEGF, CD44, HIF1alpha, and IL-8.
  • Furthermore, ERK blockage inhibits the migration and tube formation of endothelial cells induced by CXCL12.
  • Considering that inhibitors for several components of this pathway, including CXCR4 itself, are at different stages of clinical trials, this study provides theoretical justification for the clinical testing of these drugs in pancreatic cancer, thus extending the list of potential targets for treating this dismal disease.
  • [MeSH-major] Aorta / cytology. Cell Movement / physiology. Endothelium, Vascular / cytology. Pancreatic Neoplasms / metabolism. Receptors, CXCR4 / metabolism. Signal Transduction
  • [MeSH-minor] Antigens, CD44 / metabolism. Blotting, Western. Cell Adhesion. Cell Proliferation. Enzyme Inhibitors / pharmacology. Gene Expression Profiling. Humans. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Immunoprecipitation. Interleukin-8 / metabolism. MAP Kinase Signaling System. Neovascularization, Physiologic. Oligonucleotide Array Sequence Analysis. Phosphatidylinositol 3-Kinases / metabolism. Phosphorylation. Receptor, Epidermal Growth Factor / metabolism. Tyrosine / metabolism. Vascular Endothelial Growth Factor A / metabolism

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  • (PMID = 18175225.001).
  • [ISSN] 1537-3649
  • [Journal-full-title] International journal of gastrointestinal cancer
  • [ISO-abbreviation] Int J Gastrointest Cancer
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / P50-CA102701; United States / NIGMS NIH HHS / GM / R01 GM59763; United States / NIDDK NIH HHS / DK / R01 DK052913; United States / NIDDK NIH HHS / DK / R01 DK52913; United States / NCI NIH HHS / CA / P50 CA102701; United States / NIDDK NIH HHS / DK / R01 DK56620; United States / NCI NIH HHS / CA / P20 CA102701; United States / PHS HHS / / R01 59388
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antigens, CD44; 0 / CD44 protein, human; 0 / Enzyme Inhibitors; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Interleukin-8; 0 / Receptors, CXCR4; 0 / VEGFA protein, human; 0 / Vascular Endothelial Growth Factor A; 42HK56048U / Tyrosine; EC 2.7.1.- / Phosphatidylinositol 3-Kinases; EC 2.7.10.1 / Receptor, Epidermal Growth Factor
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20. Guo X, Li T, Wang Y, Shao L, Zhang Y, Ma D, Han W: CMTM5 induces apoptosis of pancreatic cancer cells and has synergistic effects with TNF-alpha. Biochem Biophys Res Commun; 2009 Sep 11;387(1):139-42
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  • [Title] CMTM5 induces apoptosis of pancreatic cancer cells and has synergistic effects with TNF-alpha.
  • Our previous data show that CKLF-like MARVEL transmembrane domain-containing member 5 (CMTM5) is a potential tumor suppressor gene, but its function in pancreatic cancer is unknown.
  • Herein we first report that CMTM5 is also absent in pancreatic cancer cell lines with promoter methylation.
  • Compared with normal pancreatic tissues, CMTM5 is significantly decreased in cancer tissues.
  • Restoration of CMTM5-v1 not only induces MIA PaCa-2 cell apoptosis with activation of caspase 3, 8 and 9, but also has synergistic effects with TNF-alpha.
  • Thus, CMTM5 may play a role in the pancreatic cancer.
  • [MeSH-major] Apoptosis. Chemokines / metabolism. Pancreatic Neoplasms / metabolism. Tumor Suppressor Proteins / metabolism
  • [MeSH-minor] Caspase 3 / metabolism. Caspase 8 / metabolism. Caspase 9 / metabolism. DNA Methylation. Gene Silencing. Humans. MARVEL Domain-Containing Proteins. Promoter Regions, Genetic. Tumor Necrosis Factor-alpha / pharmacology

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  • (PMID = 19577543.001).
  • [ISSN] 1090-2104
  • [Journal-full-title] Biochemical and biophysical research communications
  • [ISO-abbreviation] Biochem. Biophys. Res. Commun.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / CMTM5 protein, human; 0 / Chemokines; 0 / MARVEL Domain-Containing Proteins; 0 / Tumor Necrosis Factor-alpha; 0 / Tumor Suppressor Proteins; EC 3.4.22.- / Caspase 3; EC 3.4.22.- / Caspase 8; EC 3.4.22.- / Caspase 9
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21. Weiss FU, Marques IJ, Woltering JM, Vlecken DH, Aghdassi A, Partecke LI, Heidecke CD, Lerch MM, Bagowski CP: Retinoic acid receptor antagonists inhibit miR-10a expression and block metastatic behavior of pancreatic cancer. Gastroenterology; 2009 Dec;137(6):2136-45.e1-7
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  • [Title] Retinoic acid receptor antagonists inhibit miR-10a expression and block metastatic behavior of pancreatic cancer.
  • BACKGROUND & AIMS: The infiltrating ductal adenocarcinoma of the pancreas is among the most lethal of all solid malignancies, largely owing to a high frequency of early metastasis.
  • We identified microRNA-10a (miR-10a) as an important mediator of metastasis formation in pancreatic tumor cells and investigated the upstream and downstream regulatory mechanisms of miR-10a.
  • METHODS: Northern blot analysis revealed increased expression levels of miR-10a in metastatic pancreatic adenocarcinoma.
  • The role of miR-10a was analyzed by Morpholino and short interfering RNA transfection of pancreatic carcinoma cell lines and resected specimens of human pancreatic carcinoma.
  • Metastatic behavior of primary pancreatic tumors and cancer cell lines was tested in xenotransplantation experiments in zebrafish embryos.
  • RESULTS: We show that miR-10a expression promotes metastatic behavior of pancreatic tumor cells and that repression of miR-10a is sufficient to inhibit invasion and metastasis formation.
  • Interestingly, suppression of HOXB1 and HOXB3 in pancreatic cancer cells is sufficient to promote metastasis formation.
  • CONCLUSIONS: These findings suggest that miR-10a is a key mediator of metastatic behavior in pancreatic cancer, which regulates metastasis via suppression of HOXB1 and HOXB3.
  • [MeSH-major] Adenocarcinoma / therapy. Benzoates / pharmacology. Chromans / pharmacology. Gene Expression Regulation, Neoplastic / drug effects. Genetic Therapy. MicroRNAs / metabolism. Pancreatic Neoplasms / therapy. Receptors, Retinoic Acid / antagonists & inhibitors
  • [MeSH-minor] Animals. Blotting, Northern. Cadherins / metabolism. Cell Line, Tumor. Homeodomain Proteins / genetics. Homeodomain Proteins / metabolism. Humans. Morpholines / metabolism. Neoplasm Invasiveness. Oligonucleotides, Antisense / metabolism. RNA Interference. RNA, Small Interfering / metabolism. Retinoids / pharmacology. Transfection. Up-Regulation. Xenograft Model Antitumor Assays. Zebrafish / embryology. alpha Catenin / metabolism. beta Catenin / metabolism

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  • (PMID = 19747919.001).
  • [ISSN] 1528-0012
  • [Journal-full-title] Gastroenterology
  • [ISO-abbreviation] Gastroenterology
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Benzoates; 0 / CDH1 protein, human; 0 / CTNNB1 protein, human; 0 / Cadherins; 0 / Chromans; 0 / HOXB1 homeodomain protein; 0 / Homeodomain Proteins; 0 / HoxB3 protein, human; 0 / MicroRNAs; 0 / Morpholines; 0 / Oligonucleotides, Antisense; 0 / RNA, Small Interfering; 0 / Receptors, Retinoic Acid; 0 / Retinoids; 0 / alpha Catenin; 0 / beta Catenin; 144092-31-9 / Ro 41-5253
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22. Li Z, Fallon J, Mandeli J, Wetmur J, Woo SL: A genetically enhanced anaerobic bacterium for oncopathic therapy of pancreatic cancer. J Natl Cancer Inst; 2008 Oct 1;100(19):1389-400
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  • [Title] A genetically enhanced anaerobic bacterium for oncopathic therapy of pancreatic cancer.
  • BACKGROUND: A major obstacle in treatment of solid tumors is the inefficient delivery of therapeutic agents to the hypoxic cores.
  • Hypoxia offers the potential for anaerobic bacteria colonization and tumor destruction by the bacteria, and dormant spores of wild-type Clostridium perfringens (Cp) germinate and proliferate within the hypoxic cores of pancreatic tumors in mice.
  • METHODS: Recombinant Cp strains in which superoxide dismutase, a major oxygen tolerance gene, was deleted (Cp/sod(-)) were constructed to enhance its selective growth in tumors.
  • The ability of the recombinant Cp strains to kill tumors was investigated in C57/BL6 mice bearing murine PANC02 tumors.
  • RESULTS: Cp/sod(-) showed reduced toxic effects compared with wild-type Cp when spores were administered intravenously into PANC02 tumor-bearing mice.
  • Mice treated with Cp/sod(-)/PVL spores demonstrated a reduction in neutrophils and macrophages in tumors, logarithmically elevated growth of intratumoral bacteria, enhanced tumor necrosis, and substantially prolonged survival without apparent systemic and organ toxic effects, compared with mice treated with both wild-type Cp and Cp/sod(-) spores.
  • Accordingly, 47% of Cp/sod(-)/PVL-treated mice (n = 15) achieved tumor-free survival for over 120 days, whereas all mice treated with Cp/sod(-) or phosphate-buffered saline (n = 10 per group) died within 50 days.
  • CONCLUSIONS: Cp/sod(-)/PVL provides a prototype for a novel class of oncopathic microbes that may have potential for the safe and effective treatment of pancreatic cancer and other poorly vascularized tumors.

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  • [CommentIn] NIH Guide Grants Contracts. 2016 Jul 29;:NOT-OD-16-124 [27483554.001]
  • [RetractionIn] Li Z, Fallon J, Mandeli J, Wetmur J, Woo SL. J Natl Cancer Inst. 2010 Feb 24;102(4):283 [20176752.001]
  • [CommentIn] Fed Regist. 2016 Jul 25;81(142):48426-48427 [27737274.001]
  • (PMID = 18812551.001).
  • [ISSN] 1460-2105
  • [Journal-full-title] Journal of the National Cancer Institute
  • [ISO-abbreviation] J. Natl. Cancer Inst.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / CA-120017
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Retracted Publication
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bacterial Toxins; 0 / Biomarkers, Tumor; 0 / Exotoxins; 0 / Hif1a protein, mouse; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Leukocidins; 0 / Panton-Valentine leukocidin; EC 1.15.1.1 / Superoxide Dismutase
  • [Other-IDs] NLM/ PMC2720732
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23. Kumagai T, Akagi T, Desmond JC, Kawamata N, Gery S, Imai Y, Song JH, Gui D, Said J, Koeffler HP: Epigenetic regulation and molecular characterization of C/EBPalpha in pancreatic cancer cells. Int J Cancer; 2009 Feb 15;124(4):827-33
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  • [Title] Epigenetic regulation and molecular characterization of C/EBPalpha in pancreatic cancer cells.
  • Molecular-targeted therapy is a hopeful approach for pancreatic cancer.
  • Silencing of tumor suppressor genes can occur by histone deacetylation and/or DNA methylation in the promoter.
  • Here, we identified epigenetically silenced genes in pancreatic cancer cells.
  • Pancreatic cancer cell line, PANC-1 cells were treated either with or without 5Aza-dC (a DNA methyltransferase inhibitor) and suberoylanilide hydroxamic acid (SAHA, a histone deacetylase inhibitor), and mRNA was isolated from these cells.
  • The induction of these 4 genes was validated by real-time PCR in several pancreatic cancer cell lines.
  • Interestingly, expression of C/EBPalpha was significantly restored in 6 of 6 pancreatic cancer cell lines.
  • Chromatin immunoprecipitation assay revealed that histone H3 of the promoter region of C/EBPalpha was acetylated in PANC-1 treated with SAHA; and bisulfate sequencing showed methylation of its promoter region in several pancreatic cancer cell lines.
  • Forced expression of C/EBPalpha markedly suppressed clonal proliferation of PANC-1 cells.
  • Immunohistochemical analysis revealed that C/EBPalpha localized in the cytoplasm in pancreatic adenocarcinoma cells, whereas it localized predominantly in the nucleus in normal pancreatic cells.
  • Our data demonstrated that aberrant silencing, as well as, inappropriate cytoplasmic localization of C/EBPalpha causes dysregulation of its function, suggesting that C/EBPalpha is a novel candidate tumor suppressor gene in pancreatic cancer cells.

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  • (PMID = 19035457.001).
  • [ISSN] 1097-0215
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / R01 CA026038; United States / NCI NIH HHS / CA / R01 CA026038-21; United States / NCI NIH HHS / CA / R01 CA026038-29; United States / NCI NIH HHS / CA / 5R01CA026038-30
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antigens, Neoplasm; 0 / Antineoplastic Agents; 0 / CCAAT-Enhancer-Binding Protein-alpha; 0 / E2F1 Transcription Factor; 0 / Histones; 0 / Hydroxamic Acids; 58IFB293JI / vorinostat
  • [Other-IDs] NLM/ NIHMS323849; NLM/ PMC3471542
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24. Gong XG, Lv YF, Li XQ, Xu FG, Ma QY: Gemcitabine resistance induced by interaction between alternatively spliced segment of tenascin-C and annexin A2 in pancreatic cancer cells. Biol Pharm Bull; 2010;33(8):1261-7
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  • [Title] Gemcitabine resistance induced by interaction between alternatively spliced segment of tenascin-C and annexin A2 in pancreatic cancer cells.
  • Pancreatic cancer is the fourth leading cause of cancer-related death in the western countries and it is resistant to almost all cytotoxic drugs.
  • In the pancreatic cancer cell culture system in vitro, it was proved that exogenous recombinant TNfnA-D combined with the cell surface ANXA2 specifically and their interaction suppressed gemcitabine-induced cytotoxicity on pancreatic cancer cells in a dose-dependent manner.
  • Meanwhile, the TNfnA-D/ANXA2 interaction increased the phosphorylation of phosphatidylinositol 3-kinase (PI3K), Akt, inhibitory kappaB (IkappaB) kinase alpha/beta (IKKalpha/beta), IkappaBalpha, and p65 nuclear factor-kappaB (NF-kappaB) significantly.
  • For the first time, this study show that ANXA2/TNfnA-D interaction induced gemcitabine resistance via the canonical PI3K/Akt/NF-kappaB signaling pathways in pancreatic cancer cells.
  • Therefore, therapy targeting ANXA2/TNfnA-D and/or p65 NF-kappaB may have potential clinical application for patients with pancreatic cancers.
  • [MeSH-major] Alternative Splicing. Annexin A2 / biosynthesis. Antimetabolites, Antineoplastic / pharmacology. Deoxycytidine / analogs & derivatives. Drug Resistance, Neoplasm. Pancreatic Neoplasms / pathology. Tenascin / biosynthesis
  • [MeSH-minor] Blotting, Western. Cell Culture Techniques. Cell Line, Tumor. Cell Proliferation / drug effects. Dose-Response Relationship, Drug. Down-Regulation. Flow Cytometry. Humans. Phosphorylation. Promoter Regions, Genetic. Protein Binding. RNA, Small Interfering / genetics. Recombinant Proteins / biosynthesis. Recombinant Proteins / genetics. Transcription Factor RelA / biosynthesis

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  • (PMID = 20686216.001).
  • [ISSN] 1347-5215
  • [Journal-full-title] Biological & pharmaceutical bulletin
  • [ISO-abbreviation] Biol. Pharm. Bull.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] Japan
  • [Chemical-registry-number] 0 / ANXA2 protein, human; 0 / Annexin A2; 0 / Antimetabolites, Antineoplastic; 0 / RNA, Small Interfering; 0 / Recombinant Proteins; 0 / Tenascin; 0 / Transcription Factor RelA; 0W860991D6 / Deoxycytidine; B76N6SBZ8R / gemcitabine
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25. Bobe G, Weinstein SJ, Albanes D, Hirvonen T, Ashby J, Taylor PR, Virtamo J, Stolzenberg-Solomon RZ: Flavonoid intake and risk of pancreatic cancer in male smokers (Finland). Cancer Epidemiol Biomarkers Prev; 2008 Mar;17(3):553-62
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  • [Title] Flavonoid intake and risk of pancreatic cancer in male smokers (Finland).
  • Extending research on the protective effect of flavonoids in cell culture and animal studies, we examined the association between consumption of flavonoids and flavonoid-rich foods and development of exocrine pancreatic cancer within the alpha-Tocopherol, beta-Carotene Cancer Prevention Study cohort.
  • Of the 27,111 healthy male smokers (50-69 years) who completed a self-administered dietary questionnaire at baseline, 306 developed exocrine pancreatic cancer during follow-up (1985-2004; median, 16.1 years).
  • Overall, flavonoid intake was not significantly associated with pancreatic cancer.
  • However, in stratified analysis, greater total flavonoid intake was associated with decreased pancreatic cancer risk in participants randomized during the trial to placebo (fourth versus first quartile: hazard ratio, 0.36; 95% confidence interval, 0.17-0.78; P trend = 0.009) and not to supplemental alpha-tocopherol (50 mg/d) and/or beta-carotene (20 mg/d; P interaction = 0.002).
  • Our data suggest that a flavonoid-rich diet may decrease pancreatic cancer risk in male smokers not consuming supplemental alpha-tocopherol and/or beta-carotene.
  • [MeSH-major] Flavonoids / administration & dosage. Pancreatic Neoplasms / epidemiology. Smoking / adverse effects

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  • (PMID = 18349272.001).
  • [ISSN] 1055-9965
  • [Journal-full-title] Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology
  • [ISO-abbreviation] Cancer Epidemiol. Biomarkers Prev.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CN / N01-CN-45165; United States / CCR NIH HHS / RC / N01-RC-37004; United States / CCR NIH HHS / RC / N01-RC-45035; United States / Intramural NIH HHS / /
  • [Publication-type] Journal Article; Randomized Controlled Trial; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Flavonoids
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26. Dineen SP, Roland CL, Greer R, Carbon JG, Toombs JE, Gupta P, Bardeesy N, Sun H, Williams N, Minna JD, Brekken RA: Smac mimetic increases chemotherapy response and improves survival in mice with pancreatic cancer. Cancer Res; 2010 Apr 1;70(7):2852-61
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  • [Title] Smac mimetic increases chemotherapy response and improves survival in mice with pancreatic cancer.
  • Failure of chemotherapy in the treatment of pancreatic cancer is often due to resistance to therapy-induced apoptosis.
  • We show that JP1201, a Smac mimetic, is a potent enhancer of chemotherapy in robust mouse models of pancreatic cancer.
  • Combination of JP1201 with gemcitabine reduced primary and metastatic tumor burden in orthotopic xenograft and syngenic tumor models, induced regression of established tumors, and prolonged survival in xenograft and transgenic models of pancreatic cancer.
  • The effect of JP1201 was phenocopied by XIAP small interfering RNA in vitro and correlated with elevated levels of tumor necrosis factor alpha protein in vivo.
  • The continued development of JP1201 and other strategies designed to enhance therapy-induced apoptosis in pancreatic cancer is warranted.

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  • (PMID = 20332237.001).
  • [ISSN] 1538-7445
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / CA070907-12; United States / NCI NIH HHS / CA / P50 CA070907; United States / NCI NIH HHS / CA / P50 CA070907-12
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / DIABLO protein, human; 0 / Intracellular Signaling Peptides and Proteins; 0 / Mitochondrial Proteins; 0 / RNA, Small Interfering; 0 / TNF-Related Apoptosis-Inducing Ligand; 0 / Tumor Necrosis Factor-alpha; 0 / X-Linked Inhibitor of Apoptosis Protein; 0W860991D6 / Deoxycytidine; B76N6SBZ8R / gemcitabine
  • [Other-IDs] NLM/ NIHMS175711; NLM/ PMC2848888
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27. Nakashima H, Nakamura M, Yamaguchi H, Yamanaka N, Akiyoshi T, Koga K, Yamaguchi K, Tsuneyoshi M, Tanaka M, Katano M: Nuclear factor-kappaB contributes to hedgehog signaling pathway activation through sonic hedgehog induction in pancreatic cancer. Cancer Res; 2006 Jul 15;66(14):7041-9
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  • [Title] Nuclear factor-kappaB contributes to hedgehog signaling pathway activation through sonic hedgehog induction in pancreatic cancer.
  • The hedgehog (Hh) signaling pathway, which functions as an organizer in embryonic development, is implicated in the development of various tumors.
  • In pancreatic cancer, pathway activation is reported to result from aberrant expression of the ligand, sonic Hh (Shh).
  • We hypothesized that nuclear factor-kappaB (NF-kappaB), a hallmark transcription factor in inflammatory responses, contributes to the overexpression of Shh in pancreatic cancer.
  • In the present study, we found a close positive correlation between NF-kappaB p65 and Shh expression in surgically resected pancreas specimens, including specimens of chronic pancreatitis and pancreatic adenocarcinoma.
  • We showed that blockade of NF-kappaB suppressed constitutive expression of Shh mRNA in pancreatic cancer cells.
  • Further activation of NF-kappaB by inflammatory stimuli, including interleukin-1beta, tumor necrosis factor-alpha, and lipopolysaccharide, induced overexpression of Shh, resulting in activation of the Hh pathway.
  • NF-kappaB-induced Shh expression actually activated the Hh pathway in a ligand-dependent manner and enhanced cell proliferation in pancreatic cancer cells.
  • In addition, inhibition of the Hh pathway as well as NF-kappaB suppressed the enhanced cell proliferation.
  • Our data suggest that NF-kappaB activation is one of the mechanisms underlying Shh overexpression in pancreatic cancer and that proliferation of pancreatic cancer cells is accelerated by NF-kappaB activation in part through Shh overexpression.
  • [MeSH-major] Carcinoma, Pancreatic Ductal / metabolism. NF-kappa B / metabolism. Pancreatic Neoplasms / metabolism. Trans-Activators / biosynthesis
  • [MeSH-minor] Animals. COS Cells. Cell Growth Processes / physiology. Cell Line, Tumor. Cercopithecus aethiops. Hedgehog Proteins. Humans. RNA, Messenger / biosynthesis. RNA, Messenger / genetics. Signal Transduction. Transcription Factor RelA / biosynthesis. Transcription Factor RelA / metabolism. Up-Regulation

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  • (PMID = 16849549.001).
  • [ISSN] 0008-5472
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Hedgehog Proteins; 0 / NF-kappa B; 0 / RNA, Messenger; 0 / SHH protein, human; 0 / Trans-Activators; 0 / Transcription Factor RelA
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28. Ide Y, Miyoshi E, Nakagawa T, Gu J, Tanemura M, Nishida T, Ito T, Yamamoto H, Kozutsumi Y, Taniguchi N: Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer. Biochem Biophys Res Commun; 2006 Mar 10;341(2):478-82
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  • [Title] Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer.
  • The goal of this study was to identify glycosyltransferases that are specifically expressed in pancreatic cancer.
  • To investigate the gene expression of glycosyltransferases between pancreatic cancer and normal pancreatic tissues, we performed DNA-microarray (involving about 1000 oligosaccharide-related genes) using RNA mixtures of pancreatic cancer cells and normal pancreatic tissues.
  • Eighty-six genes were up-regulated and thirty-two were down-regulated in pancreatic cancer, compared to normal pancreatic tissue.
  • Among these changes, it is noteworthy that the expression of GnT-IVa was decreased and the expression of GnT-IVb was increased in pancreatic cancer, compared to normal pancreatic tissues.
  • Although GnT-IVa and -IVb are involved in the same reaction as a glycosyltransferase, their chromosomal localization is different.
  • When 5 cases of pancreatic cancer tissues were examined using the real-time RT-PCR method, the expression of GnT-IVb was dominant in tumor tissues and the expression of GnT-IVa was dominant in the surrounding normal tissues.
  • The expression of GnT-IVa was increased in all 3 cell lines that had been treated with 5-aza-C and butyrate.
  • These results suggest that the down-regulation of GnT-IVa in pancreatic cancer cells is due to an epigenetic abnormality in the gene.
  • [MeSH-major] Gene Expression Regulation, Neoplastic. N-Acetylglucosaminyltransferases / biosynthesis. N-Acetylglucosaminyltransferases / chemistry. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Antimetabolites, Antineoplastic / pharmacology. Azacitidine / pharmacology. Blotting, Northern. Butyrates / pharmacology. Cell Line, Tumor. Down-Regulation. Epigenesis, Genetic. Female. Genes, Dominant. Humans. Male. Models, Biological. Oligonucleotide Array Sequence Analysis. Oligosaccharides / chemistry. Pancreas / metabolism. Protein Isoforms. RNA, Messenger / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Up-Regulation

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  • (PMID = 16434023.001).
  • [ISSN] 0006-291X
  • [Journal-full-title] Biochemical and biophysical research communications
  • [ISO-abbreviation] Biochem. Biophys. Res. Commun.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antimetabolites, Antineoplastic; 0 / Butyrates; 0 / Oligosaccharides; 0 / Protein Isoforms; 0 / RNA, Messenger; EC 2.4.1.- / N-Acetylglucosaminyltransferases; EC 2.4.1.145 / alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase; M801H13NRU / Azacitidine
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29. Grzesiak JJ, Bouvet M: Divalent cations modulate the integrin-mediated malignant phenotype in pancreatic cancer cells. Cancer Sci; 2008 Aug;99(8):1553-63
Hazardous Substances Data Bank. CALCIUM, ELEMENTAL .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Divalent cations modulate the integrin-mediated malignant phenotype in pancreatic cancer cells.
  • We have previously demonstrated that pathophysiological shifts in the concentrations of extracellular Mg(2+) and Ca(2+) activate the alpha(2)beta(1) integrin-mediated malignant phenotype on type I collagen in pancreatic cancer cells, as evidenced by increased adhesion, migration and proliferation.
  • In the present study, we examined the integrin and divalent cation specificity of pancreatic cancer cell interactions with other physiologically relevant extracellular matrix proteins, including fibronectin, type IV collagen, laminin and vitronectin.
  • Our results indicate that, like alpha(2)beta(1) integrin-mediated interactions with type I collagen, beta(1) integrin-mediated adhesion to fibronectin, type IV collagen and laminin are promoted by Mg(2+) but not by Ca(2+).
  • On vitronectin, cells attach via alpha(v)beta(5) and beta(1) integrins, and in the presence of either divalent cation.
  • We also demonstrate that, like type I collagen, pancreatic cancer cell migration and proliferation on fibronectin, laminin and type IV collagen is maximal when Mg(2+) is present at concentrations that promote optimal adhesion and Ca(2+) is present at concentrations less than Mg(2+).
  • On vitronectin, Panc-1 cell migration is maximal with decreased Mg(2+) and increased Ca(2+), but the reverse is true for BxPC-3 cells.
  • Both cell lines exhibited maximal proliferation with increased Mg(2+) and decreased Ca(2+), however.
  • Together with evidence indicating that the in vivo local tumor microenvironment contains increased Mg(2+) and decreased Ca(2+), our studies demonstrate that such divalent cation shifts could activate the integrin-mediated malignant phenotype in pancreatic cancer.
  • [MeSH-major] Calcium / metabolism. Cations / metabolism. Integrins / metabolism. Magnesium / metabolism. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Antigens, CD29 / metabolism. Cell Adhesion / physiology. Cell Proliferation. Collagen Type IV / metabolism. Fibronectins / metabolism. Humans. Integrin alpha2beta1 / metabolism. Laminin. Phenotype. Tumor Cells, Cultured. Vitronectin / metabolism

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  • (PMID = 18754866.001).
  • [ISSN] 1349-7006
  • [Journal-full-title] Cancer science
  • [ISO-abbreviation] Cancer Sci.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA109949-03
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Antigens, CD29; 0 / Cations; 0 / Collagen Type IV; 0 / Fibronectins; 0 / Integrin alpha2beta1; 0 / Integrins; 0 / Laminin; 0 / Vitronectin; I38ZP9992A / Magnesium; SY7Q814VUP / Calcium
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30. Mulé JJ: Dendritic cell-based vaccines for pancreatic cancer and melanoma. Ann N Y Acad Sci; 2009 Sep;1174:33-40
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  • [Title] Dendritic cell-based vaccines for pancreatic cancer and melanoma.
  • Based on leads from our recent animal studies, we are embarking on a series of new clinical trials to evaluate potential improvements in dendritic cell (DC)-based vaccines for melanoma and pancreatic cancer.
  • The first new strategy involves the use of a powerful chemokine (denoted secondary lymphoid tissue chemokine; SLC/CCL-21), which can both create functioning lymph node-like structures at sites of vaccination with tumor-loaded DCs and dramatically enhance vaccine efficacy in animal tumor models.
  • The second strategy, in the setting of pancreatic cancer, involves a gene therapy and immunotherapy combination of a locally administered tumor necrosis factor-alpha gene vector followed by radiation (to induce tumor apoptosis/necrosis) and intratumorally administered monocyte-derived DCs (to uptake and present antigens from dying tumor cells to elicit potent, systemic, antitumor immunity).
  • [MeSH-major] Cancer Vaccines / therapeutic use. Dendritic Cells / immunology. Melanoma / immunology. Pancreatic Neoplasms / immunology
  • [MeSH-minor] Animals. Bone Marrow Transplantation. Chemokine CCL21 / immunology. Chemokines / immunology. Chemokines / therapeutic use. Chemokines, C / immunology. Humans. Immunotherapy / methods. Lymph Nodes / immunology. Mice. Skin / immunology. Skin Neoplasms / immunology. Skin Neoplasms / radiotherapy. Skin Neoplasms / surgery. Whole-Body Irradiation

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  • (PMID = 19769734.001).
  • [ISSN] 1749-6632
  • [Journal-full-title] Annals of the New York Academy of Sciences
  • [ISO-abbreviation] Ann. N. Y. Acad. Sci.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Cancer Vaccines; 0 / Chemokine CCL21; 0 / Chemokines; 0 / Chemokines, C; 0 / XCL1 protein, human
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31. Poch B, Lotspeich E, Ramadani M, Gansauge S, Beger HG, Gansauge F: Systemic immune dysfunction in pancreatic cancer patients. Langenbecks Arch Surg; 2007 May;392(3):353-8
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  • [Title] Systemic immune dysfunction in pancreatic cancer patients.
  • BACKGROUND AND AIMS: We investigated the immune status in 32 pancreatic cancer patients (PC) in comparison with healthy controls (HC).
  • MATERIALS AND METHODS: Using flow cytometry, peripheral blood lymphocytes (PBL) were characterized by the expression of surface markers for T helper cells (CD4), T suppressor cells (CD8), B cells (CD19) and NK cells (CD56).
  • The serum levels of TNF-alpha, IL-1beta, IL-2, IL-10, IL-12, IL-18, IL-1RA, sIL-2R and TGF-beta were determined by ELISA.
  • In PC, we found reduced serum levels of IL-2 and significantly elevated levels of TNF-alpha, TGF-beta1, IL-10, IL-2R, IL-1beta and IL-1RA.
  • CONCLUSION: These data provide evidence for a systemic immune dysfunction in pancreatic cancer patients characterized by a shift towards a T helper cell type 2 cytokine profile, a significant elevation of substances related to T cell suppression and a reduced blastogenic response to PHA and anti-CD3 antibodies of PBL.
  • [MeSH-major] Cytokines / blood. Lymphocytes / immunology. Pancreatic Neoplasms / immunology
  • [MeSH-minor] Aged. Aged, 80 and over. Case-Control Studies. Female. Humans. Immunity, Cellular. Immunophenotyping. Interleukins / blood. Male. Middle Aged. Mitogens / pharmacology. Prospective Studies. Transforming Growth Factor alpha / blood. Transforming Growth Factor beta / blood. Treatment Outcome

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  • [Journal-full-title] Langenbeck's archives of surgery
  • [ISO-abbreviation] Langenbecks Arch Surg
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
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32. Yadav VR, Sung B, Prasad S, Kannappan R, Cho SG, Liu M, Chaturvedi MM, Aggarwal BB: Celastrol suppresses invasion of colon and pancreatic cancer cells through the downregulation of expression of CXCR4 chemokine receptor. J Mol Med (Berl); 2010 Dec;88(12):1243-53
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  • [Title] Celastrol suppresses invasion of colon and pancreatic cancer cells through the downregulation of expression of CXCR4 chemokine receptor.
  • Although metastasis accounts for >90% of cancer-related deaths, no therapeutic that targets this process has yet been approved.
  • Because the chemokine receptor CXCR4 is one of the targets closely linked with tumor metastasis, inhibitors of this receptor have the potential to abrogate metastasis.
  • In the current report, we demonstrate that celastrol can downregulate the CXCR4 expression on breast cancer MCF-7 cells stably transfected with HER2, an oncogene known to induce the chemokine receptor.
  • Downregulation of CXCR4 by the triterpenoid was not cell type-specific as downregulation occurred in colon cancer, squamous cell carcinoma, and pancreatic cancer cells.
  • Abrogation of the chemokine receptor by celastrol or by gene-silencing was accompanied by suppression of invasiveness of colon cancer cells induced by CXCL12, the ligand for CXCR4.
  • This effect was not cell type-specific as celastrol also abolished invasiveness of pancreatic tumor cells, and this effect again correlated with the disappearance of both the CXCR4 mRNA and CXCR4 protein.
  • Overall, these results show that celastrol has potential in suppressing invasion and metastasis of cancer cells by down-modulation of CXCR4 expression.

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  • (PMID = 20798912.001).
  • [ISSN] 1432-1440
  • [Journal-full-title] Journal of molecular medicine (Berlin, Germany)
  • [ISO-abbreviation] J. Mol. Med.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / P01 CA124787; United States / NCI NIH HHS / CA / P01 CA124787-01A2; United States / NCI NIH HHS / CA / CA-124787-01A2
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / CXCR4 protein, human; 0 / Chemokine CXCL12; 0 / HSP90 Heat-Shock Proteins; 0 / NF-kappa B; 0 / Receptors, CXCR4; 0 / Triterpenes; 0 / Tumor Necrosis Factor-alpha; 34157-83-0 / tripterine
  • [Other-IDs] NLM/ NIHMS307553; NLM/ PMC3142743
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33. Kolb A, Kleeff J, Arnold N, Giese NA, Giese T, Korc M, Friess H: Expression and differential signaling of heregulins in pancreatic cancer cells. Int J Cancer; 2007 Feb 1;120(3):514-23
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  • [Title] Expression and differential signaling of heregulins in pancreatic cancer cells.
  • The EGF family of ligands and receptors plays an important role in the pathogenesis of pancreatic ductal adenocarcinoma (PDAC) and contributes to its aggressiveness.
  • Quantitative RT-PCR analysis revealed that HRGs as well as its signaling ErbB receptors were present in 4 of 4 human pancreatic cancer cell lines (PCCL).
  • HRG-beta1 stimulated the growth of 3 of 4 PCCL, whereas HRG-alpha1 inhibited cell growth in 3 of 4 cell lines.
  • Responses towards HRGs could in part be predicted by ErbB2 and ErbB3 expression levels.
  • HRGs induced phosphorylation of different ErbB receptors as well as activation of MAPK, p38MAPK, JNK and PI3K in a cell- and ligand-specific manner.
  • In vivo, HRG was upregulated in pancreatic cancer tissues and localized predominantly in the cancer cells.
  • High HRG-beta levels but not HRG-alpha levels were associated with decreased patient survival.
  • In conclusion, HRG is expressed by pancreatic cancer cells and influences pancreatic cancer cell growth and patient survival.
  • [MeSH-major] Nerve Tissue Proteins / physiology. Pancreatic Neoplasms / physiopathology. Signal Transduction / physiology
  • [MeSH-minor] Cell Line, Tumor. Cell Proliferation / drug effects. Dose-Response Relationship, Drug. Enzyme Activation / drug effects. Epidermal Growth Factor / pharmacology. Gene Expression Regulation, Neoplastic. Humans. Immunoblotting. JNK Mitogen-Activated Protein Kinases / metabolism. Neuregulin-1 / genetics. Neuregulin-1 / pharmacology. Neuregulin-1 / physiology. Phosphatidylinositol 3-Kinases / metabolism. Phosphorylation / drug effects. RNA, Messenger / genetics. RNA, Messenger / metabolism. Receptor, Epidermal Growth Factor / genetics. Receptor, Epidermal Growth Factor / metabolism. Receptor, ErbB-2 / genetics. Receptor, ErbB-2 / metabolism. Receptor, ErbB-3 / genetics. Receptor, ErbB-3 / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Survival Analysis. p38 Mitogen-Activated Protein Kinases / metabolism

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  • (PMID = 17096356.001).
  • [ISSN] 0020-7136
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA-40162
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / NRG1 protein, human; 0 / Nerve Tissue Proteins; 0 / Neuregulin-1; 0 / RNA, Messenger; 0 / heregulin alpha; 155646-83-6 / heregulin beta1; 62229-50-9 / Epidermal Growth Factor; EC 2.7.1.- / Phosphatidylinositol 3-Kinases; EC 2.7.10.1 / Receptor, Epidermal Growth Factor; EC 2.7.10.1 / Receptor, ErbB-2; EC 2.7.10.1 / Receptor, ErbB-3; EC 2.7.11.24 / JNK Mitogen-Activated Protein Kinases; EC 2.7.11.24 / p38 Mitogen-Activated Protein Kinases
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34. El-Rayes BF, Ali S, Philip PA, Sarkar FH: Protein kinase C: a target for therapy in pancreatic cancer. Pancreas; 2008 May;36(4):346-52
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  • [Title] Protein kinase C: a target for therapy in pancreatic cancer.
  • OBJECTIVES: Protein kinase C (PKC) is involved in tumor growth and apoptosis and hence represents a potential target for cancer therapy.
  • This study investigated the expression of PKC in pancreatic tumor tissue in comparison to adjacent normal tissue and determined the modulation of PKC by bryostatin-1 (BRYO) on pancreatic cancer cell lines.
  • METHODS: Pancreatic tissue was obtained from 18 patients who had a resection (14 with ductal adenocarcinoma and 4 with adenoma and high-grade dysplasia).
  • HPAC cells were treated with gemcitabine and BRYO and in sequential and concomitant combination.
  • To evaluate cell viability, apoptosis, and electrophoretic mobility shift assay, 3-(4,5-dimetylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, enzyme-linked immunosorbent assay, and nuclear factor kappaB (NF-kappaB) assays were used.
  • RESULTS: As compared with the adjacent normal tissue, PKC-alpha, PKC-beta1, and PKC-delta were higher in the tumor; PKC-epsilon was higher in the normal tissue.
  • Pretreatment with gemcitabine followed by BRYO resulted in decreased cell viability, increased apoptosis, and inhibited NF-kappaB than either agent alone or BRYO followed by gemcitabine.
  • CONCLUSION: Protein kinase C is overexpressed and activated in pancreatic cancer as compared with normal tissue.
  • Inhibition of PKC could sensitize pancreatic cancer cell lines to the effects of gemcitabine.
  • [MeSH-major] Antineoplastic Combined Chemotherapy Protocols / therapeutic use. Isoenzymes / antagonists & inhibitors. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / enzymology. Protein Kinase C / antagonists & inhibitors
  • [MeSH-minor] Adenocarcinoma / drug therapy. Adenocarcinoma / enzymology. Adenocarcinoma / pathology. Adenoma / drug therapy. Adenoma / enzymology. Adenoma / pathology. Bryostatins / administration & dosage. Cell Survival / drug effects. Deoxycytidine / administration & dosage. Deoxycytidine / analogs & derivatives. Humans. Protein Kinase Inhibitors / therapeutic use. Reference Values

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  • (PMID = 18437080.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bryostatins; 0 / Isoenzymes; 0 / Protein Kinase Inhibitors; 0W860991D6 / Deoxycytidine; 37O2X55Y9E / bryostatin 1; B76N6SBZ8R / gemcitabine; EC 2.7.11.13 / Protein Kinase C
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35. Wang HQ, Meng X, Gao YY, Liu BQ, Niu XF, Zhang HY, Du ZX: Characterization of BAG3 cleavage during apoptosis of pancreatic cancer cells. J Cell Physiol; 2010 Jul;224(1):94-100
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  • [Title] Characterization of BAG3 cleavage during apoptosis of pancreatic cancer cells.
  • Caspases are a conserved family of cell death proteases that cleave intracellular substrates at Asp residues to modify their function and promote apoptosis.
  • In this report, we identify BAG3 as a novel caspases substrate.
  • Cleavage of the BAG3 protein occurs in the C-terminal part of the protein majorly at Asp347 (KEVD347 downward arrow S) in vitro and in pancreatic cancer SW1990 and PANC-1 cells undergoing apoptosis.
  • [MeSH-major] Adaptor Proteins, Signal Transducing / metabolism. Apoptosis. Caspases / metabolism. Pancreatic Neoplasms / enzymology. Protein Processing, Post-Translational
  • [MeSH-minor] Apoptosis Regulatory Proteins. Aspartic Acid. Caspase Inhibitors. Cell Line, Tumor. Cysteine Proteinase Inhibitors / pharmacology. Etoposide / pharmacology. Humans. Leupeptins / pharmacology. Mutation. Peptide Fragments / metabolism. Protein Structure, Tertiary. Recombinant Proteins / metabolism. Staurosporine / pharmacology. Time Factors. Transfection. Tumor Necrosis Factor-alpha / metabolism. Ultraviolet Rays

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  • [Copyright] (c) 2010 Wiley-Liss, Inc.
  • (PMID = 20232307.001).
  • [ISSN] 1097-4652
  • [Journal-full-title] Journal of cellular physiology
  • [ISO-abbreviation] J. Cell. Physiol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Adaptor Proteins, Signal Transducing; 0 / Apoptosis Regulatory Proteins; 0 / BAG3 protein, human; 0 / Caspase Inhibitors; 0 / Cysteine Proteinase Inhibitors; 0 / Leupeptins; 0 / Peptide Fragments; 0 / Recombinant Proteins; 0 / Tumor Necrosis Factor-alpha; 133407-82-6 / benzyloxycarbonylleucyl-leucyl-leucine aldehyde; 30KYC7MIAI / Aspartic Acid; 6PLQ3CP4P3 / Etoposide; EC 3.4.22.- / Caspases; H88EPA0A3N / Staurosporine
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36. Hu HT, Ma QY, Zhang D, Shen SG, Han L, Ma YD, Li RF, Xie KP: HIF-1alpha links beta-adrenoceptor agonists and pancreatic cancer cells under normoxic condition. Acta Pharmacol Sin; 2010 Jan;31(1):102-10
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  • [Title] HIF-1alpha links beta-adrenoceptor agonists and pancreatic cancer cells under normoxic condition.
  • AIM: To examine whether beta-adrenoceptor (beta-AR) agonists can induce hypoxia-inducible factor (HIF)-1alpha accumulation which then up-regulate the expression of its target genes in pancreatic cancer cells at normoxia, and to further elucidate the mechanism involved.
  • METHODS: Pulse-chase assay, RT-PCR, and Western blot were employed to detect the effects of beta-AR agonists and antagonists, siRNA as well as several inhibitors of signal transduction pathways on MIA PaCa2 and BxPC-3 pancreatic cancer cells.
  • RESULTS: Treatment of pancreatic cancer cell lines with beta-AR agonists led to accumulation of HIF-1alpha and then up-regulated expression of its target genes independently of oxygen levels.
  • Our data suggest a novel mechanism in pancreatic cancer cells that links beta-AR and HIF-1alpha signaling under normoxic conditions, with implications for the control of glucose transport, angiogenesis and metastasis.
  • [MeSH-major] Adrenergic beta-Agonists / pharmacology. Hypoxia-Inducible Factor 1, alpha Subunit / drug effects. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Adrenergic beta-1 Receptor Agonists. Adrenergic beta-2 Receptor Agonists. Blotting, Western. Cell Line, Tumor. Cyclic AMP-Dependent Protein Kinases / metabolism. Humans. Mitogen-Activated Protein Kinase 1 / metabolism. Mitogen-Activated Protein Kinase 3 / metabolism. Proto-Oncogene Proteins c-akt / metabolism. RNA, Small Interfering / metabolism. Receptor, Epidermal Growth Factor / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Signal Transduction / drug effects. Up-Regulation / drug effects

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  • (PMID = 20037603.001).
  • [ISSN] 1745-7254
  • [Journal-full-title] Acta pharmacologica Sinica
  • [ISO-abbreviation] Acta Pharmacol. Sin.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Adrenergic beta-1 Receptor Agonists; 0 / Adrenergic beta-2 Receptor Agonists; 0 / Adrenergic beta-Agonists; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / RNA, Small Interfering; EC 2.7.10.1 / Receptor, Epidermal Growth Factor; EC 2.7.11.1 / Proto-Oncogene Proteins c-akt; EC 2.7.11.11 / Cyclic AMP-Dependent Protein Kinases; EC 2.7.11.24 / Mitogen-Activated Protein Kinase 1; EC 2.7.11.24 / Mitogen-Activated Protein Kinase 3
  • [Other-IDs] NLM/ PMC4002695
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37. Orchekowski R, Hamelinck D, Li L, Gliwa E, vanBrocklin M, Marrero JA, Vande Woude GF, Feng Z, Brand R, Haab BB: Antibody microarray profiling reveals individual and combined serum proteins associated with pancreatic cancer. Cancer Res; 2005 Dec 1;65(23):11193-202
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  • [Title] Antibody microarray profiling reveals individual and combined serum proteins associated with pancreatic cancer.
  • We used antibody microarrays to probe the associations of multiple serum proteins with pancreatic cancer and to explore the use of combined measurements for sample classification.
  • Serum samples from pancreatic cancer patients (n = 61), patients with benign pancreatic disease (n = 31), and healthy control subjects (n = 50) were probed in replicate experiment sets by two-color, rolling circle amplification on microarrays containing 92 antibodies and control proteins.
  • The antibodies that had reproducibly different binding levels between the patient classes revealed different types of alterations, reflecting inflammation (high C-reactive protein, alpha-1-antitrypsin, and serum amyloid A), immune response (high IgA), leakage of cell breakdown products (low plasma gelsolin), and possibly altered vitamin K usage or glucose regulation (high protein-induced vitamin K antagonist-II).
  • A logistic-regression algorithm distinguished the cancer samples from the healthy control samples with a 90% and 93% sensitivity and a 90% and 94% specificity in duplicate experiment sets.
  • The cancer samples were distinguished from the benign disease samples with a 95% and 92% sensitivity and an 88% and 74% specificity in duplicate experiment sets.
  • This study furthered the development of antibody microarrays for molecular profiling, provided insights into the nature of serum-protein alterations in pancreatic cancer patients, and showed the potential of combined measurements to improve sample classification accuracy.
  • [MeSH-major] Adenocarcinoma / blood. Blood Proteins / analysis. Pancreatic Neoplasms / blood. Protein Array Analysis / methods


38. Nomoto S, Kinoshita T, Mori T, Kato K, Sugimoto H, Kanazumi N, Takeda S, Nakao A: Adverse prognosis of epigenetic inactivation in RUNX3 gene at 1p36 in human pancreatic cancer. Br J Cancer; 2008 May 20;98(10):1690-5
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  • [Title] Adverse prognosis of epigenetic inactivation in RUNX3 gene at 1p36 in human pancreatic cancer.
  • Alteration in transforming growth factor-beta signalling pathway is one of the main causes of pancreatic cancer.
  • RUNX3 locus 1p36 is commonly deleted in a variety of human cancers, including pancreatic cancer.
  • Therefore, we examined genetic and epigenetic alterations of RUNX3 in human pancreatic cancer.
  • Thirty-two patients with pancreatic cancer were investigated in this study.
  • Promoter hypermethylation was detected in 20 (62.5%) of 32 pancreatic cancer tissues, confirmed by sequence of bisulphite-treated DNA.
  • Loss of heterozygosity was detected in 11 (34.3%) of 32 pancreatic cancers.
  • Hypermethylation and LOH appear to be common mechanisms for inactivation of RUNX3 in pancreatic cancer.
  • Therefore, RUNX3 may be an important tumour suppressor gene related to pancreatic cancer.
  • [MeSH-major] Chromosomes, Human, Pair 1. Core Binding Factor Alpha 3 Subunit / genetics. Gene Silencing. Pancreatic Neoplasms / genetics

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  • (PMID = 18475302.001).
  • [ISSN] 1532-1827
  • [Journal-full-title] British journal of cancer
  • [ISO-abbreviation] Br. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Core Binding Factor Alpha 3 Subunit; 0 / Runx3 protein, human; 0 / Transforming Growth Factor beta
  • [Other-IDs] NLM/ PMC2391125
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39. Fahrig R, Quietzsch D, Heinrich JC, Heinemann V, Boeck S, Schmid RM, Praha C, Liebert A, Sonntag D, Krupitza G, Hänel M: RP101 improves the efficacy of chemotherapy in pancreas carcinoma cell lines and pancreatic cancer patients. Anticancer Drugs; 2006 Oct;17(9):1045-56
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  • [Title] RP101 improves the efficacy of chemotherapy in pancreas carcinoma cell lines and pancreatic cancer patients.
  • RP101 [(E)-5-(2-bromovinyl)-2'-deoxyuridine (BVDU)], which supports apoptosis and prevents the acquisition of chemoresistance, was tested in cultured human pancreatic tumor cells.
  • Furthermore, RP101 activated antitumor immunity as demonstrated by enhanced cytolytic activity of NK-92 natural killer cells.
  • This was concomitant with an enhanced expression of lymphotoxins alpha and beta, natural killer cell transcript 4, tumor necrosis factor LIGHT/TNFSF-14, and intercellular adhesion molecule-1 in pancreas carcinoma cells.
  • These results encouraged us to investigate the effect of RP101 in pancreas cancer patients.
  • In a first pilot study, 13 patients in stage III and VI of the disease were treated with gemcitabine +cisplatin+RP101.
  • A second study with 21 patients in similar stages of disease, treated with RP101+gemcitabine alone, confirmed the results of the pilot study.
  • Considering both studies, the tumor control was 94%.
  • [MeSH-major] Bromodeoxyuridine / analogs & derivatives. Pancreatic Neoplasms / drug therapy
  • [MeSH-minor] Adult. Aged. Cell Line, Tumor. Cisplatin / pharmacology. DNA-(Apurinic or Apyrimidinic Site) Lyase / genetics. Deoxycytidine / analogs & derivatives. Deoxycytidine / pharmacokinetics. Deoxycytidine / pharmacology. Humans. Killer Cells, Natural / immunology. Middle Aged


40. Qu CF, Songl YJ, Rizvi SM, Li Y, Smith R, Perkins AC, Morgenstern A, Brechbiel M, Allen BJ: In vivo and in vitro inhibition of pancreatic cancer growth by targeted alpha therapy using 213Bi-CHX.A"-C595. Cancer Biol Ther; 2005 Aug;4(8):848-53
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  • [Title] In vivo and in vitro inhibition of pancreatic cancer growth by targeted alpha therapy using 213Bi-CHX.A"-C595.
  • PURPOSE: The aim of this study was to investigate the effect of targeted alpha therapy for the control of in vitro pancreatic cancer cell clusters and micrometastatic cancer lesions in vivo.
  • METHODS: The expression of tumor-associated antigen MUC-1 on three pancreatic cancer cell clusters and animal xenografts was detected by indirect immmunostaining.
  • Monoclonal antibodies C595 (test) and A2 (non-specific control) were labeled with 213Bi using the chelator CHX.A" to form the alpha-immunoconjugate (AIC).
  • Cell clusters were incubated with AIC and examined at 48 h.
  • In vivo, an antiproliferative effect for tumors was tested at two days post-subcutaneous cell inoculation.
  • Changes in tumor progression were assessed by tumor size.
  • RESULTS: MUC-1 is strongly expressed on CFPAC-1, PANC-1 and moderate expression was found CAPAN-1 cell clusters and tumor xenografts.
  • The AICs can target and kill cancer cell clusters (100 mm) in vitro.
  • Some 73-81 % of cells were TUNEL positive cells in the clusters after incubation with AIC.
  • At two days post- cell inoculation in mice, a single local injection of 74 and 148 MBq/kg of AIC causes complete inhibition of tumor growth.
  • Systemic injections of 111, 222 and 333 MBq/kg of AIC cause significant tumor growth delay after 16 weeks, compared with the nonspecific control providing 333 MBq/kg after 16 weeks.
  • CONCLUSIONS: CFPAC-1, PANC-1 and CAPAN-1 pancreatic cancer cell clusters and pancreatic tumor xenografts show high expression of the MUC-1 target antigen.
  • 213Bi-C595 can specifically target and regress pancreatic cancer cell clusters in vitro, and delay and inhibit tumor growth in vivo.
  • 213Bi-C595 may be a useful agent for the treatment of micrometastatic pancreatic cancer with overexpression of MUC 1 antigen in post-surgical patients with minimal residual disease.
  • [MeSH-major] Antibodies, Monoclonal / therapeutic use. Isothiocyanates / therapeutic use. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / radiotherapy. Pentetic Acid / analogs & derivatives. Radioimmunotherapy
  • [MeSH-minor] Animals. Antigens, Neoplasm. Bismuth / therapeutic use. Cell Line, Tumor. Humans. Mice. Mucin-1. Mucins / analysis. Mucins / immunology. Xenograft Model Antitumor Assays

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  • (PMID = 16082185.001).
  • [ISSN] 1538-4047
  • [Journal-full-title] Cancer biology & therapy
  • [ISO-abbreviation] Cancer Biol. Ther.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antibodies, Monoclonal; 0 / Antigens, Neoplasm; 0 / Isothiocyanates; 0 / MUC1 protein, human; 0 / Mucin-1; 0 / Mucins; 142434-84-2 / N-(2-amino-3-(4-isothiocyanatophenyl)propyl)cyclohexane-1,2-diamine-N,N',N',N'',N''-pentaacetic acid; 7A314HQM0I / Pentetic Acid; U015TT5I8H / Bismuth
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41. Wilson W 3rd, Baldwin AS: Maintenance of constitutive IkappaB kinase activity by glycogen synthase kinase-3alpha/beta in pancreatic cancer. Cancer Res; 2008 Oct 1;68(19):8156-63
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  • [Title] Maintenance of constitutive IkappaB kinase activity by glycogen synthase kinase-3alpha/beta in pancreatic cancer.
  • Constitutive nuclear factor kappaB (NF-kappaB) activation is among the many deregulated signaling pathways that are proposed to drive pancreatic cancer cell growth and survival.
  • Recent reports suggest that glycogen synthase kinase-3beta (GSK-3beta) plays a key role in maintaining basal NF-kappaB target gene expression and cell survival in pancreatic cancer cell lines.
  • However, the mechanism by which GSK-3beta facilitates constitutive NF-kappaB signaling in pancreatic cancer remains unclear.
  • In this report, we analyze the contributions of both GSK-3 isoforms (GSK-3alpha and GSK-3beta) in regulating NF-kappaB activation and cell proliferation in pancreatic cancer cell lines (Panc-1 and MiaPaCa-2).
  • We show that GSK-3 isoforms are differentially required to maintain basal NF-kappaB DNA binding activity, transcriptional activity, and cell proliferation in Panc-1 and MiaPaCa-2 cells.
  • Our data also indicate that IkappaB kinase (IKK) subunits are not equally required to regulate pancreatic cancer-associated NF-kappaB activity and cell growth.
  • Importantly, we provide the first evidence that GSK-3 maintains constitutive NF-kappaB signaling in pancreatic cancer by regulating IKK activity.
  • These data provide new insight into GSK-3-dependent NF-kappaB regulation and further establish GSK-3 and IKK as potential therapeutic targets for pancreatic cancer.

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  • (PMID = 18829575.001).
  • [ISSN] 1538-7445
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / CA075080-10; United States / NIAID NIH HHS / AI / R37 AI035098; United States / NCI NIH HHS / CA / R01 CA075080; United States / NCI NIH HHS / CA / CA73756; United States / NCI NIH HHS / CA / R01 CA073756; United States / NIAID NIH HHS / AI / AI35098; United States / NCI NIH HHS / CA / CA75080; United States / NCI NIH HHS / CA / CA073756-10; United States / NCI NIH HHS / CA / 5P50CA106991; United States / NCI NIH HHS / CA / P50 CA106991-050002; United States / NIAID NIH HHS / AI / AI035098-16; United States / NCI NIH HHS / CA / R01 CA075080-10; United States / NCI NIH HHS / CA / P50 CA106991; United States / NIAID NIH HHS / AI / R37 AI035098-16; United States / NCI NIH HHS / CA / R01 CA073756-10; United States / NCI NIH HHS / CA / CA106991-050002; United States / NIAID NIH HHS / AI / R01 AI035098
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Isoenzymes; 0 / N-(4-methoxybenzyl)-N'-(5-nitro-1,3-thiazol-2-yl)urea; 0 / NF-kappa B; 0 / Thiazoles; 8W8T17847W / Urea; EC 2.7.11.1 / glycogen synthase kinase 3 beta; EC 2.7.11.10 / I-kappa B Kinase; EC 2.7.11.26 / Glycogen Synthase Kinase 3; EC 2.7.11.26 / glycogen synthase kinase 3 alpha
  • [Other-IDs] NLM/ NIHMS93606; NLM/ PMC2647811
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42. Wang F, Li SS, Segersvärd R, Strömmer L, Sundqvist KG, Holgersson J, Permert J: Hypoxia inducible factor-1 mediates effects of insulin on pancreatic cancer cells and disturbs host energy homeostasis. Am J Pathol; 2007 Feb;170(2):469-77
MedlinePlus Health Information. consumer health - Pancreatic Cancer.

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Hypoxia inducible factor-1 mediates effects of insulin on pancreatic cancer cells and disturbs host energy homeostasis.
  • Intratumoral hypoxia and paracrine insulin stimulate the expression of hypoxia inducible factor-1alpha (HIF-1alpha) in pancreatic cancer cells.
  • In the present studies, we investigated whether insulin-induced HIF-1alpha expression is a prerequisite for insulin to induce other trophic effects in MiaPaCa2 human pancreatic cancer cells and whether inhibition of HIF-1alpha expression would decrease tumor glycolysis and improve host energy homeostasis.
  • We found that hypoxia was a prerequisite for induction of HIF-1alpha mRNA expression by insulin in MiaPaCa2 cells.
  • Under hypoxic conditions, insulin stimulated glycolysis, cell proliferation, and the secretion of vascular endothelial growth factor in regular MiaPaCa2 cells but not in a MiaPaCa2 variant (si-MiaPaCa2) that expressed specific short interfering RNA for HIF-1alpha and therefore lacked HIF-1alpha protein.
  • When si-MiaPaCa2 cells were transplanted into the pancreas of athymic mice, they were less tumorigenic and expressed less hexokinase than regular MiaPaCa2 cells.
  • Body weight gain was attenuated in mice hosting tumors composed of regular MiaPaCa2 but not si-MiaPaCa2 cells.
  • These results suggest that an interaction between insulin and HIF-1alpha helps sustain pancreatic cancer cells and disturbs host energy homeostasis.
  • [MeSH-major] Glycolysis / drug effects. Homeostasis / drug effects. Hypoglycemic Agents / pharmacology. Hypoxia-Inducible Factor 1, alpha Subunit / biosynthesis. Insulin / pharmacology. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Animals. Cell Hypoxia. Cell Line, Tumor. Cell Proliferation / drug effects. Gene Expression Regulation / drug effects. Hexokinase / biosynthesis. Humans. Mice. Mice, Nude. Neoplasm Transplantation. Vascular Endothelial Growth Factor A / biosynthesis

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  • (PMID = 17255315.001).
  • [ISSN] 0002-9440
  • [Journal-full-title] The American journal of pathology
  • [ISO-abbreviation] Am. J. Pathol.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / HIF1A protein, human; 0 / Hypoglycemic Agents; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Insulin; 0 / Vascular Endothelial Growth Factor A; EC 2.7.1.1 / Hexokinase
  • [Other-IDs] NLM/ PMC1851851
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43. Tang H, Dong X, Day RS, Hassan MM, Li D: Antioxidant genes, diabetes and dietary antioxidants in association with risk of pancreatic cancer. Carcinogenesis; 2010 Apr;31(4):607-13
The Lens. Cited by Patents in .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Antioxidant genes, diabetes and dietary antioxidants in association with risk of pancreatic cancer.
  • To test the hypothesis that polymorphic variants of antioxidant genes modify the risk of pancreatic cancer, we examined seven single-nucleotide polymorphisms (SNPs) of genes coding for superoxide dismutase (SOD) 2, glutathione S-transferase alpha 4 (GSTA4), catalase and glutathione peroxidase in 575 patients with pancreatic adenocarcinoma and 648 healthy controls in a case-control study.
  • A borderline significant interaction between diabetes and SOD2 Ex2+24T>C CT/TT genotype was observed (P(interaction) = 0.051); the AORs (95% CI) were 0.98 (0.73-1.32) for non-diabetics carrying the CT/TT genotype, 1.73 (0.94-3.18) for diabetics carrying the CC genotype and 3.49 (2.22-5.49) for diabetics carrying the CT/TT genotype compared with non-diabetics carrying the CC genotype.
  • Moreover, the SOD2 -1221G>A AA genotype carriers had a significantly increased risk for pancreatic cancer among those with a low dietary vitamin E intake but decreased risk among those with a high vitamin E intake (P(interaction) = 0.002).
  • There was a non-significant interaction between diabetes and GSTA4 Ex5-64G>A genotypes (P(interaction) = 0.078).
  • These data suggest that genetic variations in antioxidant defenses modify the risk of pancreatic cancer in diabetics or individuals with a low dietary vitamin E intake.

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  • (PMID = 20097730.001).
  • [ISSN] 1460-2180
  • [Journal-full-title] Carcinogenesis
  • [ISO-abbreviation] Carcinogenesis
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / R01 CA098380; United States / NIEHS NIH HHS / ES / P30 ES07784; United States / NCI NIH HHS / CA / R01 CA98380
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] England
  • [Chemical-registry-number] 1406-18-4 / Vitamin E; EC 1.15.1.1 / Superoxide Dismutase; EC 1.15.1.1 / superoxide dismutase 2; EC 2.5.1.18 / Glutathione Transferase; EC 4.4.1.20 / leukotriene-C4 synthase; PQ6CK8PD0R / Ascorbic Acid
  • [Other-IDs] NLM/ PMC2847085
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44. Su Y, Loos M, Giese N, Hines OJ, Diebold I, Görlach A, Metzen E, Pastorekova S, Friess H, Büchler P: PHD3 regulates differentiation, tumour growth and angiogenesis in pancreatic cancer. Br J Cancer; 2010 Nov 9;103(10):1571-9
Gene Ontology. gene/protein/disease-specific - Gene Ontology annotations from this paper .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] PHD3 regulates differentiation, tumour growth and angiogenesis in pancreatic cancer.
  • PURPOSE: Tumour hypoxia activates hypoxia-inducible factor-1 (HIF-1) and indluences angiogenesis, cell survival and invasion.
  • The effects of PHD3 in tumour growth are largely unknown.
  • EXPERIMENTAL DESIGN: PHD3 expression was analysed in human pancreatic cancer tissues and cancer cell lines by real-time quantitative PCR and immunohistochemistry.
  • Matrigel invasion assays were performed to examine tumour cell invasion.
  • The effect of PHD3 on tumour growth in vivo was evaluated in an established orthotopic murine model.
  • RESULTS: PHD3 was upregulated in well-differentiated human tumours and cell lines, and regulated hypoxic VEGF secretion.
  • PHD3 overexpression mediated tumour cell growth and invasion by induction of apoptosis in a nerve growth factor-dependent manner by the activation of caspase-3 and phosphorylation of focal adhesion kinase HIF-1 independently.
  • In vivo, PHD3 inhibited tumour growth by abrogation of tumour angiogenesis.
  • CONCLUSION: Our results indicate essential functions of PHD3 in tumour growth, apoptosis and angiogenesis and through HIF-1-dependent and HIF-1-independent pathways.
  • [MeSH-major] Dioxygenases / genetics. Neovascularization, Pathologic / pathology. Pancreatic Neoplasms / pathology
  • [MeSH-minor] Adenocarcinoma / pathology. Adenocarcinoma / surgery. Animals. Annexin A5 / analysis. Apoptosis. Carcinoma, Pancreatic Ductal / enzymology. Carcinoma, Pancreatic Ductal / pathology. Carcinoma, Pancreatic Ductal / surgery. Caspase 3 / metabolism. Cell Differentiation. Cell Line, Tumor. Enzyme-Linked Immunosorbent Assay. Humans. Hypoxia-Inducible Factor 1, alpha Subunit / genetics. Hypoxia-Inducible Factor 1, alpha Subunit / physiology. Hypoxia-Inducible Factor-Proline Dioxygenases. Mice. Neoplasm Invasiveness / genetics. Neoplasm Invasiveness / pathology. Polymerase Chain Reaction. RNA, Messenger / genetics. RNA, Neoplasm / genetics. Reverse Transcriptase Polymerase Chain Reaction. Transplantation, Heterologous. Up-Regulation. Vascular Endothelial Growth Factor A / analysis

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  • (PMID = 20978507.001).
  • [ISSN] 1532-1827
  • [Journal-full-title] British journal of cancer
  • [ISO-abbreviation] Br. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Annexin A5; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / RNA, Messenger; 0 / RNA, Neoplasm; 0 / Vascular Endothelial Growth Factor A; EC 1.13.11.- / Dioxygenases; EC 1.14.11.29 / EGLN3 protein, human; EC 1.14.11.29 / Hypoxia-Inducible Factor-Proline Dioxygenases; EC 3.4.22.- / Caspase 3
  • [Other-IDs] NLM/ PMC2990580
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45. Kondo H, Hazama S, Kawaoka T, Yoshino S, Yoshida S, Tokuno K, Takashima M, Ueno T, Hinoda Y, Oka M: Adoptive immunotherapy for pancreatic cancer using MUC1 peptide-pulsed dendritic cells and activated T lymphocytes. Anticancer Res; 2008 Jan-Feb;28(1B):379-87
The Lens. Cited by Patents in .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Adoptive immunotherapy for pancreatic cancer using MUC1 peptide-pulsed dendritic cells and activated T lymphocytes.
  • BACKGROUND: Pancreatic cancer has a poor prognosis.
  • The clinical efficacy of immunotherapy using both dendritic cells pulsed with MUC1 peptide (MUC1-DC) and, cytotoxic T lymphocyte (CTL) sensitized with a pancreatic cancer, YPK-1, expressing MUC1 (MUC1-CTL) was evaluated.
  • PATIENTS AND METHODS: Twenty patients with unresectable or recurrent pancreatic cancer were enrolled.
  • Peripheral blood mononuclear cells (PBMCs) were separated into adherent cells for induction of MUC1-DCs and floating cells for MUC1-CTLs.
  • MUC1-DCs were generated by culture with granulocyte monocyte colony stimulating factor (GM-CSF) and interleukin-4 (IL-4) and then exposed to MUC1 peptide and TNF-alpha.
  • Five patients had stable disease.
  • CONCLUSION: Adoptive immunotherapy with MUC1-DC and MUC1-CTL may be feasible and effective for pancreatic cancer.
  • [MeSH-major] Carcinoma, Pancreatic Ductal / therapy. Dendritic Cells / immunology. Immunotherapy, Adoptive / methods. Mucin-1 / immunology. Pancreatic Neoplasms / therapy. T-Lymphocytes, Cytotoxic / immunology
  • [MeSH-minor] Aged. Aged, 80 and over. Cell Line, Tumor. Female. Humans. Lymphocyte Activation. Male. Middle Aged


46. Mori-Iwamoto S, Kuramitsu Y, Ryozawa S, Mikuria K, Fujimoto M, Maehara S, Maehara Y, Okita K, Nakamura K, Sakaida I: Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine. Int J Oncol; 2007 Dec;31(6):1345-50
NCI CPTC Antibody Characterization Program. NCI CPTC Antibody Characterization Program .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine.
  • Pancreatic cancer remains a devastating disease and >96% of patients with pancreatic cancer do not survive for more than 5 years.
  • Gemcitabine (2'-deoxy-2'-difluoro-deoxycytidine: Gemzar) appears to be the only clinically effective drug for pancreatic cancer, but it has little impact on outcome.
  • Proteomic analysis of gemcitabine-sensitive cells (KLM1) and resistant pancreatic cells (KLM1-R) was performed to identify target proteins of the gemcitabine.
  • We found seven proteins, HSP27, peroxiredoxin 2, endoplasmic reticulum protein ERp29 precursor, 6-phosphogluconolactonase, triosphospate isomerase, alpha enolase, and nucleophosmine that could play a role in determining the sensitivity of pancreatic cancer to gemcitabine.
  • In addition, increased HSP27 expression in tumor specimens was related to higher resistibility to gemcitabine in patients of pancreatic cancer.
  • HSP27 may play an important role in the resistibility to gemcitabine, and it could also be a possible biomarker for predicting the response of pancreatic cancer patients to treatment with gemcitabine.
  • [MeSH-major] Antimetabolites, Antineoplastic / pharmacology. Biomarkers, Tumor / analysis. Deoxycytidine / analogs & derivatives. Heat-Shock Proteins / analysis. Neoplasm Proteins / analysis. Pancreatic Neoplasms / drug therapy. Proteomics
  • [MeSH-minor] Biopsy, Needle. Blotting, Western. Cell Line, Tumor. Drug Resistance, Neoplasm. HSP27 Heat-Shock Proteins. Humans. Immunohistochemistry

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  • (PMID = 17982661.001).
  • [ISSN] 1019-6439
  • [Journal-full-title] International journal of oncology
  • [ISO-abbreviation] Int. J. Oncol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Greece
  • [Chemical-registry-number] 0 / Antimetabolites, Antineoplastic; 0 / Biomarkers, Tumor; 0 / HSP27 Heat-Shock Proteins; 0 / HSPB1 protein, human; 0 / Heat-Shock Proteins; 0 / Neoplasm Proteins; 0W860991D6 / Deoxycytidine; B76N6SBZ8R / gemcitabine
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47. Beilke S, Oswald F, Genze F, Wirth T, Adler G, Wagner M: The zinc-finger protein KCMF1 is overexpressed during pancreatic cancer development and downregulation of KCMF1 inhibits pancreatic cancer development in mice. Oncogene; 2010 Jul 15;29(28):4058-67
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] The zinc-finger protein KCMF1 is overexpressed during pancreatic cancer development and downregulation of KCMF1 inhibits pancreatic cancer development in mice.
  • Potassium channel modulatory factor 1 (KCMF1) was found upregulated in a differential screen in the metaplastic epithelium in the pancreas of transforming growth factor (TGF)-alpha transgenic mice.
  • Expression analysis indicated broad overexpression in human cancer tissues.
  • Therefore, we investigated the hypothesis that KCMF1 promotes metaplastic changes and tumor development.
  • Upregulation of nuclear KCMF1 expression is evident in preneoplastic lesions and in several epithelial malignancies, such as pancreatic cancer in mice and humans.
  • In cell culture and in the chicken chorioallantoic membrane model, KCMF1 enhances proliferation, migration and invasion of HEK-293 and Panc1 cells.
  • In crossbreeding experiments, KCMF1-knockdown gene trap mice showed a reduced number and size of premalignant lesions and absence of pancreatic cancer formation in TGF-alpha transgenic mice.
  • This effect is related to the decreased expression of G1 to S cell-cycle regulators such as cyclin D and cyclin-dependent kinase (CDK) 4.
  • Our data support the hypothesis that KCMF1 mediates pro-oncogenic functions in vitro and in vivo and downregulation of KCMF1 results in the inhibition of pancreatic cancer formation in mice.
  • These effects are mediated through downregulation of cell-cycle control genes such as cyclin D and CDK4.
  • [MeSH-major] Down-Regulation. Pancreatic Neoplasms / genetics. Ubiquitin-Protein Ligases / genetics
  • [MeSH-minor] Animals. Base Sequence. Cell Line. DNA Primers. Humans. Mice. Mice, Transgenic


48. Ide T, Kitajima Y, Miyoshi A, Ohtsuka T, Mitsuno M, Ohtaka K, Koga Y, Miyazaki K: Tumor-stromal cell interaction under hypoxia increases the invasiveness of pancreatic cancer cells through the hepatocyte growth factor/c-Met pathway. Int J Cancer; 2006 Dec 15;119(12):2750-9
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  • [Title] Tumor-stromal cell interaction under hypoxia increases the invasiveness of pancreatic cancer cells through the hepatocyte growth factor/c-Met pathway.
  • The hypoxic environment in tumor is reported to play an important role in pancreatic cancer progression.
  • The interaction between stromal and cancer cells also contributes to the malignant behavior of pancreatic cancer.
  • In the present study, we investigated whether hypoxic stimulation affects stromal as well as pancreatic cancer cells.
  • Our findings demonstrated that hypoxia remarkably elevated the HIF-1alpha expression in both pancreatic cancer (PK8) and fibroblast cells (MRC5).
  • Hypoxic stimulation accelerated the invasive activity of PK8 cells, and invasiveness was thus further accelerated when the hypoxic PK8 cells were cultured with conditioned medium prepared from hypoxic MRC5 cells (hypoxic conditioned medium).
  • MMP-2, MMP-7, MT1-MMP and c-Met expressions were increased in PK8 cells under hypoxia.
  • Hypoxic stimulation also increased the hepatocyte growth factor (HGF) secretion from MRC5 cells, which led to an elevation of c-Met phosphorylation in PK8 cells.
  • Conversely, the elevated cancer invasion, MMP activity and c-Met phosphorylation of PK8 cells were reduced by the removal of HGF from hypoxic conditioned medium.
  • In immunohistochemical study, the HIF-1alpha expression was observed in surrounding stromal as well as pancreatic cancer cells, thus indicating hypoxia exists in both of cancer and stromal cells.
  • Moreover, the stromal HGF expression was found to significantly correlate with not only the stromal HIF-1alpha expression but also the c-Met expression in cancer cells.
  • These results indicate that the hypoxic environment within stromal as well as cancer cells activates the HGF/c-Met system, thereby contributing to the aggressive invasive features of pancreatic cancer.
  • [MeSH-major] Cell Communication / physiology. Hepatocyte Growth Factor / genetics. Proto-Oncogene Proteins c-met / genetics. Stromal Cells / metabolism
  • [MeSH-minor] Blotting, Western. Cell Hypoxia / physiology. Cell Line, Tumor. Cell Movement / drug effects. Cell Movement / physiology. Cell Proliferation / drug effects. Culture Media, Conditioned / pharmacology. Fibroblasts / cytology. Fibroblasts / drug effects. Fibroblasts / metabolism. Humans. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Matrix Metalloproteinase 2 / genetics. Matrix Metalloproteinase 2 / metabolism. Matrix Metalloproteinases / genetics. Matrix Metalloproteinases / metabolism. Neoplasm Invasiveness. Pancreatic Neoplasms / genetics. Pancreatic Neoplasms / metabolism. Pancreatic Neoplasms / pathology. RNA, Messenger / genetics. RNA, Messenger / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Signal Transduction / drug effects. Signal Transduction / physiology. Time Factors. Tissue Inhibitor of Metalloproteinases / genetics. Tissue Inhibitor of Metalloproteinases / metabolism

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  • [Copyright] Copyright 2006 Wiley-Liss, Inc.
  • (PMID = 16998831.001).
  • [ISSN] 0020-7136
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Culture Media, Conditioned; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / RNA, Messenger; 0 / Tissue Inhibitor of Metalloproteinases; 67256-21-7 / Hepatocyte Growth Factor; EC 2.7.10.1 / Proto-Oncogene Proteins c-met; EC 3.4.24.- / Matrix Metalloproteinases; EC 3.4.24.24 / Matrix Metalloproteinase 2
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49. Jutooru I, Chadalapaka G, Lei P, Safe S: Inhibition of NFkappaB and pancreatic cancer cell and tumor growth by curcumin is dependent on specificity protein down-regulation. J Biol Chem; 2010 Aug 13;285(33):25332-44
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  • [Title] Inhibition of NFkappaB and pancreatic cancer cell and tumor growth by curcumin is dependent on specificity protein down-regulation.
  • Curcumin activates diverse anticancer activities that lead to inhibition of cancer cell and tumor growth, induction of apoptosis, and antiangiogenic responses.
  • In this study, we observed that curcumin inhibits Panc28 and L3.6pL pancreatic cancer cell and tumor growth in nude mice bearing L3.6pL cells as xenografts.
  • In addition, curcumin decreased expression of p50 and p65 proteins and NFkappaB-dependent transactivation and also decreased Sp1, Sp3, and Sp4 transcription factors that are overexpressed in pancreatic cancer cells.
  • Because both Sp transcription factors and NFkappaB regulate several common genes such as cyclin D1, survivin, and vascular endothelial growth factor that contribute to the cancer phenotype, we also investigated interactions between Sp and NFkappaB transcription factors.
  • Results of Sp1, Sp3, and Sp4 knockdown by RNA interference demonstrate that both p50 and p65 are Sp-regulated genes and that inhibition of constitutive or tumor necrosis factor-induced NFkappaB by curcumin is dependent on down-regulation of Sp1, Sp3, and Sp4 proteins by this compound.
  • Curcumin also decreased mitochondrial membrane potential and induced reactive oxygen species in pancreatic cancer cells, and this pathway is required for down-regulation of Sp proteins in these cells, demonstrating that the mitochondriotoxic effects of curcumin are important for its anticancer activities.

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  • (PMID = 20538607.001).
  • [ISSN] 1083-351X
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / R01 CA108718; United States / NCI NIH HHS / CA / R01 CA136571; United States / NCI NIH HHS / CA / R01CA108718; United States / NCI NIH HHS / CA / R01CA136571
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / NF-kappa B; 0 / RNA, Small Interfering; 0 / Reactive Oxygen Species; 0 / Sp Transcription Factors; 0 / Sp1 Transcription Factor; 0 / Sp4 Transcription Factor; 0 / Tumor Necrosis Factor-alpha; 0 / Vascular Endothelial Growth Factor A; 136601-57-5 / Cyclin D1; 148710-94-5 / Sp3 Transcription Factor; BBX060AN9V / Hydrogen Peroxide; EC 2.7.10.1 / Vascular Endothelial Growth Factor Receptor-1; IT942ZTH98 / Curcumin
  • [Other-IDs] NLM/ PMC2919096
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50. Lang SA, Moser C, Gaumann A, Klein D, Glockzin G, Popp FC, Dahlke MH, Piso P, Schlitt HJ, Geissler EK, Stoeltzing O: Targeting heat shock protein 90 in pancreatic cancer impairs insulin-like growth factor-I receptor signaling, disrupts an interleukin-6/signal-transducer and activator of transcription 3/hypoxia-inducible factor-1alpha autocrine loop, and reduces orthotopic tumor growth. Clin Cancer Res; 2007 Nov 1;13(21):6459-68
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Targeting heat shock protein 90 in pancreatic cancer impairs insulin-like growth factor-I receptor signaling, disrupts an interleukin-6/signal-transducer and activator of transcription 3/hypoxia-inducible factor-1alpha autocrine loop, and reduces orthotopic tumor growth.
  • Because insulin-like growth factor-I receptor (IGF-IR) and signal transducer and activator of transcription 3 (STAT3) signaling pathways are implicated in the progression of pancreatic cancer, we hypothesized that blocking Hsp90 with geldanamycin derivates [17-allylamino-geldanamycin (17-AAG), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG)] would impair IGF-I- and interleukin-6-mediated signaling and thus reduce pancreatic tumor growth and angiogenesis in vivo.
  • EXPERIMENTAL DESIGN: Human pancreatic cancer cells (HPAF-II, L3.6pl) were used for experiments.
  • Effects of 17-DMAG (25 mg/kg; thrice a week; i.p.) on tumor growth and vascularization were investigated in a s.c. xenograft model and in an orthotopic model of pancreatic cancer.
  • In vivo, 17-DMAG significantly reduced s.c. tumor growth and diminished STAT3 phosphorylation and IGF-IRbeta expression in tumor tissues.
  • In an orthotopic model, pancreatic tumor growth and vascularization were both significantly reduced upon Hsp90 inhibition, as reflected by final tumor weights and CD31 staining, respectively.
  • CONCLUSIONS: Blocking Hsp90 disrupts IGF-I and IL-6-induced proangiogenic signaling cascades by targeting IGF-IR and STAT3 in pancreatic cancer, leading to significant growth-inhibitory effects.
  • Therefore, we suggest that Hsp90 inhibitors could prove to be valuable in the treatment of pancreatic cancer.
  • [MeSH-major] Gene Expression Regulation, Neoplastic. HSP90 Heat-Shock Proteins / metabolism. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Interleukin-6 / metabolism. Pancreatic Neoplasms / metabolism. Pancreatic Neoplasms / pathology. Receptor, IGF Type 1 / metabolism. STAT3 Transcription Factor / metabolism. Signal Transduction
  • [MeSH-minor] Animals. Benzoquinones / pharmacology. Cell Line, Tumor. Gene Expression Profiling. Humans. Lactams, Macrocyclic / pharmacology. Mice. Mice, Nude. Neoplasm Transplantation. Neovascularization, Pathologic

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  • (PMID = 17975158.001).
  • [ISSN] 1078-0432
  • [Journal-full-title] Clinical cancer research : an official journal of the American Association for Cancer Research
  • [ISO-abbreviation] Clin. Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Benzoquinones; 0 / HSP90 Heat-Shock Proteins; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Interleukin-6; 0 / Lactams, Macrocyclic; 0 / STAT3 Transcription Factor; 001L2FE0M3 / 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin; 4GY0AVT3L4 / tanespimycin; EC 2.7.10.1 / Receptor, IGF Type 1
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51. Okuyama N, Ide Y, Nakano M, Nakagawa T, Yamanaka K, Moriwaki K, Murata K, Ohigashi H, Yokoyama S, Eguchi H, Ishikawa O, Ito T, Kato M, Kasahara A, Kawano S, Gu J, Taniguchi N, Miyoshi E: Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation. Int J Cancer; 2006 Jun 1;118(11):2803-8
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation.
  • Changes in oligosaccharide structures have been reported in certain types of malignant transformations and, thus, could be used for tumor markers in certain types of cancer.
  • In the case of pancreatic cancer cell lines, a variety of fucosylated proteins are secreted into their conditioned media.
  • To identify fucosylated proteins in the serum of patients with pancreatic cancer, we performed western blot analyses using Aleuria Aurantica Lectin (AAL), which is specific for fucosylated structures.
  • An approximately 40 kD protein was found to be highly fucosylated in pancreatic cancer and an N-terminal analysis revealed that it was the beta chain of haptoglobin.
  • While the appearance of fucosylated haptoglobin has been reported in other diseases such as hepatocellular carcinoma, liver cirrhosis, gastric cancer and colon cancer, the incidence was significantly higher in the case of pancreatic cancer.
  • Fucosylated haptoglobin was observed more frequently at the advanced stage of pancreatic cancer and disappeared after an operation.
  • A mass spectrometry analysis of haptoglobin purified from the serum of patients with pancreatic cancer and the medium from a pancreatic cancer cell line, PSN-1, showed that the alpha 1-3/alpha 1-4/alpha 1-6 fucosylation of haptoglobin was increased in pancreatic cancer.
  • When a hepatoma cell line, Hep3B, was cultured with the conditioned media from pancreatic cancer cells, haptoglobin secretion was dramatically increased.
  • These findings suggest that fucosylated haptoglobin could serve as a novel marker for pancreatic cancer.
  • One is that pancreatic cancer cells, themselves, produce fucosylated haptoglobin; the other is that pancreatic cancer produces a factor, which induces the production of fucosylated haptoglobin in the liver.
  • [MeSH-major] Biomarkers, Tumor / analysis. Globins / analysis. Globins / metabolism. Pancreatic Neoplasms / diagnosis. Pancreatic Neoplasms / pathology
  • [MeSH-minor] Blotting, Western. Female. Humans. Male. Mass Spectrometry. Middle Aged. Molecular Structure. Oligosaccharides / chemistry

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  • (PMID = 16385567.001).
  • [ISSN] 0020-7136
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Biomarkers, Tumor; 0 / Oligosaccharides; 0 / hepatoglobin; 9004-22-2 / Globins
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52. Murugesan SR, King CR, Osborn R, Fairweather WR, O'Reilly EM, Thornton MO, Wei LL: Combination of human tumor necrosis factor-alpha (hTNF-alpha) gene delivery with gemcitabine is effective in models of pancreatic cancer. Cancer Gene Ther; 2009 Nov;16(11):841-7
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  • [Title] Combination of human tumor necrosis factor-alpha (hTNF-alpha) gene delivery with gemcitabine is effective in models of pancreatic cancer.
  • Pancreatic adenocarcinoma is an aggressive and highly lethal malignancy.
  • Currently, gemcitabine is commonly used in patients with pancreatic cancer.
  • However, the life expectancy of pancreatic cancer patients remains poor.
  • We explored the possibility of increased anti-tumor activity by combining human tumor necrosis factor-alpha (hTNF-alpha) with current front-line therapy.
  • Human TNF-alpha displays potent anti-tumor activity, but its use is limited by the toxicity of systemic administration.
  • We developed a gene delivery approach using intratumoral injections of an adenoviral vector expressing hTNF-alpha, AdEgr.TNF.11D (TNFerade), to increase local concentrations of hTNF-alpha within the tumor, thereby maximizing local anti-tumor activity and yet minimizing the systemic toxicities.
  • An ongoing phase III clinical trial is testing the efficacy of AdEgr.TNF.11D-injected intratumorally and combining with chemotherapy in locally advanced pancreatic cancer.
  • In this study, we show that treatment with AdEgr.TNF.11D and gemcitabine results in a high level of hTNF-alpha expression in human pancreatic cancer cell lines.
  • The combined treatment was well tolerated, highly active and produced marked delays in the growth of human pancreatic xenograft tumors relative to either agent alone.
  • Our results strongly suggest that combination of AdEgr.TNF.11D and gemcitabine may be a potentially useful therapeutic approach for the improved treatment of pancreatic cancer.
  • [MeSH-major] Antineoplastic Agents / therapeutic use. Deoxycytidine / analogs & derivatives. Genetic Therapy / methods. Pancreatic Neoplasms / therapy. Tumor Necrosis Factor-alpha / metabolism
  • [MeSH-minor] Adenoviridae / genetics. Animals. Cell Line, Tumor. Combined Modality Therapy. Female. Genetic Vectors / genetics. Humans. Mice. Mice, Inbred BALB C. Mice, Nude. Xenograft Model Antitumor Assays


53. Nagaraj S, Ziske C, Strehl J, Messmer D, Sauerbruch T, Schmidt-Wolf IG: Dendritic cells pulsed with alpha-galactosylceramide induce anti-tumor immunity against pancreatic cancer in vivo. Int Immunol; 2006 Aug;18(8):1279-83
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Dendritic cells pulsed with alpha-galactosylceramide induce anti-tumor immunity against pancreatic cancer in vivo.
  • Ductal pancreatic adenocarcinoma is the fourth leading cause of cancer death in the Western world.
  • Thus, new approaches are necessary to improve the outcome of patients with exocrine pancreatic cancer.
  • In the present study, we tried to enhance the anti-tumor effect against pancreatic carcinoma by supplementary triggering of NKT cells in vivo.
  • We challenged Panc02 tumor-bearing mice by intratumoral vaccination with alpha-galactosylceramide (alpha-GalCer)-loaded dendritic cells (DCs).
  • A significant expansion of IFNgamma-producing NKT cells was observed which also correlated with decrease in tumor growth in vivo.
  • Hence, DCs loaded with alpha-GalCer could lead to a novel treatment option for patients with pancreatic cancer.
  • [MeSH-major] Cancer Vaccines / immunology. Carcinoma, Pancreatic Ductal / therapy. Dendritic Cells / immunology. Galactosylceramides / pharmacology. Immunotherapy, Adoptive / methods. Pancreatic Neoplasms / therapy
  • [MeSH-minor] Animals. Cell Line, Tumor. Interferon-gamma / biosynthesis. Interferon-gamma / immunology. Killer Cells, Natural / immunology. Major Histocompatibility Complex / immunology. Male. Mice. Mice, Inbred C57BL. Spleen / cytology. Spleen / immunology

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  • (PMID = 16772371.001).
  • [ISSN] 0953-8178
  • [Journal-full-title] International immunology
  • [ISO-abbreviation] Int. Immunol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Cancer Vaccines; 0 / Galactosylceramides; 0 / alpha-galactosylceramide; 82115-62-6 / Interferon-gamma
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54. Mori A, Moser C, Lang SA, Hackl C, Gottfried E, Kreutz M, Schlitt HJ, Geissler EK, Stoeltzing O: Up-regulation of Krüppel-like factor 5 in pancreatic cancer is promoted by interleukin-1beta signaling and hypoxia-inducible factor-1alpha. Mol Cancer Res; 2009 Aug;7(8):1390-8
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  • [Title] Up-regulation of Krüppel-like factor 5 in pancreatic cancer is promoted by interleukin-1beta signaling and hypoxia-inducible factor-1alpha.
  • Krüppel-like factor 5 (KLF5) is a transcription factor involved in cell transformation, proliferation, and carcinogenesis that can be up-regulated by RAS mutations.
  • However, controversy persists as to whether it functions as a tumor suppressor or as an oncogene.
  • Because KRAS is frequently mutated in pancreatic cancer, we investigated the regulation of KLF5 in this cancer entity.
  • Our results show that KLF5 is overexpressed in pancreatic cancer cells and exceeds KLF5 expression of KRAS-mutated colon cancer cells.
  • Surprisingly, inhibition of B-Raf/C-Raf or MAPK/Erk did not reduce KLF5 levels, suggesting that KLF5 expression is not promoted by KRAS-Raf-MEK-Erk signaling in pancreatic cancer.
  • This finding is in striking contrast to reports on MEK-Erk-mediated KLF5 induction in colon cancer cells.
  • Moreover, KLF5 expression levels neither correlated with the mutational status of KRAS nor with MEK phosphorylation in pancreatic cancer cells.
  • Furthermore, KLF5 expression was significantly elevated by high cell density, by anchorage-independent cell growth, and in tumor spheroids.
  • In conclusion, overexpression of KLF5 in human pancreatic cancer cells is not mediated by KRAS/Raf/MAPK/Erk signaling, but involves the IL-1beta/IL-1R system, p38, and the transcription factor HIF-1alpha.
  • [MeSH-major] Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Interleukin-1beta / metabolism. Kruppel-Like Transcription Factors / genetics. Pancreatic Neoplasms / genetics. Signal Transduction. Up-Regulation / genetics
  • [MeSH-minor] Cell Count. Cell Hypoxia / drug effects. Cell Proliferation / drug effects. Gene Expression Regulation, Neoplastic / drug effects. Gene Knockdown Techniques. Humans. Spheroids, Cellular / drug effects. Spheroids, Cellular / metabolism. Tumor Cells, Cultured


55. Ryschich E, Jesnowski R, Ringel J, Harms W, Fabian OV, Saller R, Schrewe M, Engel A, Schmidt J, Löhr M: Combined therapy of experimental pancreatic cancer with CYP2B1 producing cells: low-dose ifosfamide and local tumor irradiation. Int J Cancer; 2005 Feb 10;113(4):649-53
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  • [Title] Combined therapy of experimental pancreatic cancer with CYP2B1 producing cells: low-dose ifosfamide and local tumor irradiation.
  • Local therapy of pancreatic cancer with microencapsulated CYP2B1-producing cells and ifosfamide showed an effect both on the primary tumor and on distant metastatases.
  • Other studies have demonstrated that local tumor irradiation leads to the activation of the intratumoral lymphocyte infiltration.
  • The aim of our study was to investigate the efficacy of the combined therapy with low-dose irradiation, ifosfamide and CYP2B1-producing cells.
  • Syngenic pancreatic cancer was induced in 38 Lewis-rats by subcutaneous inoculation of 1 x 10(6) (DSL6A) tumor cells.
  • Microencapsulated CYP2B1-producing cells were injected peritumorally 10--12 weeks after tumor implantation.
  • The tumor growth was monitored for 3 weeks.
  • The tumor infiltration with CD4+, CD8+, NK-cells, microvessel density and proliferation rates were investigated by immunohistochemistry.
  • Cytokine plasma level for TNF-alpha were measured by ELISA.
  • The mean tumor volume was significantly reduced after combined ifosfamide plus radiation therapy in the first week, whereas monotherapy with ifosfamide or radiation significantly decreased tumor growth earliest after 2 and 3 weeks, respectively.
  • The high plasma level of TNF-alpha in the control group was significantly reduced after combined ifosfamide/irradiation treatment.
  • The lymphocyte infiltration and tumor proliferation were not significantly different between the groups.
  • The combination of ifosfamide/CYP2B1-producing cells and irradiation showed an earlier therapeutical effect on the growth of rat pancreatic cancer than the irradiation or ifosfamide alone.
  • There was no evidence of late activation of lymphocyte infiltration and PCNA-positive tumor cells.
  • [MeSH-major] Antineoplastic Agents, Alkylating / therapeutic use. Cytochrome P-450 CYP2B1 / physiology. Ifosfamide / therapeutic use. Pancreatic Neoplasms / therapy
  • [MeSH-minor] Animals. Cell Proliferation / drug effects. Cell Proliferation / radiation effects. Combined Modality Therapy. Dose-Response Relationship, Drug. Drug Compounding. Lymphocytes / drug effects. Lymphocytes / radiation effects. Male. Microcirculation. Proliferating Cell Nuclear Antigen / metabolism. Radiation Dosage. Rats. Rats, Inbred Lew. Tumor Cells, Cultured. Tumor Necrosis Factor-alpha / metabolism

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  • (PMID = 15455374.001).
  • [ISSN] 0020-7136
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antineoplastic Agents, Alkylating; 0 / Proliferating Cell Nuclear Antigen; 0 / Tumor Necrosis Factor-alpha; EC 1.14.14.1 / Cytochrome P-450 CYP2B1; UM20QQM95Y / Ifosfamide
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56. Mori T, Doi R, Toyoda E, Koizumi M, Ito D, Kami K, Kida A, Masui T, Kawaguchi Y, Fujimoto K: Regulation of the resistance to TRAIL-induced apoptosis as a new strategy for pancreatic cancer. Surgery; 2005 Jul;138(1):71-7
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  • [Title] Regulation of the resistance to TRAIL-induced apoptosis as a new strategy for pancreatic cancer.
  • BACKGROUND: Tumor necrosis factor-related, apoptosis-inducing ligand (TRAIL) is a potent inducer of apoptosis in a wide variety of tumor cells, but it does not cause toxicity in the majority of normal cells.
  • However, a number of tumor cell lines are known to be resistant to TRAIL-induced apoptosis.
  • The purpose of this study was to determine the mechanisms of resistance to TRAIL in pancreatic cancer cells.
  • METHODS: In human pancreatic cancer cell lines, the sensitivity to TRAIL-induced apoptosis was tested.
  • In the TRAIL-resistant pancreatic cancer cells, effects of cycloheximide, a protein synthesis inhibitor, on death signal-transducing proteins were tested.
  • RESULTS: Pancreatic cancer cells responded to TRAIL in a different way.
  • Resistant cell lines, AsPC-1, Suit-2, and CFPAC-1, expressed higher levels of FLIP-S protein, one of the splice variants of FLIP.
  • Cycloheximide reduced the expression of FLIP in the resistant cells.
  • Combined treatment with cycloheximide and TRAIL induced cleaved forms of caspases and simultaneously restored the sensitivity to TRAIL-induced apoptosis in the resistant cells.
  • CONCLUSIONS: Pancreatic cancer cells are resistant to TRAIL-induced apoptosis via strong expression of the anti-apoptotic protein FLIP-S.
  • Suppression of FLIP-S by cycloheximide restored sensitivity to TRAIL-induced apoptosis in resistant cancer cells.
  • These findings may provide useful information for the development of TRAIL-based therapeutic strategies aimed at restoring the functionality of apoptotic pathways in pancreatic cancer cells.
  • [MeSH-major] Apoptosis / drug effects. Membrane Glycoproteins / pharmacology. Pancreatic Neoplasms / drug therapy. Tumor Necrosis Factor-alpha / pharmacology
  • [MeSH-minor] Apoptosis Regulatory Proteins. Caspases / metabolism. Cell Line, Tumor. Cycloheximide / pharmacology. Drug Resistance, Neoplasm. Gene Expression / drug effects. Humans. Protein Synthesis Inhibitors / pharmacology. Receptors, TNF-Related Apoptosis-Inducing Ligand. Receptors, Tumor Necrosis Factor / genetics. Signal Transduction / drug effects. TNF-Related Apoptosis-Inducing Ligand

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  • (PMID = 16003319.001).
  • [ISSN] 0039-6060
  • [Journal-full-title] Surgery
  • [ISO-abbreviation] Surgery
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Apoptosis Regulatory Proteins; 0 / Membrane Glycoproteins; 0 / Protein Synthesis Inhibitors; 0 / Receptors, TNF-Related Apoptosis-Inducing Ligand; 0 / Receptors, Tumor Necrosis Factor; 0 / TNF-Related Apoptosis-Inducing Ligand; 0 / TNFRSF10A protein, human; 0 / TNFRSF10B protein, human; 0 / TNFSF10 protein, human; 0 / Tumor Necrosis Factor-alpha; 98600C0908 / Cycloheximide; EC 3.4.22.- / Caspases
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57. Chow JY, Dong H, Quach KT, Van Nguyen PN, Chen K, Carethers JM: TGF-beta mediates PTEN suppression and cell motility through calcium-dependent PKC-alpha activation in pancreatic cancer cells. Am J Physiol Gastrointest Liver Physiol; 2008 Apr;294(4):G899-905
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  • [Title] TGF-beta mediates PTEN suppression and cell motility through calcium-dependent PKC-alpha activation in pancreatic cancer cells.
  • Transforming growth factor-beta (TGF-beta) suppresses growth via the TGF-beta-SMAD pathway but promotes growth in cancer cells with disrupted SMAD signaling and corresponds to an invasive phenotype.
  • TGF-beta also downregulates the tumor suppressor PTEN that is rarely mutated in sporadic pancreatic cancer; this downregulation may mediate cell proliferation and invasiveness, but the mechanism is unknown.
  • We have previously demonstrated that SMAD4-null BxPc-3 pancreatic cancer cells treated with TGF-beta1 (10 ng/ml) suppressed PTEN expression and increased cell proliferation.
  • TGF-beta-treated cells were examined for PKC activation and its coupling to PTEN expression, utilizing pharmacological and knockdown methods.
  • Calcium mobilization and cell migration were also examined.
  • In BxPc-3 cells, only two PKC isoforms were activated by TGF-beta, and PTEN downregulation by TGF-beta was specifically mediated by PKC-alpha.
  • In parallel, TGF-beta rapidly induced an increase in cytoplasmic free calcium from intracellular stores, consistent with subsequent PKC-alpha activation.
  • The TGF-beta-induced increase in cell migration was blocked by knockdown of PKC-alpha.
  • Thus calcium-dependent PKC-alpha mediates TGF-beta-induced transcriptional downregulation of PTEN, and this pathway promotes cell migration in a SMAD4-null environment.
  • The TGF-beta-PKC-alpha-PTEN cascade may be a key pathway for pancreatic cancer cells to proliferate and metastasize.

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  • (PMID = 18239055.001).
  • [ISSN] 0193-1857
  • [Journal-full-title] American journal of physiology. Gastrointestinal and liver physiology
  • [ISO-abbreviation] Am. J. Physiol. Gastrointest. Liver Physiol.
  • [Language] ENG
  • [Grant] United States / NIDDK NIH HHS / DK / R01 DK067287; United States / NIDDK NIH HHS / DK / K01-DK-073090; United States / NIDDK NIH HHS / DK / R01 DK067287-02; United States / NIDDK NIH HHS / DK / DK-067287; United States / NIDDK NIH HHS / DK / R24 DK080506; United States / NIDDK NIH HHS / DK / DK067287-02; United States / NIDDK NIH HHS / DK / K01 DK073090; None / None / / K01 DK073090-01A1; United States / NIDDK NIH HHS / DK / DK080506-02; United States / NIDDK NIH HHS / DK / K01 DK073090-01A1; United States / NIDDK NIH HHS / DK / R24 DK080506-02; United States / NIDDK NIH HHS / DK / DK-080506
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Carbazoles; 0 / Chelating Agents; 0 / Indoles; 0 / Isoenzymes; 0 / Protein Kinase Inhibitors; 0 / RNA, Small Interfering; 0 / SMAD4 protein, human; 0 / Smad4 Protein; 0 / Transforming Growth Factor beta1; 136194-77-9 / Go 6976; 139890-68-9 / 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester; 526U7A2651 / Egtazic Acid; EC 2.7.11.13 / Protein Kinase C; EC 2.7.11.13 / Protein Kinase C-alpha; EC 2.7.11.13 / protein kinase C lambda; EC 3.1.3.48 / PTEN protein, human; EC 3.1.3.67 / PTEN Phosphohydrolase; SY7Q814VUP / Calcium
  • [Other-IDs] NLM/ NIHMS125133; NLM/ PMC2820122
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58. Sawai H, Okada Y, Funahashi H, Matsuo Y, Takahashi H, Takeyama H, Manabe T: Integrin-linked kinase activity is associated with interleukin-1 alpha-induced progressive behavior of pancreatic cancer and poor patient survival. Oncogene; 2006 Jun 1;25(23):3237-46
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  • [Title] Integrin-linked kinase activity is associated with interleukin-1 alpha-induced progressive behavior of pancreatic cancer and poor patient survival.
  • Cancer cell adhesion and invasion into extracellular matrix are regulated by integrin-linked kinase (ILK) activity in a phosphatidylinositol 3-kinase (PI3-K)-dependent manner.
  • In this study, we demonstrated that ILK and beta(1)-integrin play important roles in interleukin (IL)-1alpha-induced enhancement of adhesion and invasion of pancreatic cancer cells through p38 mitogen-activated protein kinase (MAPK) signaling pathway and activator protein-1 (AP-1) activation.
  • Alteration of ILK kinase activity controlled IL-1alpha-induced p38 MAPK phosphorylation and its downstream AP-1 activation with subsequent regulation of pancreatic cancer cell adhesion and invasion.
  • Overexpressed ILK enhances the IL-1alpha-induced p38 MAPK phosphorylation more strongly through glycogen synthase kinase 3 (GSK-3) activation, and subsequently induces AP-1 activation, which promotes aggressive capabilities of pancreatic cancer cells.
  • In immunohistochemical analysis, statistically significant association between strong expression of ILK and poor prognosis of pancreatic cancer patients were observed, and strong expression of ILK in cancerous tissues can be a significant prognostic indicator of pancreatic cancer patients.
  • Our results suggest that ILK is involved with aggressive capability in pancreatic cancer and that these regulations can be helpful to understand biological processes for a better translational treatment for pancreatic cancer patients.
  • [MeSH-major] Antigens, CD29 / metabolism. Interleukin-1 / physiology. Pancreatic Neoplasms / enzymology. Pancreatic Neoplasms / mortality. Protein-Serine-Threonine Kinases / physiology
  • [MeSH-minor] Cell Adhesion / physiology. Cell Line, Tumor. Disease Progression. Humans. Neoplasm Invasiveness / pathology. Prognosis. Survival Analysis


59. El-Metwally TH, Hussein MR, Pour PM, Kuszynski CA, Adrian TE: High concentrations of retinoids induce differentiation and late apoptosis in pancreatic cancer cells in vitro. Cancer Biol Ther; 2005 May;4(5):602-11
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  • [Title] High concentrations of retinoids induce differentiation and late apoptosis in pancreatic cancer cells in vitro.
  • BACKGROUND: Our previous investigations showed that retinoids, at specific concentrations, can inhibit cell proliferation.
  • In this investigation, we hypothesize that high concentrations of retinoids can induce phenotypic changes (differentiation) and late apoptosis in pancreatic cancer cells in vitro.
  • Cotreatment with the RAR-alpha antagonist, Ro41-5253 or pan-TGF-beta neutralizing antibody abolished the phenotypic and antiproliferative effects of all-trans retinoic acid.
  • CONCLUSIONS: High concentrations of retinoids were able to induce phenotypic changes (differentiation) and late apoptosis in pancreatic cancer cells in vitro.
  • [MeSH-major] Apoptosis / drug effects. Cell Differentiation / drug effects. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / physiopathology. Retinoids / pharmacology
  • [MeSH-minor] Carbonic Anhydrases / biosynthesis. Cell Line, Tumor. Cell Proliferation / drug effects. Dose-Response Relationship, Drug. Enzyme Induction / drug effects. Gene Expression Regulation, Neoplastic / drug effects. Humans. In Vitro Techniques. Microscopy, Electron. Receptor, Epidermal Growth Factor / metabolism. Receptors, Retinoic Acid / antagonists & inhibitors. Time Factors. Transforming Growth Factor beta / metabolism. Transforming Growth Factor beta / secretion. Tretinoin / pharmacology

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  • (PMID = 15970678.001).
  • [ISSN] 1538-4047
  • [Journal-full-title] Cancer biology & therapy
  • [ISO-abbreviation] Cancer Biol. Ther.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Receptors, Retinoic Acid; 0 / Retinoids; 0 / Transforming Growth Factor beta; 0 / retinoic acid receptor alpha; 5688UTC01R / Tretinoin; EC 2.7.10.1 / Receptor, Epidermal Growth Factor; EC 4.2.1.1 / Carbonic Anhydrases
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60. Baril P, Gangeswaran R, Mahon PC, Caulee K, Kocher HM, Harada T, Zhu M, Kalthoff H, Crnogorac-Jurcevic T, Lemoine NR: Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the beta4 integrin and the PI3k pathway. Oncogene; 2007 Mar 29;26(14):2082-94
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  • [Title] Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the beta4 integrin and the PI3k pathway.
  • Pancreatic ductal adenocarcinoma is a devastating disease, characterized by a rapid progression and poor treatment response.
  • Using gene expression profiling of pancreatic cancer tissues, we previously identified periostin as a potential diagnostic and therapeutic target.
  • In this study, we report the overexpression of periostin in a larger set of pancreatic cancer tissues and show that although the periostin transcript is exclusively expressed in tumour cells, the protein product is only detected in the extracellular matrix adjacent to cancer cells.
  • Using an enzyme-linked immunosorbent assay (ELISA) assay, we show significantly increased levels of periostin in the sera of pancreatic cancer patients compared to non-cancer controls.
  • We demonstrate that periostin promotes the invasiveness of tumour cells by increasing the motility of cells without inducing expression of proteases, and enhances the survival of tumour cells exposed to hypoxic conditions.
  • At the molecular level, we provide evidence that the alpha(6)beta(4) integrin complex acts as the cell receptor of periostin in pancreatic cancer cells and that interaction promotes phosphorylation of focal adhesion kinase (FAK) and protein kinase B (AKT) though activation of the PI3 kinase pathway, but not the RAS/MEK/ERK pathway.
  • These findings suggest an important role of periostin in pancreatic cancer and provide a rationale to study periostin for diagnostic and therapeutic applications.
  • [MeSH-major] Carcinoma, Pancreatic Ductal / pathology. Cell Adhesion Molecules / physiology. Integrin beta4 / metabolism. Pancreatic Neoplasms / pathology. Phosphatidylinositol 3-Kinases / metabolism
  • [MeSH-minor] Anoxia / metabolism. Apoptosis. Cell Line, Tumor. Cell Movement / genetics. Focal Adhesion Kinase 1 / metabolism. Humans. Integrin alpha6beta4 / metabolism. Neoplasm Invasiveness. Phosphorylation. Proto-Oncogene Proteins c-akt / metabolism. RNA, Messenger / analysis. RNA, Messenger / metabolism. Transcription, Genetic


61. Grzesiak JJ, Smith KC, Burton DW, Deftos LJ, Bouvet M: Integrin-mediated laminin-1 adhesion upregulates CXCR4 and IL-8 expression in pancreatic cancer cells. Surgery; 2007 Jun;141(6):804-14
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  • [Title] Integrin-mediated laminin-1 adhesion upregulates CXCR4 and IL-8 expression in pancreatic cancer cells.
  • BACKGROUND: We have shown recently that alpha(2)beta(1) integrin-mediated type I collagen adhesion promotes a more malignant phenotype in pancreatic cancer cell lines than other extracellular matrix (ECM) proteins.
  • MiaPaCa-2 cells, by contrast, do not express collagen-binding integrins, but are metastatic in our orthotopic mouse model and migrate maximally on laminin-1 (Ln-1).
  • It has also been shown that CXCR4 and IL-8 expression correlates directly with metastasis in pancreatic cancer in vivo.
  • We therefore examined the potential of the ECM to regulate CXCR4 and IL-8 expression in pancreatic cancer cells.
  • METHODS: We cultured 8 pancreatic cancer cell lines on fibronectin (Fn), types I and IV collagen, Ln-1 and vitronectin (Vn), and examined cell lysates for CXCR4 by immunoblotting and media for IL-8 by ELISA.
  • We also conducted cell migration assays with stromal-derived factor-1 (SDF-1) as the chemoattractant to examine integrin-binding specificity and CXCR4 function.
  • RESULTS: All cell lines expressed CXCR4 protein.
  • MiaPaCa-2 cell growth on Ln-1 increased significantly CXCR4 and IL-8 expression relative to other ECM proteins.
  • Migration inhibition studies showed that both the alpha(6)beta(1) and alpha(3)beta(1) integrins mediate MiaPaCa-2 migration on Ln-1.
  • Growth studies showed further that CXCR4 expression on Ln-1 was mediated by the alpha(6)beta(1) integrin whereas IL-8 expression was mediated by both the alpha(6)beta(1) and alpha(3)beta(1) integrins.
  • The expression of functional CXCR4 was also shown in migration assays, where SDF-1 significantly increased pancreatic cancer cell chemotaxis on Ln-1.
  • CONCLUSIONS: These data indicate that integrin-mediated Ln-1 adhesion upregulates CXCR4 and IL-8 expression and may play a mechanistic role in pancreatic cancer metastases.

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  • (PMID = 17560257.001).
  • [ISSN] 0039-6060
  • [Journal-full-title] Surgery
  • [ISO-abbreviation] Surgery
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / R21 CA109949-01; United States / NIAMS NIH HHS / AR / AR47347; United States / NCI NIH HHS / CA / R21 CA109949-02; United States / NCI NIH HHS / CA / R33 CA109949-03; United States / NCI NIH HHS / CA / R33 CA109949; United States / NIDDK NIH HHS / DK / DK60588; United States / NCI NIH HHS / CA / CA109949-01; United States / NIAMS NIH HHS / AR / R01 AR047347; United States / NIDDK NIH HHS / DK / R01 DK060588; United States / NCI NIH HHS / CA / R21 CA109949
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / CXCL12 protein, human; 0 / Chemokine CXCL12; 0 / Chemokines, CXC; 0 / Cxcl12 protein, mouse; 0 / Extracellular Matrix Proteins; 0 / Integrin alpha3beta1; 0 / Integrin alpha6beta1; 0 / Integrins; 0 / Interleukin-8; 0 / Laminin; 0 / Receptors, CXCR4; 0 / laminin 1
  • [Other-IDs] NLM/ NIHMS25619; NLM/ PMC1994963
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62. Cappello P, Tomaino B, Chiarle R, Ceruti P, Novarino A, Castagnoli C, Migliorini P, Perconti G, Giallongo A, Milella M, Monsurrò V, Barbi S, Scarpa A, Nisticò P, Giovarelli M, Novelli F: An integrated humoral and cellular response is elicited in pancreatic cancer by alpha-enolase, a novel pancreatic ductal adenocarcinoma-associated antigen. Int J Cancer; 2009 Aug 1;125(3):639-48
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] An integrated humoral and cellular response is elicited in pancreatic cancer by alpha-enolase, a novel pancreatic ductal adenocarcinoma-associated antigen.
  • Pancreatic ductal adenocarcinoma (PDAC) is a fatal disease with a very poor 5-year survival rate. alpha-Enolase is a glycolytic enzyme that also acts as a surface plasminogen receptor.
  • We find that it is overexpressed in PDAC and present on the cell surface of PDAC cell lines.
  • The clinical correlation of its expression with tumor status has been reported for lung and hepatocellular carcinoma.
  • We have previously demonstrated that sera from PDAC patients contain IgG autoantibodies to alpha-enolase.
  • The present work was intended to assess the ability of alpha-enolase to induce antigen-specific T cell responses.
  • We show that alpha-enolase-pulsed dendritic cells (DC) specifically stimulate healthy autologous T cells to proliferate, secrete IFN-gamma and lyse PDAC cells but not normal cells.
  • In vivo, alpha-enolase-specific T cells inhibited the growth of PDAC cells in immunodeficient mice.
  • In 8 out of 12 PDAC patients with circulating IgG to alpha-enolase, the existence of alpha-enolase-specific T cells was also demonstrated.
  • Taken as a whole, these results indicate that alpha-enolase elicits a PDAC-specific, integrated humoral and cellular response.
  • It is thus a promising and clinically relevant molecular target candidate for immunotherapeutic approaches as new adjuvants to conventional treatments in pancreatic cancer.
  • [MeSH-major] Antibodies, Neoplasm / immunology. Antigens, Neoplasm / immunology. Carcinoma, Pancreatic Ductal / enzymology. Carcinoma, Pancreatic Ductal / immunology. Cell Proliferation. Pancreatic Neoplasms / enzymology. Pancreatic Neoplasms / immunology. Phosphopyruvate Hydratase / metabolism. T-Lymphocytes
  • [MeSH-minor] Animals. Antibody Formation. Blotting, Western. Cell Line, Tumor. Dendritic Cells / immunology. Gene Expression Regulation, Enzymologic. Gene Expression Regulation, Neoplastic. Humans. Immunity, Cellular. Immunoglobulin G / blood. Immunohistochemistry. Interferon-gamma / secretion. Keratinocytes / immunology. Mice. Pancreas / enzymology. Pancreas / immunology. Skin / cytology. T-Lymphocytes, Cytotoxic / immunology. Up-Regulation

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  • (PMID = 19425054.001).
  • [ISSN] 1097-0215
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antibodies, Neoplasm; 0 / Antigens, Neoplasm; 0 / Immunoglobulin G; 82115-62-6 / Interferon-gamma; EC 4.2.1.11 / Phosphopyruvate Hydratase
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63. Riggs DR, Jackson BJ, Vona-Davis L, Nigam A, McFadden DW: In vitro effects of keyhole limpet hemocyanin in breast and pancreatic cancer in regards to cell growth, cytokine production, and apoptosis. Am J Surg; 2005 Jun;189(6):680-4
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] In vitro effects of keyhole limpet hemocyanin in breast and pancreatic cancer in regards to cell growth, cytokine production, and apoptosis.
  • BACKGROUND: We have previously shown the inhibitory effects of keyhole limpet hemocyanin (KLH) against breast and pancreatic cancer in vitro.
  • We hypothesize that its actions in breast and pancreas cancer cells are via apoptotic or cytokine pathways.
  • METHODS: Two breast cancer cell lines, ZR75-1 and MCF-7, and one pancreas cancer cell line, PANC-1, were treated with KLH at 500 mug, 250 mug, and 250 ng/mL.
  • Cell viability, cytokine production, and apoptosis were measured.
  • RESULTS: Significant growth inhibition was observed in all cell lines at all KLH concentrations tested.
  • Significant changes in cytokine production were observed in all cell lines.
  • An increase in early and late apoptotic activity was observed in the MCF-7, whereas a reduction in late apoptotic activity was observed in the ZR75-1 cells.
  • CONCLUSIONS: KLH directly inhibits the growth of human breast and pancreas cancer in vitro by apoptotic and nonapoptotic mechanisms.
  • [MeSH-major] Adjuvants, Immunologic / pharmacology. Breast Neoplasms / metabolism. Hemocyanin / pharmacology. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Apoptosis / drug effects. Cell Line, Tumor. Female. Humans. In Vitro Techniques. Interleukins / metabolism. Male. Tumor Necrosis Factor-alpha / metabolism

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  • (PMID = 15910720.001).
  • [ISSN] 0002-9610
  • [Journal-full-title] American journal of surgery
  • [ISO-abbreviation] Am. J. Surg.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Adjuvants, Immunologic; 0 / Interleukins; 0 / Tumor Necrosis Factor-alpha; 9013-72-3 / Hemocyanin; FV4Y0JO2CX / keyhole-limpet hemocyanin
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64. Bai J, Sui J, Demirjian A, Vollmer CM Jr, Marasco W, Callery MP: Predominant Bcl-XL knockdown disables antiapoptotic mechanisms: tumor necrosis factor-related apoptosis-inducing ligand-based triple chemotherapy overcomes chemoresistance in pancreatic cancer cells in vitro. Cancer Res; 2005 Mar 15;65(6):2344-52
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  • [Title] Predominant Bcl-XL knockdown disables antiapoptotic mechanisms: tumor necrosis factor-related apoptosis-inducing ligand-based triple chemotherapy overcomes chemoresistance in pancreatic cancer cells in vitro.
  • Pancreatic cancer is lethal because of its invasiveness, rapid progression, and profound resistance to chemotherapy and radiation therapy.
  • To identify the molecular mechanisms underlying this, we have examined the expression and potency of three major death receptors: tumor necrosis factor receptor (TNF-R), TNF-related apoptosis-inducing ligand receptor (TRAIL-R), and Fas in mediating cytotoxicity in four invasive pancreatic cancer cell lines.
  • We have analyzed the expression of major antiapoptotic factors, cell cycle regulators and death receptor decoys (DcR) in comparison with normal pancreas tissues and five other human malignant tumor cell lines.
  • We have found that different pancreatic cancer cell lines coexpress high-level TRAIL-R, Fas, and TNF-R1 but are strongly resistant to apoptosis triggered by the death receptors.
  • DcR2 and DcR3 overexpression may partly contribute to the resistance of pancreatic cancer cells to TRAIL-R- and Fas-mediated cytotoxicity.
  • Bcl-XL and Bcl-2 are predominantly overexpressed in pancreatic cancer cell lines, respectively.
  • Bcl-XL is also predominantly overexpressed in prostate, colorectal, and intestinal cancer cells.
  • The knockdown of the predominant Bcl-XL overexpression significantly reduces the viability of pancreatic cancer cells to TNFalpha- and TRAIL-mediated apoptosis by sublethal-dose single and combined antitumor drugs, including geldanamycin, PS-341, Trichostatin A, and doxorubicine.
  • Bcl-XL plays a vital role in pancreatic cancer chemoresistance.
  • Geldanamycin, PS-341, and TRAIL triple combination may be a novel therapeutic strategy for pancreatic cancer.
  • [MeSH-major] Antineoplastic Combined Chemotherapy Protocols / pharmacology. Apoptosis / physiology. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / pathology. Proto-Oncogene Proteins c-bcl-2 / deficiency. Tumor Necrosis Factor-alpha / pharmacology
  • [MeSH-minor] Apoptosis Regulatory Proteins. Benzoquinones. Boronic Acids / administration & dosage. Boronic Acids / pharmacology. Bortezomib. Cell Line, Tumor. Doxorubicin / administration & dosage. Doxorubicin / pharmacology. Drug Synergism. Gene Expression Regulation, Neoplastic. Gene Silencing. HSP90 Heat-Shock Proteins / metabolism. Humans. Hydroxamic Acids / administration & dosage. Hydroxamic Acids / pharmacology. Lactams, Macrocyclic. Membrane Glycoproteins. Pyrazines / administration & dosage. Pyrazines / pharmacology. Quinones / administration & dosage. Quinones / pharmacology. TNF-Related Apoptosis-Inducing Ligand. bcl-X Protein

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  • (PMID = 15781649.001).
  • [ISSN] 0008-5472
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Apoptosis Regulatory Proteins; 0 / BCL2L1 protein, human; 0 / Benzoquinones; 0 / Boronic Acids; 0 / HSP90 Heat-Shock Proteins; 0 / Hydroxamic Acids; 0 / Lactams, Macrocyclic; 0 / Membrane Glycoproteins; 0 / Proto-Oncogene Proteins c-bcl-2; 0 / Pyrazines; 0 / Quinones; 0 / TNF-Related Apoptosis-Inducing Ligand; 0 / TNFSF10 protein, human; 0 / Tumor Necrosis Factor-alpha; 0 / bcl-X Protein; 3X2S926L3Z / trichostatin A; 69G8BD63PP / Bortezomib; 80168379AG / Doxorubicin; Z3K3VJ16KU / geldanamycin
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65. Schwartz DL, Bankson JA, Lemos R Jr, Lai SY, Thittai AK, He Y, Hostetter G, Demeure MJ, Von Hoff DD, Powis G: Radiosensitization and stromal imaging response correlates for the HIF-1 inhibitor PX-478 given with or without chemotherapy in pancreatic cancer. Mol Cancer Ther; 2010 Jul;9(7):2057-67
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  • [Title] Radiosensitization and stromal imaging response correlates for the HIF-1 inhibitor PX-478 given with or without chemotherapy in pancreatic cancer.
  • Growing tumors are hypoxic and respond to microenvironmental stress through increased expression of the hypoxia inducible factor-1alpha (HIF-1alpha) transcription factor, resulting in an adaptive switch to glycolytic metabolism, angiogenic signaling, survival, and metastasis.
  • HIF-1alpha expression is associated with tumor resistance to cytotoxic therapy and inferior patient outcomes.
  • Pancreatic cancer is the most hypoxic of all solid tumors and remains refractory to current chemoradiotherapy.
  • We have seen nuclear HIF-1alpha in 88% of human pancreatic ductal carcinoma but in only 16% of normal pancreas.
  • Stroma adjacent to the pancreatic ductal carcinoma also showed HIF-1alpha in 43% of cases.
  • We investigated the novel selective HIF-1alpha inhibitor PX-478 on in vitro and in vivo radiation response of human pancreatic cancer models.
  • Inhibition of HIF-1alpha by PX-478 increased cell killing by radiation.
  • In mice with Panc-1, CF-PAC-1, or SU.86.86 pancreatic xenografts, concurrent administration of PX-478 potentiated the antitumor effects of fractionated radiation, with or without combined treatment with 5-fluorouracil or gemcitabine.
  • Early tumor responses to combined PX-478/radiation treatment could be rapidly and repeatedly quantified by vascular imaging biomarkers.
  • Dual-tracer dynamic contrast enhanced-magnetic resonance imaging and ultrasound imaging discriminated response to combined treatment prior to detection of differences in anatomic tumor size at 10 days posttreatment.
  • Therefore, PX-478 is a mechanistically appealing and potentially clinically relevant enhancer of pancreatic cancer radiosensitivity, inhibiting tumor and stromal HIF-1 proangiogenic signaling and reducing the innate radiation resistance of hypoxic tumor cells.

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  • [Copyright] (c)2010 AACR.
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  • (PMID = 20587661.001).
  • [ISSN] 1538-8514
  • [Journal-full-title] Molecular cancer therapeutics
  • [ISO-abbreviation] Mol. Cancer Ther.
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / P30 CA016672; United States / NCI NIH HHS / CA / CA109552-050002; United States / NCI NIH HHS / CA / R01 CA098920-07; United States / NIDCR NIH HHS / DE / K08 DE018061; United States / NIDCR NIH HHS / DE / DE018061-04; United States / NCI NIH HHS / CA / P30 CA016672-34; United States / NIDCR NIH HHS / DE / K08 DE018061-04; United States / PHS HHS / / 095920; United States / NCI NIH HHS / CA / U24 CA126577; United States / NCI NIH HHS / CA / P01 CA109552-050002; United States / NCI NIH HHS / CA / R01 CA098920; United States / PHS HHS / / 126577; United States / PHS HHS / / 016672; United States / NCI NIH HHS / CA / U24 CA126577-05; United States / NCI NIH HHS / CA / CA095060-080003; United States / NCI NIH HHS / CA / P50 CA095060; United States / NCI NIH HHS / CA / CA017094-290031; United States / NCI NIH HHS / CA / P01 CA017094; United States / NCI NIH HHS / CA / P01 CA017094-290031; United States / PHS HHS / / 017094; United States / NCI NIH HHS / CA / P50 CA095060-080003; United States / NCI NIH HHS / CA / CA098920-07; United States / NCI NIH HHS / CA / P01 CA109552; United States / NCI NIH HHS / CA / CA109552; United States / PHS HHS / / 095060
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / 2-amino-3-(4'-N,N-bis(2-chloroethyl)amino)phenylpropionic acid N-oxide; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Mustard Compounds; 0 / Phenylpropionates
  • [Other-IDs] NLM/ NIHMS222288; NLM/ PMC2935253
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66. Komachi M, Tomura H, Malchinkhuu E, Tobo M, Mogi C, Yamada T, Kimura T, Kuwabara A, Ohta H, Im DS, Kurose H, Takeyoshi I, Sato K, Okajima F: LPA1 receptors mediate stimulation, whereas LPA2 receptors mediate inhibition, of migration of pancreatic cancer cells in response to lysophosphatidic acid and malignant ascites. Carcinogenesis; 2009 Mar;30(3):457-65
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  • [Title] LPA1 receptors mediate stimulation, whereas LPA2 receptors mediate inhibition, of migration of pancreatic cancer cells in response to lysophosphatidic acid and malignant ascites.
  • Malignant ascites from pancreatic cancer patients has been reported to stimulate migration of pancreatic cancer cells through lysophosphatidic acid (LPA) and LPA(1) receptors.
  • Indeed, ascites- and LPA-induced migration was inhibited by Ki16425, an LPA(1) and LPA(3) antagonist, in Panc-1 cells.
  • Unexpectedly, however, in the presence of Ki16425, ascites and LPA inhibited cell migration in response to epidermal growth factor (EGF).
  • The inhibitory migratory response to ascites and LPA was also observed in the cells treated with pertussis toxin (PTX), a G(i) protein inhibitor, and attenuated by a small interfering RNA (siRNA) specific to the LPA(2) receptor.
  • Moreover, LP-105, an LPA(2) agonist, also inhibited EGF-induced migration in the PTX-treated cells.
  • A similar inhibitory migration response through LPA(2) receptors was also observed in YAPC-PD, BxPC-3, CFPAC-1 and PK-1 pancreatic cancer cell lines.
  • LPA also inhibited the invasion of Panc-1 cells in the PTX-treated cells in the in vitro Matrigel invasion assay.
  • We conclude that LPA(2) receptors are coupled to the G(12/13) protein/Rho-signaling pathway, leading to the inhibition of EGF-induced migration and invasion of pancreatic cancer cells.
  • [MeSH-major] Ascites / metabolism. Cell Movement / drug effects. Lysophospholipids / pharmacology. Pancreatic Neoplasms / metabolism. Receptors, Lysophosphatidic Acid / physiology
  • [MeSH-minor] Cell Line, Tumor. Collagen. Drug Combinations. Epidermal Growth Factor / pharmacology. GTP-Binding Protein alpha Subunits, Gi-Go / antagonists & inhibitors. Humans. Isoxazoles / pharmacology. Laminin. Neoplasm Invasiveness. Pertussis Toxin / pharmacology. Propionates / pharmacology. Proteoglycans. RNA, Small Interfering / genetics. rhoA GTP-Binding Protein / metabolism

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  • (PMID = 19129242.001).
  • [ISSN] 1460-2180
  • [Journal-full-title] Carcinogenesis
  • [ISO-abbreviation] Carcinogenesis
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / 3-(4-(4-((1-(2-chlorophenyl)ethoxy)carbonyl amino)-3-methyl-5-isoxazolyl) benzylsulfanyl) propanoic acid; 0 / Drug Combinations; 0 / Isoxazoles; 0 / Laminin; 0 / Lysophospholipids; 0 / Propionates; 0 / Proteoglycans; 0 / RNA, Small Interfering; 0 / Receptors, Lysophosphatidic Acid; 119978-18-6 / matrigel; 22002-87-5 / lysophosphatidic acid; 62229-50-9 / Epidermal Growth Factor; 9007-34-5 / Collagen; EC 2.4.2.31 / Pertussis Toxin; EC 3.6.5.1 / GTP-Binding Protein alpha Subunits, Gi-Go; EC 3.6.5.2 / rhoA GTP-Binding Protein
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67. Kayed H, Jiang X, Keleg S, Jesnowski R, Giese T, Berger MR, Esposito I, Löhr M, Friess H, Kleeff J: Regulation and functional role of the Runt-related transcription factor-2 in pancreatic cancer. Br J Cancer; 2007 Oct 22;97(8):1106-15
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  • [Title] Regulation and functional role of the Runt-related transcription factor-2 in pancreatic cancer.
  • In the present study, the localisation of the Runt-related transcription factor-2 (Runx2), its transcriptional activity, as well as its regulation of expression was analysed in human pancreatic ductal adenocarcinoma (PDAC).
  • Runt-related transcription factor-2 expression was silenced using specific siRNA oligonucleotides in pancreatic cancer cells (Panc-1) and immortalised pancreatic stellate cells (IPSCs).
  • There was a 6.1-fold increase in median Runx2 mRNA levels in PDAC tissues compared to normal pancreatic tissues (P<0.0001).
  • Runt-related transcription factor-2 was localised in pancreatic cancer cells, tubular complexes, and PanIN lesions of PDAC tissues as well as in tumour-associated fibroblasts/stellate cells.
  • Coculture of IPSCs and Panc-1 cells, as well as treatment with TGF-beta1 and BMP2, led to increased Runx2 expression in Panc-1 cells.
  • Runt-related transcription factor-2 overexpression was associated with decreased MMP1 release as well as decreased growth and invasion of Panc-1 cells.
  • In addition, Runx2 has the potential to regulate the transcription of extracellular matrix modulators such as SPARC and MMP1, thereby influencing the tumour microenvironment.
  • [MeSH-major] Carcinoma, Pancreatic Ductal / metabolism. Core Binding Factor Alpha 1 Subunit / metabolism. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Blotting, Western. Cell Line, Tumor. Enzyme-Linked Immunosorbent Assay. Gene Expression. Humans. Immunohistochemistry. Matrix Metalloproteinase 1 / biosynthesis. RNA, Messenger / analysis. RNA, Small Interfering. Reverse Transcriptase Polymerase Chain Reaction. Transfection

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  • (PMID = 17876328.001).
  • [ISSN] 0007-0920
  • [Journal-full-title] British journal of cancer
  • [ISO-abbreviation] Br. J. Cancer
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Core Binding Factor Alpha 1 Subunit; 0 / RNA, Messenger; 0 / RNA, Small Interfering; 0 / RUNX2 protein, human; EC 3.4.24.7 / Matrix Metalloproteinase 1
  • [Other-IDs] NLM/ PMC2360444
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68. Matsumoto G, Muta M, Umezawa K, Suzuki T, Misumi K, Tsuruta K, Okamoto A, Toi M: Enhancement of the caspase-independent apoptotic sensitivity of pancreatic cancer cells by DHMEQ, an NF-kappaB inhibitor. Int J Oncol; 2005 Nov;27(5):1247-55
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  • [Title] Enhancement of the caspase-independent apoptotic sensitivity of pancreatic cancer cells by DHMEQ, an NF-kappaB inhibitor.
  • The effects of the nuclear factor (NF)-kappaB inhibitor, dehydroxymethylepoxyquinomicin (DHMEQ), combined with tumor necrosis factor (TNF)-alpha were evaluated in PK-8 pancreatic cancer cells.
  • NF-kappaB was activated by TNF-alpha; however, the administration of DHMEQ abrogated its transcriptional activity.
  • The addition of DHMEQ to TNF-alpha markedly induced apoptosis in PK-8 cells with down-regulation of anti-apoptotic c-FLIP and survivin.
  • Combined treatment significantly suppressed cell viability in vitro, and the anti-tumor effect of DHMEQ was also significant in vivo.
  • We investigated the apoptosis signaling pathway involved in these cell killing effects.
  • Z-VAD-fmk (a pan-caspase inhibitor) perfectly inhibited the up-regulation of caspase-3 but failed to reverse the cell viability.
  • Thus, the addition of DHMEQ to TNF-alpha was capable of inducing caspase-independent apoptosis in pancreatic cancer cells.
  • Therefore, DHMEQ in combination with TNF-alpha may be a promising treatment for pancreatic cancer.
  • [MeSH-major] Apoptosis / drug effects. Benzamides / pharmacology. Caspases / metabolism. Cyclohexanones / pharmacology. Pancreatic Neoplasms / pathology. Tumor Necrosis Factor-alpha / physiology
  • [MeSH-minor] Caspase 3. Cell Survival. Drug Interactions. Humans. Kinetics. Mitochondria / enzymology. Tumor Cells, Cultured. Up-Regulation

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  • (PMID = 16211219.001).
  • [ISSN] 1019-6439
  • [Journal-full-title] International journal of oncology
  • [ISO-abbreviation] Int. J. Oncol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Greece
  • [Chemical-registry-number] 0 / Benzamides; 0 / Cyclohexanones; 0 / Tumor Necrosis Factor-alpha; 0 / dehydroxymethylepoxyquinomicin; EC 3.4.22.- / CASP3 protein, human; EC 3.4.22.- / Caspase 3; EC 3.4.22.- / Caspases
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69. Wang F, Larsson J, Herrington MK, Permert J: PP56 improves energy homeostasis in a mouse model of pancreatic cancer. Tumour Biol; 2010 Aug;31(4):309-13
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  • [Title] PP56 improves energy homeostasis in a mouse model of pancreatic cancer.
  • In this study, we investigated whether the anti-inflammatory drug PP56 (alpha-trinositol) may improve cancer-induced metabolic disorders.
  • We implanted human MiaPaCa2 pancreatic cancer cells in the pancreas of 14 athymic mice for 12 weeks, using six intact littermates as normal controls.
  • During the 12 weeks, seven tumor-cell recipients were treated with PP56 by daily injection (PPT mice).
  • The tumor-cell recipients that were otherwise untreated were used as tumor controls (TC mice).
  • Impaired glucose tolerance and decreased body weight gain were seen in TC but not PPT mice.
  • When an enzyme for fatty acid beta-oxidation namely medium-chain acyl-CoA dehydrogenase (MCAD) was determined in tumor grafts; tumors from PPT mice showed more MCAD than those from TC mice.
  • This suggests that PP56 stimulated fatty acid beta-oxidation in MiaPaCa2 cells in vivo.
  • In vitro, we demonstrated that MiaPaCa2 cells consumed more fatty acids in the presence of PP56.
  • We also showed that PP56 increased glucose transport in L6 skeletal muscle cells in vitro.
  • In conclusion, PP56 increases the turnover of circulating nutrients such as glucose and helps maintain energy homeostasis in mice with pancreatic cancer.
  • [MeSH-major] Anti-Inflammatory Agents, Non-Steroidal / pharmacology. Disease Models, Animal. Energy Metabolism / drug effects. Homeostasis / drug effects. Inositol Phosphates / pharmacology. Pancreatic Neoplasms / drug therapy
  • [MeSH-minor] Acyl-CoA Dehydrogenase / metabolism. Animals. Blood Glucose / metabolism. Cells, Cultured. Fatty Acids / metabolism. Humans. Male. Mice. Mice, Inbred C57BL. Muscle, Skeletal / cytology. Muscle, Skeletal / drug effects. Muscle, Skeletal / metabolism. Rats

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  • (PMID = 20422342.001).
  • [ISSN] 1423-0380
  • [Journal-full-title] Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine
  • [ISO-abbreviation] Tumour Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Anti-Inflammatory Agents, Non-Steroidal; 0 / Blood Glucose; 0 / Fatty Acids; 0 / Inositol Phosphates; EC 1.3.8.7 / Acyl-CoA Dehydrogenase; VYF3049W3N / atrinositol
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70. Wang L, Zhou W, Gou S, Wang T, Liu T, Wang C: Insulin promotes proliferative vitality and invasive capability of pancreatic cancer cells via hypoxia-inducible factor 1alpha pathway. J Huazhong Univ Sci Technolog Med Sci; 2010 Jun;30(3):349-53
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  • [Title] Insulin promotes proliferative vitality and invasive capability of pancreatic cancer cells via hypoxia-inducible factor 1alpha pathway.
  • This study examined whether insulin-stimulated hypoxia-inducible factor 1alpha (HIF-1alpha) expression plays a crucial role in promoting the proliferative vitality and invasive capability in human pancreatic cancer cells.
  • PANC-1 cells were divided into three groups: Control group, insulin group and insulin+YC-1 (a pharmacological inhibitor of HIF-1alpha) group in terms of different treatments.
  • Cells in the insulin group or insulin+YC-1 group were treated with insulin (0.1, 1, 10 and 100 nmol/L) alone or combined with 3-(5'-hydroxymethyl-2'-furyl)-1-benzyl indazole (YC-1, 0.1, 1, 10 and 100 micromol/L).
  • HIF-1alpha mRNA and protein expression in PANC-1 cells was determined by real-time RT-PCR and Western blotting respectively.
  • Cell proliferation and invasion were measured by using growth curve and invasion assay, respectively.
  • However, neither insulin nor YC-1 altered HIF-1alpha mRNA levels in PANC-1 cells.
  • Moreover, insulin could enhance the proliferation and invasion of PANC-1 cells, while YC-1 could weaken this effect.
  • It was concluded that the malignant proliferation and local invasion of pancreatic cancer cells may be related to high-insulin microenvironment.
  • The tumor biological behavior change resulting from high-insulin microenvironment may be associated with the increased expression of HIF-1alpha protein.
  • [MeSH-major] Cell Proliferation / drug effects. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Indazoles / pharmacology. Insulin / pharmacology. Pancreatic Neoplasms / pathology
  • [MeSH-minor] Cell Line, Tumor. Guanylate Cyclase. Humans. Neoplasm Invasiveness. RNA, Messenger / genetics. RNA, Messenger / metabolism. Signal Transduction

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  • (PMID = 20556580.001).
  • [ISSN] 1672-0733
  • [Journal-full-title] Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban
  • [ISO-abbreviation] J. Huazhong Univ. Sci. Technol. Med. Sci.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] China
  • [Chemical-registry-number] 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Indazoles; 0 / Insulin; 0 / RNA, Messenger; 154453-18-6 / 3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole; EC 4.6.1.2 / Guanylate Cyclase
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71. Hosoi F, Izumi H, Kawahara A, Murakami Y, Kinoshita H, Kage M, Nishio K, Kohno K, Kuwano M, Ono M: N-myc downstream regulated gene 1/Cap43 suppresses tumor growth and angiogenesis of pancreatic cancer through attenuation of inhibitor of kappaB kinase beta expression. Cancer Res; 2009 Jun 15;69(12):4983-91
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  • [Title] N-myc downstream regulated gene 1/Cap43 suppresses tumor growth and angiogenesis of pancreatic cancer through attenuation of inhibitor of kappaB kinase beta expression.
  • N-myc downstream regulated gene 1 (NDRG1)/Cap43 expression is a predictive marker of good prognosis in patients with pancreatic cancer as we reported previously.
  • In this study, NDRG1/Cap43 decreased the expression of various chemoattractants, including CXC chemokines for inflammatory cells, and the recruitment of macrophages and neutrophils with suppression of both angiogenesis and growth in mouse xenograft models.
  • Decreased IKKbeta expression in cells overexpressing NDRG1/Cap43 resulted in reduction of both nuclear translocation of p65 and p50 and their binding to the NF-kappaB motif.
  • The introduction of an exogenous IKKbeta gene restored NDRG1/Cap43-suppressed expression of melanoma growth-stimulating activity alpha/CXCL1, epithelial-derived neutrophil activating protein-78/CXCL5, interleukin-8/CXCL8 and vascular endothelial growth factor-A, accompanied by increased phosphorylation of IkappaBalpha in NDRG1/Cap43-expressing cells.
  • In patients with pancreatic cancer, NDRG1/Cap43 expression levels were also inversely correlated with the number of infiltrating macrophages in the tumor stroma.
  • This study suggests a novel mechanism by which NDRG1/Cap43 modulates tumor angiogenesis/growth and infiltration of macrophages/neutrophils through attenuation of NF-kappaB signaling.
  • [MeSH-major] Cell Cycle Proteins / physiology. Cell Division / genetics. I-kappa B Kinase / metabolism. Intracellular Signaling Peptides and Proteins / physiology. Neovascularization, Pathologic / genetics. Pancreatic Neoplasms / pathology
  • [MeSH-minor] Base Sequence. Cell Line, Tumor. Chemokines / metabolism. DNA Primers. Humans. Phosphorylation

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  • (PMID = 19491262.001).
  • [ISSN] 1538-7445
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Cell Cycle Proteins; 0 / Chemokines; 0 / DNA Primers; 0 / Intracellular Signaling Peptides and Proteins; 0 / N-myc downstream-regulated gene 1 protein; EC 2.7.11.10 / I-kappa B Kinase
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72. Vervoort L, Burvenich I, Staelens S, Dumolyn C, Waegemans E, Van Steenkiste M, Baird SK, Scott AM, De Vos F: Preclinical evaluation of monoclonal antibody 14C5 for targeting pancreatic cancer. Cancer Biother Radiopharm; 2010 Apr;25(2):193-205
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  • [Title] Preclinical evaluation of monoclonal antibody 14C5 for targeting pancreatic cancer.
  • The use of radiolabeled antibodies that are able to target primary tumors as well as metastatic tumor sites with minimal reactivity to normal tissues is a promising approach for treating pancreatic cancer.
  • In this study, the integrin alpha(v)beta(5) is studied as a target for the diagnosis of and potential therapy for human pancreatic cancer by using the radiolabeled murine monoclonal antibody (mAb) 14C5.
  • Biopsy specimens from human pancreatic tumors were examined for the expression of the integrin alpha(v)beta(5).
  • The pancreatic tumor cell line Capan-1 was used to test the in vitro targeting potency of mAb 14C5 labeled with 125/131-iodine and 111-indium.
  • Biodistribution and tumor-targeting characteristics were studied in Capan-1 xenografts.
  • All tumor sections were positive for the integrin alpha(v)beta(5), with an extensive positive staining of the stroma.
  • In vivo radioisotope tumor uptake was maximum at 48-72 hours, with the uptake of (111)In-p-SCN-Bz-DOTA-14C5 (35.84 +/- 8.64 percentage of injected dose per g [%ID/g]) being 3.9- and 2.2-folds higher than (131)I-14C5 (12.16 +/- 1.03%ID/g) and (111)In-p-SCN-Bz-DTPA-14C5 (14.30 +/- 3.76%ID/g), respectively.
  • Planar gamma imaging with mAb 14C5 indicated clear localization of the pancreatic tumors versus minimal normal tissue uptake. mAb 14C5 is a promising new antibody for targeting the integrin alpha(v)beta(5) for the diagnosis of and potential therapy for pancreatic cancer.
  • [MeSH-major] Antibodies, Monoclonal / therapeutic use. Pancreatic Neoplasms / therapy. Radiopharmaceuticals. Xenograft Model Antitumor Assays
  • [MeSH-minor] Animals. Drug Evaluation, Preclinical. Female. Humans. Iodine Radioisotopes. Mice. Mice, Nude. Pancreas / immunology. Pancreas / metabolism. Pancreas / pathology. Pentetic Acid / analogs & derivatives. Pentetic Acid / pharmacokinetics. Radioimmunoassay. Receptors, Vitronectin / immunology. Receptors, Vitronectin / metabolism. Tissue Distribution. Tumor Cells, Cultured

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  • (PMID = 20423233.001).
  • [ISSN] 1557-8852
  • [Journal-full-title] Cancer biotherapy & radiopharmaceuticals
  • [ISO-abbreviation] Cancer Biother. Radiopharm.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / 14C5 monoclonal antibody; 0 / Antibodies, Monoclonal; 0 / Iodine Radioisotopes; 0 / Radiopharmaceuticals; 0 / Receptors, Vitronectin; 0 / integrin alphaVbeta5; 102650-30-6 / 1-(4-isothiocyanatobenzyl)diethylenetriaminepentaacetic acid; 7A314HQM0I / Pentetic Acid
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73. Saruc M, Iki K, Pour PM: Morphometric studies in human pancreatic cancer argues against the etiological role of type 2 diabetes in pancreatic cancer. Histol Histopathol; 2010 04;25(4):423-32
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  • [Title] Morphometric studies in human pancreatic cancer argues against the etiological role of type 2 diabetes in pancreatic cancer.
  • BACKGROUND: To understand the role of islet amyloid polypeptide (IAPP) in type 2 diabetes and pancreatic cancer (PC), we investigated the patterns of its expression and its ratio to insulin, glucagon, somatostatin and pancreatic polypeptide cells by morphometry in tissues from these two diseases in comparison to the normal pancreas.
  • MATERIALS AND METHODS: Pancreatic tissues from 11 donors (five without pancreatic disease and six with type 2 diabetes) and 11 surgical specimens from PC patients obtained from the cancer area (zone A) and the adjacent tumor-free area (zone B) were examined immunohistochemically.
  • The size of islets, the number on beta-, alpha-, delta- pp- and IAPP-expressing cells and their ratios in the islets of these tissues were determined.
  • RESULTS: In the normal pancreas, only 50% of the beta-cells while alpha- and delta-cells co-expressed IAPP only sporadically.
  • In tissues from diabetics as well as in zone A, the number of the beta-cells and the IAPP-expressing cells was reduced significantly, while the number of alpha- and delta-cells was increased.
  • In zone B, however, significantly more beta-cell and IAPP-expressing cells and a significantly lower number of alpha-cells were found compared to those in zone A.
  • Significant differences were also found between the specimens from type 2 diabetics and pancreatic cancer relative to the ratios of IAPP/beta-cell, IAPP/alpha-cells and beta-cell/delta-cells.
  • CONCLUSION: The morphometric data show a decrease rather than an increase in the number of IAPP-expressing cells in PC.
  • Differences in abnormalities in type-2 diabetics and in zone B of PC tissue strongly argue against the role of type 2 diabetes in PC.
  • Rather, the development of diabetes in subjects prone to pancreatic cancer could be a red flag for malignancy.
  • [MeSH-major] Adenocarcinoma / pathology. Diabetes Mellitus, Type 2 / pathology. Morphogenesis / physiology. Pancreas / pathology. Pancreatic Neoplasms / pathology. Somatostatin / metabolism
  • [MeSH-minor] Adolescent. Adult. Aged. Aged, 80 and over. Amyloid / metabolism. Biomarkers, Tumor / metabolism. Female. Glucagon / metabolism. Humans. Immunoenzyme Techniques. Insulin / metabolism. Islet Amyloid Polypeptide. Islets of Langerhans / metabolism. Islets of Langerhans / pathology. Male. Middle Aged. Pancreatic Polypeptide / metabolism


74. Deguchi T, Tanemura M, Miyoshi E, Nagano H, Machida T, Ohmura Y, Kobayashi S, Marubashi S, Eguchi H, Takeda Y, Ito T, Mori M, Doki Y, Sawa Y: Increased immunogenicity of tumor-associated antigen, mucin 1, engineered to express alpha-gal epitopes: a novel approach to immunotherapy in pancreatic cancer. Cancer Res; 2010 Jul 1;70(13):5259-69
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  • [Title] Increased immunogenicity of tumor-associated antigen, mucin 1, engineered to express alpha-gal epitopes: a novel approach to immunotherapy in pancreatic cancer.
  • Mucin 1 (MUC1), a bound mucin glycoprotein, is overexpressed and aberrantly glycosylated in >80% of human ductal pancreatic carcinoma.
  • Evidence suggests that MUC1 can be used as a tumor marker and is a potential target for immunotherapy of pancreatic cancer.
  • However, vaccination with MUC1 peptides fails to stimulate the immune response against cancer cells because immunity toward tumor-associated antigens (TAA), including MUC1, in cancer patients is relatively weak, and the presentation of these TAAs to the immune system is poor due to their low immunogenicity.
  • We investigated whether vaccination with immunogenetically enhanced MUC1 (by expressing alpha-gal epitopes; Galalpha1-3Galbeta1-4GlcNAc-R) can elicit effective antibody production for MUC1 itself as well as certain TAAs derived from pancreatic cancer cells and induced tumor-specific T-cell responses.
  • We also used alpha1,3galactosyltransferase (alpha1,3GT) knockout mice that were preimmunized with pig kidney and transplanted with B16F10 melanoma cells transfected with MUC1 expression vector.
  • Vaccination of these mice with alpha-gal MUC1 resulted in marked inhibition of tumor growth and significant improvement of overall survival time compared with mice vaccinated with MUC1 alone (P = 0.003).
  • Furthermore, vaccination with pancreatic cancer cells expressing alpha-gal epitopes induced immune responses against not only differentiated cancer cells but also cancer stem cells.
  • The results suggested that vaccination using cells engineered to express alpha-gal epitopes is a novel strategy for treatment of pancreatic cancer.
  • [MeSH-major] Cancer Vaccines / immunology. Immunotherapy, Active / methods. Mucin-1 / immunology. Pancreatic Neoplasms / immunology. Trisaccharides / immunology
  • [MeSH-minor] Animals. Antibody Formation. B-Lymphocytes / immunology. Epitopes / biosynthesis. Epitopes / genetics. Epitopes / immunology. Humans. Mice. Mice, Knockout. Neoplastic Stem Cells / immunology. Protein Engineering / methods. Swine. T-Lymphocytes / immunology. Transfection


75. Bai J, Sata N, Nagai H: Gene expression analysis for predicting gemcitabine sensitivity in pancreatic cancer patients. HPB (Oxford); 2007;9(2):150-5
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  • [Title] Gene expression analysis for predicting gemcitabine sensitivity in pancreatic cancer patients.
  • This study investigated the use of gene expression data to predict the sensitivity of pancreatic cancers to gemcitabine.
  • MATERIALS AND METHODS: Cancer cells isolated from 14 pancreatic cancer patients were tested in vitro for gemcitabine sensitivity using the collagen droplet drug sensitivity test (CD-DST).
  • On the basis of this test, 9 of the 14 cancers were identified as either gemcitabine-sensitive or gemcitabine-resistant.
  • Total RNA was extracted from each of those nine cancers and used as a template to synthesize Cy3-labeled cDNA.
  • Pancreatic RNA extracted from six normal individuals was used as a control.
  • RESULTS: Statistical analysis of the microarray data showed that four genes were differentially expressed in gemcitabine-sensitive cancers: microsomal glutathione S-transferase 1 (GSTT1), topoisomerase II alpha (TOP2A), caspase 3, and ATP-binding cassette and subfamily C member 2 (ABCC2).
  • CONCLUSIONS: Expression of drug resistance-related genes appeared to predict whether a cancer was gemcitabine-sensitive or -resistant.

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  • (PMID = 18333132.001).
  • [ISSN] 1365-182X
  • [Journal-full-title] HPB : the official journal of the International Hepato Pancreato Biliary Association
  • [ISO-abbreviation] HPB (Oxford)
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Other-IDs] NLM/ PMC2020785
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76. Konduri S, Schwarz RE: Estrogen receptor beta/alpha ratio predicts response of pancreatic cancer cells to estrogens and phytoestrogens. J Surg Res; 2007 Jun 1;140(1):55-66
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  • [Title] Estrogen receptor beta/alpha ratio predicts response of pancreatic cancer cells to estrogens and phytoestrogens.
  • BACKGROUND: Reports on hormone receptor expression of pancreatic cancer (PaCa) cells and treatment responses to antihormonal therapy are conflicting.
  • We examined estrogen receptor (ER) expression in PaCa cells and investigated its function in estrogen-mediated cell proliferation.
  • Cell proliferation was measured by sulforhodamine B analysis.
  • ER modulators included diethylstilbestrol (DES), estradiol (E2), 4-hydroxytamoxifen (Tam), genistein (Gen), and Coumestrol (Coum).
  • RESULTS: ERalpha levels were detected in all eight, and ERbeta in seven cell lines.
  • Median maximal growth stimulation (in %, observed at 20 to 200 nM) was 19 (DES), 39 (E2), 20 (Tam), 22 (Gen), and -9 (Coum); median maximal inhibition (at 40 to 60 microM) was 59 (DES), 36 (E2), 25 (Tam), 43 (Gen), and 50 (Coum).
  • In 7/8 cell lines, ERbeta expression outweighs ERalpha expression.
  • [MeSH-major] Diethylstilbestrol / pharmacology. Estradiol / pharmacology. Estrogen Receptor alpha / metabolism. Estrogen Receptor beta / metabolism. Estrogens, Non-Steroidal / pharmacology. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Antimetabolites, Antineoplastic / toxicity. Antineoplastic Agents / pharmacology. Blotting, Western. Cell Division / drug effects. Cell Line, Tumor. Coumestrol / pharmacology. Deoxycytidine / analogs & derivatives. Deoxycytidine / toxicity. Estrogen Antagonists / pharmacology. Genistein / pharmacology. Humans. In Vitro Techniques. Predictive Value of Tests. Tamoxifen / analogs & derivatives. Tamoxifen / pharmacology

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  • (PMID = 17275032.001).
  • [ISSN] 0022-4804
  • [Journal-full-title] The Journal of surgical research
  • [ISO-abbreviation] J. Surg. Res.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antimetabolites, Antineoplastic; 0 / Antineoplastic Agents; 0 / Estrogen Antagonists; 0 / Estrogen Receptor alpha; 0 / Estrogen Receptor beta; 0 / Estrogens, Non-Steroidal; 094ZI81Y45 / Tamoxifen; 0W860991D6 / Deoxycytidine; 17197F0KYM / afimoxifene; 4TI98Z838E / Estradiol; 731DCA35BT / Diethylstilbestrol; B76N6SBZ8R / gemcitabine; DH2M523P0H / Genistein; V7NW98OB34 / Coumestrol
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77. Chen C, Yu Z: siRNA targeting HIF-1alpha induces apoptosis of pancreatic cancer cells through NF-kappaB-independent and -dependent pathways under hypoxic conditions. Anticancer Res; 2009 Apr;29(4):1367-72
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  • [Title] siRNA targeting HIF-1alpha induces apoptosis of pancreatic cancer cells through NF-kappaB-independent and -dependent pathways under hypoxic conditions.
  • OBJECTIVE: The primary objective was to explore the molecular mechanism of small interference RNA (siRNA) targeting hypoxic inducible factor-1alpha (HIF-1alpha) for inducing apoptosis of pancreatic cancer cells through a nuclear factor-kappaB (NF-kappaB)-independent or -dependent pathway under hypoxic conditions.
  • MATERIALS AND METHODS: A cassette encoding siRNA targeting HIF-1alpha mediated by recombinant adeno-associated virus (rAAV) was constructed, giving rAAV-siHIF. rAAV-siHIF or rAAV-hrGFP were transfected into exponentially growing MiaPaCa2 cells under hypoxic conditions.
  • The proliferation and apoptosis of MiaPaCa2 cells with or without PDTC, as an inhibitor of NF-kappaB, were investigated by MTT and TUNEL.
  • RESULTS: rAAV-siHIF inhibited the expression of HIF-1alpha mRNA and protein and the activity of NF-kappaB in MiaPaCa2 cells under hypoxic conditions.
  • At the same time, rAAV-siHIF decreased MiaPaCa2 cell proliferation and induced apoptosis, but these effects were not abrogated by PDTC.
  • Moreover, PDTC also inhibited MiaPaCa2 cell proliferation and induced apoptosis while rAAV-hrGFP did not have these effects.
  • CONCLUSION: Under hypoxic conditions, HIF-1alpha plays a key role in the proliferation of MiaPaCa2 cells and inhibition of HIF-1alpha expression may lead to MiaPaCa2 cell apoptosis through NF-kappaB-independent and -dependent pathways.
  • [MeSH-major] Apoptosis. Cell Hypoxia. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. NF-kappa B / metabolism. Pancreatic Neoplasms / pathology. RNA, Small Interfering / pharmacology
  • [MeSH-minor] Blotting, Western. Cell Proliferation. Dependovirus / genetics. Electrophoretic Mobility Shift Assay. Humans. In Situ Nick-End Labeling. RNA, Messenger / genetics. RNA, Messenger / metabolism. Reverse Transcriptase Polymerase Chain Reaction. Tumor Cells, Cultured

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  • (PMID = 19414389.001).
  • [ISSN] 0250-7005
  • [Journal-full-title] Anticancer research
  • [ISO-abbreviation] Anticancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Greece
  • [Chemical-registry-number] 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / NF-kappa B; 0 / RNA, Messenger; 0 / RNA, Small Interfering
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78. He Y, Liu XD, Chen ZY, Zhu J, Xiong Y, Li K, Dong JH, Li X: Interaction between cancer cells and stromal fibroblasts is required for activation of the uPAR-uPA-MMP-2 cascade in pancreatic cancer metastasis. Clin Cancer Res; 2007 Jun 1;13(11):3115-24
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  • [Title] Interaction between cancer cells and stromal fibroblasts is required for activation of the uPAR-uPA-MMP-2 cascade in pancreatic cancer metastasis.
  • PURPOSE: Interaction between tumor cells and surrounding stromal fibroblast (SF) plays a critical role in tumor growth and invasion.
  • The aim of the study is to determine the role of SF in regulating the invasive behaviors of pancreatic cancer by evaluating the mode of SF activating the urokinase plasminogen activator (uPA)-plasmin-matrix metalloproteinase (MMP)-2 cascade.
  • EXPERIMENTAL DESIGN: The expression patterns of uPA, MMP-2, and uPA receptor (uPAR) in human metastatic pancreatic cancer were analyzed by immunohistochemistry and the roles of SF in activation of the uPA-plasmin-MMP-2 cascade were evaluated by coculturing pancreatic cancer cell lines with SF.
  • RESULTS: uPA expression and fibroblastic uPAR expression were correlated with liver metastasis of human pancreatic cancer.
  • MMP-2 rather than MMP-9 was activated in the metastatic pancreatic cancer.
  • In the in vitro culture system, the coculture of peritumor fibroblasts with metastatic pancreatic cancer BxPc3 cells resulted in activation of MMP-2 and up-regulation of uPAR expression.
  • This activation required a direct interaction between SF and cancer cells.
  • In the coculture system, intergrin alpha(6)beta(1) expression was increased in BxPc3 cells, and blocking the function of integrin alpha(6)beta(1) decreased the activation of uPA and MMP-2.
  • This suggests that interaction between integrins of cancer cells and the uPARs of the SF might be involved in the activation of the uPAR-uPA-MMP-2 cascade.
  • CONCLUSION: Our results suggest that SF plays a role in promoting pancreatic cancer metastasis via activation of the uPA-plasminogen-MMP-2 cascade.
  • [MeSH-major] Fibroblasts / metabolism. Gene Expression Regulation, Neoplastic. Matrix Metalloproteinase 2 / metabolism. Neoplasms / metabolism. Pancreatic Neoplasms / metabolism. Pancreatic Neoplasms / pathology. Receptors, Cell Surface / metabolism. Urokinase-Type Plasminogen Activator / metabolism
  • [MeSH-minor] Aged. Cell Line, Tumor. Enzyme Activation. Humans. Integrin alpha6beta1 / metabolism. Middle Aged. Neoplasm Metastasis. Plasminogen / metabolism. Receptors, Urokinase Plasminogen Activator

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  • (PMID = 17545513.001).
  • [ISSN] 1078-0432
  • [Journal-full-title] Clinical cancer research : an official journal of the American Association for Cancer Research
  • [ISO-abbreviation] Clin. Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Integrin alpha6beta1; 0 / PLAUR protein, human; 0 / Receptors, Cell Surface; 0 / Receptors, Urokinase Plasminogen Activator; 9001-91-6 / Plasminogen; EC 3.4.21.73 / Urokinase-Type Plasminogen Activator; EC 3.4.24.24 / Matrix Metalloproteinase 2
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79. Mamaghani S, Patel S, Hedley DW: Glycogen synthase kinase-3 inhibition disrupts nuclear factor-kappaB activity in pancreatic cancer, but fails to sensitize to gemcitabine chemotherapy. BMC Cancer; 2009;9:132
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  • [Title] Glycogen synthase kinase-3 inhibition disrupts nuclear factor-kappaB activity in pancreatic cancer, but fails to sensitize to gemcitabine chemotherapy.
  • BACKGROUND: Aberrant activation NF-kappaB has been proposed as a mechanism of drug resistance in pancreatic cancer.
  • Recently, inhibition of glycogen synthase kinase-3 has been shown to exert anti-tumor effects on pancreatic cancer cells by suppressing NF-kappaB.
  • Consequently, we investigated whether inhibition of GSK-3 sensitizes pancreatic cancer cells to the chemotherapeutic agent gemcitabine.
  • METHODS: GSK-3 inhibition was achieved using the pharmacological agent AR-A014418 or siRNA against GSK-3 alpha and beta isoforms.
  • Cytotoxicity was measured using a Sulphorhodamine B assay and clonogenic survival following exposure of six different pancreatic cancer cell lines to a range of doses of either gemcitabine, AR-A014418 or both for 24, 48 and 72 h.
  • Basal and TNF-alpha induced activity of NF-kappaB was assessed using a luciferase reporter assay in the presence or absence of GSK-3 inhibition.
  • RESULTS: GSK-3 inhibition reduced both basal and TNF-alpha induced NF-kappaB luciferase activity.
  • Knockdown of GSK-3 beta reduced nuclear factor kappa B luciferase activity to a greater extent than GSK-3 alpha, and the greatest effect was seen with dual knockdown of both GSK-3 isoforms.
  • In all cell lines, treatment with either AR-A014418, or gemcitabine led to growth inhibition in a dose- and time-dependent manner.
  • CONCLUSION: GSK-3 inhibition has anticancer effects against pancreatic cancer cells with a range of genetic backgrounds associated with disruption of NF-kappaB, but does not significantly sensitize these cells to the standard chemotherapy agent gemcitabine.
  • This lack of synergy might be context or cell line dependent, but could also be explained on the basis that although NF-kappaB is an important mediator of pancreatic cancer cell survival, it plays a minor role in gemcitabine resistance.
  • Further work is needed to understand the mechanisms of this effect, including the potential for rational combination of GSK3 inhibitors with other targeted agents for the treatment of pancreatic cancer.
  • [MeSH-major] Deoxycytidine / analogs & derivatives. Down-Regulation. Glycogen Synthase Kinase 3 / metabolism. NF-kappa B / metabolism. Pancreatic Neoplasms / drug therapy. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Antineoplastic Agents / therapeutic use. Cell Line, Tumor. Humans. Protein Kinase Inhibitors / pharmacology. Tumor Necrosis Factor-alpha / genetics. Tumor Necrosis Factor-alpha / metabolism


80. Shen SG, Zhang D, Hu HT, Li JH, Wang Z, Ma QY: Effects of alpha-adrenoreceptor antagonists on apoptosis and proliferation of pancreatic cancer cells in vitro. World J Gastroenterol; 2008 Apr 21;14(15):2358-63
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  • [Title] Effects of alpha-adrenoreceptor antagonists on apoptosis and proliferation of pancreatic cancer cells in vitro.
  • AIM: To discuss the expression of alpha-adrenoreceptors in pancreatic cancer cell lines PC-2 and PC-3 and the effects of alpha1- and alpha2-adrenoreceptor antagonists, yohimbine and urapidil hydrochloride, on the cell lines in vitro.
  • METHODS: We cultured the human ductal pancreatic adenocarcinoma cell lines PC-2 and PC-3 and analyzed the mRNA expression of alpha1- and alpha2-adrenergic receptors by reverse transcription polymerase chain reaction (RT-PCR).
  • The effects of yohimbine and urapidil hydrochloride on cell proliferation were assessed by 3-(4,5-dimethylthiasol-2-yl)-2,4,-diphenyltetrazolium bromide (MTT) assay.
  • MTT assays showed that urapidil hydrochloride had no effect on PC-3 cell lines.
  • However, exposure to urapidil hydrochloride increased DNA synthesis in PC-2 cell lines as compared to the control group.
  • PC-2 cell lines were sensitive to both drugs.
  • The proliferation of the 2 cell lines was inhibited by yohimbine.
  • Cell proliferation was inhibited by yohimbine via apoptosis induction.
  • CONCLUSION: The expression of alpha1- and alpha2-adrenoreceptors is different in PC-2 and PC-3 cell lines, which might be indicative of their different functions.
  • The alpha2-adrenoceptor antagonist, yohimbine, can inhibit the proliferation of both cell lines and induce their apoptosis, suggesting that yohimbine can be used as an anticancer drug for apoptosis of PC-2 and PC-3 cells.
  • [MeSH-major] Adrenergic alpha-2 Receptor Antagonists. Adrenergic alpha-Antagonists / pharmacology. Antineoplastic Agents / pharmacology. Apoptosis / drug effects. Cell Proliferation / drug effects. Pancreatic Neoplasms / pathology. Yohimbine / pharmacology
  • [MeSH-minor] Adrenergic alpha-1 Receptor Antagonists. Cell Line, Tumor. DNA Replication / drug effects. Dose-Response Relationship, Drug. Flow Cytometry. Gene Expression Regulation, Neoplastic. Humans. In Situ Nick-End Labeling. Piperazines / pharmacology. RNA, Messenger / metabolism. Receptors, Adrenergic, alpha-1 / metabolism. Receptors, Adrenergic, alpha-2 / genetics. Receptors, Adrenergic, alpha-2 / metabolism. Reverse Transcriptase Polymerase Chain Reaction

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  • (PMID = 18416462.001).
  • [ISSN] 1007-9327
  • [Journal-full-title] World journal of gastroenterology
  • [ISO-abbreviation] World J. Gastroenterol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] China
  • [Chemical-registry-number] 0 / Adrenergic alpha-1 Receptor Antagonists; 0 / Adrenergic alpha-2 Receptor Antagonists; 0 / Adrenergic alpha-Antagonists; 0 / Antineoplastic Agents; 0 / Piperazines; 0 / RNA, Messenger; 0 / Receptors, Adrenergic, alpha-1; 0 / Receptors, Adrenergic, alpha-2; 2Y49VWD90Q / Yohimbine; A78GF17HJS / urapidil
  • [Other-IDs] NLM/ PMC2705090
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81. Bobarykina AY, Minchenko DO, Opentanova IL, Moenner M, Caro J, Esumi H, Minchenko OH: Hypoxic regulation of PFKFB-3 and PFKFB-4 gene expression in gastric and pancreatic cancer cell lines and expression of PFKFB genes in gastric cancers. Acta Biochim Pol; 2006;53(4):789-99
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  • [Title] Hypoxic regulation of PFKFB-3 and PFKFB-4 gene expression in gastric and pancreatic cancer cell lines and expression of PFKFB genes in gastric cancers.
  • Previously we have shown that hypoxia strongly induces the expression of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 and -4 (PFKFB-3 and PFKFB-4) genes in several cancer cell lines via a HIF-dependent mechanism.
  • In this paper we studied the expression and hypoxic regulation of PFKFB-4 and PFKFB-3 mRNA as well as its correlation with HIF-1alpha, HIF-2alpha, VEGF and Glut1 mRNA expression in the pancreatic cancer cell line Panc1 and two gastric cancer cell lines MKN45 and NUGC3.
  • This study clearly demonstrated that PFKFB-3 and PFKFB-4 mRNA are expresses in MKN45, NUGC3 and Panc1 cancers cells and that both genes are responsive to hypoxia in vitro.
  • However, their basal level of expression and hypoxia responsiveness vary in the different cells studied.
  • Particularly, PFKFB-3 mRNA is highly expressed in MKN45 and NUGC3 cancer cells, with the highest response to hypoxia in the NUGC3 cell line.
  • The PFKFB-4 mRNA has a variable low basal level of expression in both gastric and pancreatic cancer cell lines.
  • However, the highest hypoxia response of PFKFB-4 mRNA is found in the pancreatic cancer cell line Panc1.
  • The basal level of PFKFB-4 protein expression is the highest in NUGC3 gastric cancer cell line and lowest in Panc1 cells, with the highest response to hypoxia in the pancreatic cancer cell line.
  • Further studies showed that PFKFB-3 and PFKFB-4 gene expression was highly responsive to the hypoxia mimic dimethyloxalylglycine, a specific inhibitor of HIF-alpha hydroxylase enzymes, suggesting that the hypoxia responsiveness of PFKFB-3 and PFKFB-4 genes in these cell lines is regulated by the HIF transcription complex.
  • The expression of VEGF and Glut1, which are known HIF-dependent genes, is also strongly induced under hypoxic conditions in gastric and pancreatic cancer cell lines.
  • The levels of HIF-1alpha protein are increased in both gastric and pancreatic cancer cell lines under hypoxic conditions.
  • However, the basal level of HIF-1alpha as well as HIF-2alpha mRNA expression and their hypoxia responsiveness are different in the MKN45 and NUGC3 cancer cells.
  • Thus, the expression of HIF-1alpha mRNA is decreased in both gastric cancer cell lines treated by hypoxia or dimethyloxalylglycine, but HIF-2alpha mRNA expression is not changed significantly in NUGC3 and slightly increased in MKN45 cells.
  • Expression of PFKFB-4 and PFKFB-3 was also studied in gastric cancers and corresponding nonmalignant tissue counterparts from the same patients on both the mRNA and protein levels.
  • The expression of PFKFB-3 and PFKFB-4 mRNA as well as PFKFB-1 and PFKFB-2 mRNA was observed in normal human gastric tissue and was increased in malignant gastric tumors.
  • The basal level of PFKFB-4 protein expression in gastric cancers was much higher as compared to the PFKFB-3 isoenzyme.
  • In conclusion, this study provides evidence that PFKFB-4 and PFKFB-3 genes are also expressed in gastric and pancreatic cancer cells, they strongly respond to hypoxia via a HIF-1alpha dependent mechanism and, together with the expression of PFKFB-1 and PFKFB-2 genes, possibly have a significant role in the Warburg effect which is found in malignant cells.
  • [MeSH-major] Cell Hypoxia / physiology. Gene Expression Regulation, Enzymologic. Gene Expression Regulation, Neoplastic. Hypoxia-Inducible Factor 1, alpha Subunit / genetics. Pancreatic Neoplasms / metabolism. Phosphofructokinase-2 / genetics. Stomach Neoplasms / metabolism
  • [MeSH-minor] Basic Helix-Loop-Helix Transcription Factors / genetics. Cell Line, Tumor. Genes, Neoplasm. Glucose Transporter Type 1 / genetics. Humans. RNA, Messenger / analysis. Vascular Endothelial Growth Factor A / genetics

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  • (PMID = 17143338.001).
  • [ISSN] 0001-527X
  • [Journal-full-title] Acta biochimica Polonica
  • [ISO-abbreviation] Acta Biochim. Pol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] Poland
  • [Chemical-registry-number] 0 / Basic Helix-Loop-Helix Transcription Factors; 0 / Glucose Transporter Type 1; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / PFKFB4 protein, human; 0 / RNA, Messenger; 0 / Vascular Endothelial Growth Factor A; 0 / endothelial PAS domain-containing protein 1; EC 2.7.1.105 / PFKFB3 protein, human; EC 2.7.1.105 / Phosphofructokinase-2
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82. Jöst E, Roos WP, Kaina B, Schmidberger H: Response of pancreatic cancer cells treated with interferon-alpha or beta and co-exposed to ionising radiation. Int J Radiat Biol; 2010 Sep;86(9):732-41
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  • [Title] Response of pancreatic cancer cells treated with interferon-alpha or beta and co-exposed to ionising radiation.
  • PURPOSE: Clinical trials on pancreatic cancer demonstrated that interferons (IFN) improve the therapeutic index of combined radio- and chemotherapy.
  • This is believed to be due to radiosensitisation of cells, which, however, needs experimental verification.
  • MATERIALS AND METHODS: Here, we compared the survival response of ten pancreatic tumour cell lines following ionising radiation (IR), interferon-alpha (IFN-alpha), interferon-beta (IFN-beta) and combined treatment.
  • RESULTS: In most cell lines IFN treatment on its own exerted cytotoxicity, which was independent of the expression level of the IFN receptor on the cell surface.
  • Three cell lines showed a radiosensitisation effect while two showed radioprotection.
  • Although IFN-alpha is commonly used in the clinic, IFN-beta induced a stronger cytotoxic response than IFN-alpha in vitro.
  • The likely mechanism of enhancement of radiosensitivity in the responsive cell lines was shown to be an increase of the radiation-induced apoptotic response by IFN pretreatment.
  • CONCLUSIONS: Given that the in vitro data do not conform to the impressive clinical results observed after combined radio- and chemotherapy with IFN-alpha, it is reasonable to conclude that the sensitising effect of IFN is not mediated through modulating the intrinsic radiosensitivity of pancreatic cancer cells.
  • [MeSH-major] Interferon-alpha / pharmacology. Interferon-beta / pharmacology. Pancreatic Neoplasms / therapy
  • [MeSH-minor] Apoptosis / radiation effects. Cell Line, Tumor. Combined Modality Therapy. Humans. Radiation-Protective Agents / pharmacology. Radiation-Sensitizing Agents / pharmacology

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  • (PMID = 20586542.001).
  • [ISSN] 1362-3095
  • [Journal-full-title] International journal of radiation biology
  • [ISO-abbreviation] Int. J. Radiat. Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Interferon-alpha; 0 / Radiation-Protective Agents; 0 / Radiation-Sensitizing Agents; 77238-31-4 / Interferon-beta
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83. Baker AF, Koh MY, Williams RR, James B, Wang H, Tate WR, Gallegos A, Von Hoff DD, Han H, Powis G: Identification of thioredoxin-interacting protein 1 as a hypoxia-inducible factor 1alpha-induced gene in pancreatic cancer. Pancreas; 2008 Mar;36(2):178-86
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  • [Title] Identification of thioredoxin-interacting protein 1 as a hypoxia-inducible factor 1alpha-induced gene in pancreatic cancer.
  • OBJECTIVE: To investigate the expression of thioredoxin-interacting protein (TXNIP) during hypoxia and its dependency on hypoxia-inducible factor 1alpha (HIF-1alpha) in pancreatic cancer cell lines.
  • METHODS: MiaPaCa-2 pancreatic cancer cells were transiently transfected with siRNA to HIF-1alpha and TXNIP protein measured after growth in normoxia or hypoxia.
  • In addition, HIF-1alpha dependency was assessed by transiently transfecting MiaPaCa-2 pancreatic cancer cells with HIF-1alpha with a mutated oxygen degradation domain resulting in stable HIF-1alpha expression in normoxic conditions.
  • Panc-1 pancreatic cancer cells with low endogenous TXNIP expression were stably transfected with TXNIP, and cell survival and response to platinum cancer agents were tested.
  • Quantitative immunohistochemistry was utilized to measure the expression of TXNIP and thioredoxin 1 in human pancreatic cancer tissues.
  • RESULTS: Thioredoxin-interacting protein was induced during hypoxia in pancreatic cancer cells in a HIF-1alpha-dependent manner.
  • Overexpression of TXNIP in the Panc-1 cells resulted in a higher basal apoptosis and increased sensitivity to cisplatin and oxaliplatin.
  • A negative correlation was observed between TXNIP and thioredoxin 1 expression in human pancreatic cancer tissues.
  • CONCLUSIONS: Thioredoxin-interacting protein, a putative tumor suppressor gene, is induced in response to hypoxia in a HIF-1alpha-dependent manner in pancreatic cancer cells, resulting in increased apoptosis and increased sensitivity to platinum anticancer therapy.
  • [MeSH-major] Carcinoma, Pancreatic Ductal / metabolism. Carrier Proteins / metabolism. Gene Expression Regulation, Neoplastic. Hypoxia-Inducible Factor 1, alpha Subunit / metabolism. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Antineoplastic Agents / pharmacology. Antineoplastic Agents / therapeutic use. Apoptosis. Cell Hypoxia. Cell Line, Tumor. Cell Survival / drug effects. Cisplatin / pharmacology. Cisplatin / therapeutic use. Humans. Immunohistochemistry. Mutation. Organoplatinum Compounds / pharmacology. Organoplatinum Compounds / therapeutic use. RNA Interference. RNA, Small Interfering / metabolism. Thioredoxins / metabolism. Tissue Array Analysis. Transfection. Up-Regulation

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  • (PMID = 18376310.001).
  • [ISSN] 1536-4828
  • [Journal-full-title] Pancreas
  • [ISO-abbreviation] Pancreas
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA077204; United States / NCI NIH HHS / CA / CA109552; United States / NCI NIH HHS / CA / CA90821
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antineoplastic Agents; 0 / Carrier Proteins; 0 / HIF1A protein, human; 0 / Hypoxia-Inducible Factor 1, alpha Subunit; 0 / Organoplatinum Compounds; 0 / RNA, Small Interfering; 0 / TXN protein, human; 0 / TXNIP protein, human; 04ZR38536J / oxaliplatin; 52500-60-4 / Thioredoxins; Q20Q21Q62J / Cisplatin
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84. Grzesiak JJ, Bouvet M: Activation of the alpha2beta1 integrin-mediated malignant phenotype on type I collagen in pancreatic cancer cells by shifts in the concentrations of extracellular Mg2+ and Ca2+. Int J Cancer; 2008 May 15;122(10):2199-209
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  • [Title] Activation of the alpha2beta1 integrin-mediated malignant phenotype on type I collagen in pancreatic cancer cells by shifts in the concentrations of extracellular Mg2+ and Ca2+.
  • The authors have previously demonstrated that alpha(2)beta(1) integrin-mediated pancreatic cancer cell adhesion to Type I collagen is Mg(2+)-dependent, inhibited by Ca(2+), and that this integrin, purified from cell lysates using Type I-collagen-sepharose in Mg(2+), can be eluted with Ca(2+).
  • In the present study, the authors examined the divalent cation-dependency of alpha(2)beta(1) integrin-mediated pancreatic cancer cell adhesion, migration and proliferation on Type I collagen, an extracellular matrix protein shown to be highly up-regulated, and to promote the malignant phenotype in vitro and in vivo.
  • The results indicate that cells attach to Type I collagen maximally when Mg(2+) is greater than 1 mM, and that addition of increasing concentrations of Ca(2+) reduces this adhesion.
  • These effects are reversible, in that previous cell attachment in Mg(2+) can be reversed by adding Ca(2+), and vice versa.
  • They also demonstrate that pancreatic cancer cells migrate and proliferate on Type I collagen in Mg(2+) alone, but maximally when Mg(2+) is present at concentrations that promote maximal cell adhesion and Ca(2+) is present at concentrations less than Mg(2+).
  • Cell adhesion and proliferation assays, as well as affinity chromatography on Type I collagen using anti-integrin function-blocking monoclonal antibodies indicate that the effects of these divalent cation shifts are mediated specifically by the alpha(2)beta(1) integrin.
  • As pancreatic juice contains over 1,200-fold more Mg(2+) than Ca(2+) and solid tumors are characterized by increased magnesium load, these data indicate that such pathophysiological divalent cation shifts could be involved in the activation of the alpha(2)beta(1) integrin-mediated malignant phenotype on Type I collagen in the pancreatic cancer.
  • [MeSH-major] Calcium / metabolism. Collagen Type I / metabolism. Integrin alpha2beta1 / metabolism. Magnesium / metabolism. Pancreatic Neoplasms / metabolism
  • [MeSH-minor] Cell Adhesion / physiology. Cell Movement. Cell Proliferation. Chromatography, Affinity. Humans. Immunoblotting. Phenotype. Tumor Cells, Cultured

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  • [Copyright] (c) 2008 Wiley-Liss, Inc.
  • (PMID = 18224679.001).
  • [ISSN] 1097-0215
  • [Journal-full-title] International journal of cancer
  • [ISO-abbreviation] Int. J. Cancer
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA109949-01
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Collagen Type I; 0 / Integrin alpha2beta1; I38ZP9992A / Magnesium; SY7Q814VUP / Calcium
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85. Li W, Xie L, Chen Z, Zhu Y, Sun Y, Miao Y, Xu Z, Han X: Cantharidin, a potent and selective PP2A inhibitor, induces an oxidative stress-independent growth inhibition of pancreatic cancer cells through G2/M cell-cycle arrest and apoptosis. Cancer Sci; 2010 May;101(5):1226-33
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  • [Title] Cantharidin, a potent and selective PP2A inhibitor, induces an oxidative stress-independent growth inhibition of pancreatic cancer cells through G2/M cell-cycle arrest and apoptosis.
  • It is a potent and selective inhibitor of protein phosphatase 2A (PP2A) that plays an important role in control of cell cycle, apoptosis, and cell-fate determination.
  • In the present study, we investigated the therapeutic potential of cantharidin in pancreatic cancer.
  • Cantharidin efficiently inhibited the growth of pancreatic cancer cells, but presented a much lighter toxicity effect against normal pancreatic duct cells.
  • It caused G2/M cell-cycle arrest that was accompanied by the down-regulation of cyclin-dependent kinase 1 (CDK1) and up-regulation of p21 expression.
  • It induced apoptosis and elevated the expressions of pro-apoptotic factors tumor necrosis factor-alpha (TNF-alpha), TNF-related apoptosis inducing receptor 1 (TRAILR1), TRAILR2, Bad, Bak, and Bid, and decreased the expression of anti-apoptotic Bcl-2.
  • Interestingly, unlike previous studies on other cancer cells, we found that the inhibitory role of cantharidin is independent of oxidative stress in pancreatic cancer cells.
  • Hence, in addition to being an attractive candidate compound with therapeutic potential, cantharidin also highlighted the possibility of using PP2A as a therapeutic target for pancreatic cancer treatment.
  • [MeSH-major] Apoptosis / drug effects. Cantharidin / pharmacology. Cell Division / drug effects. Enzyme Inhibitors / pharmacology. G2 Phase / drug effects. Oxidative Stress / drug effects. Pancreatic Neoplasms / drug therapy. Protein Phosphatase 2 / antagonists & inhibitors
  • [MeSH-minor] Cell Line, Tumor. Cell Proliferation / drug effects. Humans. JNK Mitogen-Activated Protein Kinases / physiology


86. Vitale G, van Eijck CH, van Koetsveld Ing PM, Erdmann JI, Speel EJ, van der Wansem Ing K, Mooij DM, Colao A, Lombardi G, Croze E, Lamberts SW, Hofland LJ: Type I interferons in the treatment of pancreatic cancer: mechanisms of action and role of related receptors. Ann Surg; 2007 Aug;246(2):259-68
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  • [Title] Type I interferons in the treatment of pancreatic cancer: mechanisms of action and role of related receptors.
  • OBJECTIVE: We evaluated the role of type I interferons (IFNs) and IFN receptors in the regulation of cell growth in 3 human pancreatic adenocarcinoma cell lines (BxPC-3, MiaPaCa-2, and Panc-1).
  • BACKGROUND: Chemotherapy and radiotherapy have a marginal role in the management of pancreatic adenocarcinoma.
  • The addition of IFN-alpha showed promising results in early clinical trials.
  • METHODS: Cell proliferation and apoptosis were evaluated by DNA measurement and DNA fragmentation, respectively.
  • Type I IFN receptor (IFNAR-1 and IFNAR-2 subunits) was determined by quantitative RT-PCR and immunocytochemistry.
  • Cell cycle distribution was evaluated by propidium iodide staining and flow-cytometric analysis.
  • The inhibitory effect of IFN-beta was stronger than IFN-alpha in all 3 cell lines and mainly modulated by the stimulation of apoptosis, although cell cycle arrest was induced as well.
  • The expression of the type I IFN receptors was significantly higher in BxPC-3 (the most sensitive cell line to IFN) and mainly localized on the membrane, whereas in Panc-1 (the most resistant cell line) about 60% to 70% of cells were negative for IFNAR-2c with a mainly cytoplasmic staining for IFNAR-2c.
  • CONCLUSION: The antitumor activity of IFN-beta is more potent than IFN-alpha in pancreatic cancer cell lines through the induction of apoptosis.
  • Further studies should investigate in vivo whether the intensity and distribution of IFNAR-1 and IFNAR-2c may predict the response to therapy with IFN-alpha and IFN-beta in pancreatic cancer.
  • [MeSH-major] Adenocarcinoma / drug therapy. Gene Expression Regulation, Neoplastic. Interferon Type I / therapeutic use. Pancreatic Neoplasms / drug therapy. RNA, Messenger / genetics. Receptor, Interferon alpha-beta / genetics
  • [MeSH-minor] Antineoplastic Agents / therapeutic use. Apoptosis / drug effects. Biomarkers, Tumor / biosynthesis. Biomarkers, Tumor / genetics. Cell Line, Tumor. Cell Proliferation / drug effects. Flow Cytometry. Humans. Immunohistochemistry. Prognosis. Reverse Transcriptase Polymerase Chain Reaction

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