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Items 1 to 100 of about 1732
1. Serdar A, Basak D, Sercan G, Ali V: Solitary amyloid tumor of the tongue base. Int J Otolaryngol; 2009;2009:515068

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Solitary amyloid tumor of the tongue base.
  • The purpose of this article is to present a rare case of localized, solitary amyloid tumor of tongue base and emphasize some of the characteristic features of challenging clinical and histopathologic diagnosis.
  • In this paper, we focused on the clinical and pathological specifications of this rare tumor, so any unnecessary examinations or measures may be spared.
  • Negative staining of amyloid material with AAC and osseous metaplasia noted in the histopathologic examination may not be thought as definite criteria for localized amyloidosis, but a supporter of localized, solitary amyloid tumor diagnosis.

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  • [Cites] Diagn Cytopathol. 2001 Mar;24(3):181-5 [11241901.001]
  • [Cites] Oral Oncol. 2006 Apr;42(4):421-9 [16488655.001]
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  • [Cites] Diagn Cytopathol. 1993 Oct;9(5):570-5 [8287770.001]
  • (PMID = 20107570.001).
  • [ISSN] 1687-921X
  • [Journal-full-title] International journal of otolaryngology
  • [ISO-abbreviation] Int J Otolaryngol
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Other-IDs] NLM/ PMC2809435
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2. Dhamija B, Hassan MF, Thambinayagam H, Moore A, Adams W, Hilton D: Intracranial Aspergillus infection associated with an amyloid tumor and lymphoma. Skull Base; 2008 Nov;18(6):405-9

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Intracranial Aspergillus infection associated with an amyloid tumor and lymphoma.
  • We illustrate the case in a patient who developed right-sided visual disturbance and facial paresthesia, where radiological diagnosis was meningioma but histopathology revealed an amyloid tumor with synchronous aspergillus infection and lymphoma at the same site.

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  • (PMID = 19412411.001).
  • [ISSN] 1531-5010
  • [Journal-full-title] Skull base : official journal of North American Skull Base Society ... [et al.]
  • [ISO-abbreviation] Skull Base
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Other-IDs] NLM/ PMC2637077
  • [Keywords] NOTNLM ; Intracranial aspergillosis / amyloid / lymphoma / meningioma / skull base
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3. Oyasiji T, Yood S: Jejunal Amyloidoma - a rare cause of gastrointestinal bleeding. Cases J; 2009;2:9100

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • We report a case of localized amyloid tumor of the jejunum which presented with abdominal pain and gastrointestinal bleeding.
  • We reviewed the pathophysiologic process that precipitates bleeding in this rare tumor.
  • All with a view to add to the growing evidence on this rare tumor which will facilitate accurate diagnosis and management.

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  • [Cites] Br J Radiol. 2008 Jan;81(961):e1-3 [18079343.001]
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  • (PMID = 20062677.001).
  • [ISSN] 1757-1626
  • [Journal-full-title] Cases journal
  • [ISO-abbreviation] Cases J
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Other-IDs] NLM/ PMC2803897
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4. Losanoff JE, Antaki F, Salwen WA, Edelman D, Reddy A, Levi E, Basson MD: Amyloid tumor of the stomach simulating an obstructing gastric carcinoma: case report and review of the literature. Endoscopy; 2009;41 Suppl 2:E45-6
The Weizmann Institute of Science GeneCards and MalaCards databases. gene/protein/disease-specific - MalaCards for amyloid tumor .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid tumor of the stomach simulating an obstructing gastric carcinoma: case report and review of the literature.

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  • (PMID = 19288419.001).
  • [ISSN] 1438-8812
  • [Journal-full-title] Endoscopy
  • [ISO-abbreviation] Endoscopy
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] Germany
  • [Number-of-references] 5
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5. Tutar E, Onat AM, Aydin A, Kervancioğlu S, Buyukhatipoglu H, Inan G, Pehlivan Y: Amyloid tumor of the breast mimicking breast carcinoma. South Med J; 2008 Feb;101(2):199-201
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  • [Title] Amyloid tumor of the breast mimicking breast carcinoma.
  • Amyloid tumors of the breast are extremely rare.
  • Amyloid involvement of the breast has no specific diagnostic features on mammography; on occasion, this causes diagnostic challenges.
  • In this paper, the case of a 58-year-old woman with an amyloid tumor of the breast, which developed secondary to long-standing rheumatoid arthritis, is presented.

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  • (PMID = 18364625.001).
  • [ISSN] 1541-8243
  • [Journal-full-title] Southern medical journal
  • [ISO-abbreviation] South. Med. J.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
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6. Nelson TJ, Alkon DL: Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide. J Biol Chem; 2005 Feb 25;280(8):7377-87
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide.
  • Alzheimer's disease (AD) is characterized by accumulation of the neurotoxic peptide beta-amyloid, which is produced by proteolysis of amyloid precursor protein (APP).
  • APP is a large membrane-bound copper-binding protein that is essential in maintaining synaptic function and may play a role in synaptogenesis. beta-Amyloid has been shown to contribute to the oxidative stress that accompanies AD.
  • However, the biochemical function of APP and the mechanism of the toxicity of beta-amyloid are still unclear.
  • In this study, we show that both beta-amyloid and APP can oxidize cholesterol to form 7beta-hydroxycholesterol, a proapoptotic oxysterol that was neurotoxic at nanomolar concentrations.
  • 7beta-Hydroxycholesterol inhibited secretion of soluble APP from cultured rat hippocampal H19-7/IGF-IR neuronal cells and inhibited tumor necrosis factor-alpha-converting enzyme alpha-secretase activity but had no effect on beta-site APP-cleaving enzyme 1 activity.
  • The rate of reaction between cholesterol and beta-amyloid was comparable to the rates of cholesterol-metabolizing enzymes (k(cat) = 0.211 min(-)1).
  • The rate of production of 7beta-hydroxycholesterol by APP was approximately 200 times lower than by beta-amyloid.
  • Higher levels produced by beta-amyloid could contribute to the oxidative stress and cell loss observed in Alzheimer's disease.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Amyloid beta-Protein Precursor / metabolism. Cholesterol / metabolism
  • [MeSH-minor] ADAM Proteins. Alzheimer Disease / etiology. Amyloid Precursor Protein Secretases. Animals. Aspartic Acid Endopeptidases / antagonists & inhibitors. Brain. Cell Line. Endopeptidases. Guinea Pigs. Hippocampus / cytology. Humans. Hydroxycholesterols / pharmacology. Kinetics. Metalloendopeptidases / antagonists & inhibitors. Neurons / drug effects. Neurons / metabolism. Neurons / secretion. Oxidation-Reduction. Oxidative Stress. Rats

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  • (PMID = 15591071.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Hydroxycholesterols; 566-26-7 / cholest-5-en-3 beta,7 alpha-diol; 97C5T2UQ7J / Cholesterol; EC 3.4.- / Amyloid Precursor Protein Secretases; EC 3.4.- / Endopeptidases; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC 3.4.23.46 / BACE1 protein, human; EC 3.4.23.46 / Bace protein, rat; EC 3.4.24.- / ADAM Proteins; EC 3.4.24.- / Metalloendopeptidases; EC 3.4.24.- / tumor necrosis factor-alpha convertase
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7. Andrade GC, Silveira RL, Pinheiro N Jr, Rocha EM, Pittella JE: [Cerebral amyloid angiopathy presenting as a brain tumor: case report]. Arq Neuropsiquiatr; 2006 Mar;64(1):153-6
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  • [Title] [Cerebral amyloid angiopathy presenting as a brain tumor: case report].
  • [Transliterated title] Angiopatia amilóide cerebral simulando tumor cerebral: relato de caso.
  • We describe the unusual case of a 45-year-old male patient harboring an intracranial mass due to cerebral amyloid angiopathy whose clinical and radiological features were those of a low grade glioma.
  • Biopsy revealed cerebral amyloid angiopathy.
  • [MeSH-major] Brain Neoplasms / pathology. Cerebral Amyloid Angiopathy / pathology. Glioma / pathology

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  • (PMID = 16622576.001).
  • [ISSN] 0004-282X
  • [Journal-full-title] Arquivos de neuro-psiquiatria
  • [ISO-abbreviation] Arq Neuropsiquiatr
  • [Language] por
  • [Publication-type] Case Reports; English Abstract; Journal Article
  • [Publication-country] Brazil
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8. Kanapathipillai M, Lentzen G, Sierks M, Park CB: Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's beta-amyloid. FEBS Lett; 2005 Aug 29;579(21):4775-80
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's beta-amyloid.
  • beta-Amyloid peptide (Abeta) is the major constituent of senile plaques, the key pathological feature of Alzheimer's disease.
  • [MeSH-major] Alzheimer Disease / metabolism. Amino Acids, Diamino / metabolism. Amyloid beta-Peptides / metabolism. Amyloid beta-Peptides / toxicity. Peptide Fragments / metabolism. Peptide Fragments / toxicity
  • [MeSH-minor] Aged. Cell Line, Tumor. Cell Survival. Humans. Microscopy, Atomic Force. Molecular Structure. Neuroblastoma

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  • (PMID = 16098972.001).
  • [ISSN] 0014-5793
  • [Journal-full-title] FEBS letters
  • [ISO-abbreviation] FEBS Lett.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amino Acids, Diamino; 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / amyloid beta-protein (1-42); 0 / hydroxyectoine; 7GXZ3858RY / ectoine
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9. Okuda I, Ubara Y, Takaichi K, Kitajima I, Motoi N, Hara S, Kokubo T: Genital beta2-microglobulin amyloidoma in a long-term dialysis patient. Am J Kidney Dis; 2006 Sep;48(3):e35-9
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  • We present the case of a 58-year-old Japanese woman with a huge amyloid tumor in the genital region.
  • From 1989 to 1991, carpal tunnel decompression was performed surgically, and beta(2)-microglobulin (beta2MG)-amyloid deposition was found in the wrists.
  • A biopsy specimen of the mass obtained by using a transvaginal approach showed material that was positive for beta2MG-amyloid immunohistologically.

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  • (PMID = 16931206.001).
  • [ISSN] 1523-6838
  • [Journal-full-title] American journal of kidney diseases : the official journal of the National Kidney Foundation
  • [ISO-abbreviation] Am. J. Kidney Dis.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / beta 2-Microglobulin
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10. Cheng JY, Fong KS, Cheah ES, Choo CT: Lacrimal gland amyloidosis. Ophthal Plast Reconstr Surg; 2006 Jul-Aug;22(4):306-8
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  • This report describes two patients with amyloid tumor of the lacrimal gland.

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  • (PMID = 16855510.001).
  • [ISSN] 0740-9303
  • [Journal-full-title] Ophthalmic plastic and reconstructive surgery
  • [ISO-abbreviation] Ophthal Plast Reconstr Surg
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
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11. Maheshwari AV, Muro-Cacho CA, Kransdorf MJ, Temple HT: Soft-tissue amyloidoma of the extremities: a case report and review of literature. Skeletal Radiol; 2009 Mar;38(3):287-92
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  • The least common presentation of an amyloid deposition is as a discrete mass called amyloidoma or amyloid tumor.

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  • (PMID = 19050870.001).
  • [ISSN] 0364-2348
  • [Journal-full-title] Skeletal radiology
  • [ISO-abbreviation] Skeletal Radiol.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article; Review
  • [Publication-country] Germany
  • [Number-of-references] 29
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12. Markert E, Gruber-Moesenbacher U, Porubsky C, Popper HH: Lung osteoma--a new benign lung lesion. Virchows Arch; 2006 Jul;449(1):117-20
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • Tumors with osseous elements can be found, such as hamartoma and amyloid tumor, and reactive lesions such as osseous metaplasia.
  • A 39-year-old male patient was treated for multiple myeloma and got a bone marrow transplantation 2 years and a few months before he presented with a solitary well-circumscribed tumor in the right middle lobe.
  • The tumor presented with a fibrous capsule and consisted of mature bone trabecules.
  • Within the tumor, fatty tissue was seen.
  • No amyloid deposition, no immature epithelial tubules as in hamartomas, and no normal lung structure as in osseous metaplasia were seen.
  • This tumor might have been induced by circulating stem cells; however, due to autologous bona marrow transplantation, this cannot be proven.
  • [MeSH-minor] Adult. Biomarkers, Tumor / analysis. Bone Marrow Transplantation. Diagnosis, Differential. Hamartoma / diagnosis. Humans. Immunohistochemistry. Male. Multiple Myeloma / pathology. Multiple Myeloma / therapy. Osteonectin / analysis

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  • (PMID = 16639606.001).
  • [ISSN] 0945-6317
  • [Journal-full-title] Virchows Archiv : an international journal of pathology
  • [ISO-abbreviation] Virchows Arch.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Biomarkers, Tumor; 0 / Osteonectin
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13. Hawke D, Mazouni C, André F, Baggerly K, Baggerly K, Tsavachidis S, Buzdar AU, Martin P, Kobayashi R, Pusztai L: Evaluation of serum profiles changes after neoadjuvant chemotherapy for breast cancer using MALDI-TOF/MS procedure. J Clin Oncol; 2009 May 20;27(15_suppl):e22072

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • Four in tumors with pCR (AFM, C3, hemopexin, SAP) and four proteins in the RD group were identified (AP1, hemopexin, Complement B, amyloid P component) Conclusions: Our study suggests that MALDI mass spectrometry may be used to predict the tumor response to neoadjuvant chemotherapy.

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  • (PMID = 27963214.001).
  • [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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14. Bisceglia M, Spagnolo D, Galliani C, Fisher C, Suster S, Kazakov DV, Cooper K, Michal M: Tumoral, quasitumoral and pseudotumoral lesions of the superficial and somatic soft tissue: new entities and new variants of old entities recorded during the last 25 years. Part XII: appendix. Pathologica; 2006 Aug;98(4):239-98

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • Detailed clinicomorphological and differential diagnostic features of approximately sixty entities were chosen on the basis of their clinical significance and morphologic distinctiveness.
  • The series included fibrous and myofibroblastic tumors (e.g. solitary fibrous tumor, high grade classic and pigmented dermatofibrosarcoma protuberans, inflammatory myofibroblastic tumor and myofibrosarcomas), fibromyxoid and fibrohistiocytic neoplasms (e.g., Evans' tumor, phosphaturic mesenchymal tumor, inflammatory myxohyaline tumor), special adipocytic/vascular/and smooth muscle lesions (e.g., chondroid lipoma, Dabska's tumor, ST hemangioblastoma, lipoleiomyosarcoma), epithelioid mesenchymal malignancies of diverse lineages (e.g., epithelioid liposarcoma, proximal-type epithelioid sarcoma, neuroendocrine extraskeletal chondromyxoid sarcoma), ST Ewing's tumor and peripheral nerve sheath tumors (perineuriomas and pigmented and rosetting tumors of the schwannoma/neurofibroma group), extranodal dendritic or histiocytic proliferative processes (follicular dendritic cell sarcoma, Rosai-Dorfman disease, Castleman's disease, and plexiform xanthomatous tumor), and tumors with myoepithelial differentiation.
  • The section devoted to selected pseudotumoral entities considered representatives of the hamartoma group (neural fibrolipomatous hamartoma, ectopic hamartomatous thymoma, rudimentary meningocele), metabolic diseases (amyloid tumor, nephrogenic fibrosing dermopathy, tophaceous pseudogout, pseudoinfiltrative parathyromatosis), stromal tissue reactions to trauma (fibroosseous pseudotumors of digits) and infections (bacillary angiomatosis), and normal organs (glomus coccygeum).

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  • (PMID = 17175794.001).
  • [ISSN] 0031-2983
  • [Journal-full-title] Pathologica
  • [ISO-abbreviation] Pathologica
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] Italy
  • [Number-of-references] 272
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15. Hirayama K, Miyasho T, Ohmachi T, Watanabe T, Yokota H, Taniyama H: Biochemical and immunohistochemical characterization of the amyloid in canine amyloid-producing odontogenic tumor. Vet Pathol; 2010 Sep;47(5):915-22

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Biochemical and immunohistochemical characterization of the amyloid in canine amyloid-producing odontogenic tumor.
  • The amyloid of canine amyloid-producing odontogenic tumor (APOT) was evaluated biochemically and immunohistochemically.
  • The N-terminal amino-acid sequence of purified amyloid protein from a canine APOT was strikingly similar to the sequence in both rat ameloblastin and porcine sheathlin.
  • Immunohistochemically, the amyloid in APOT from 9 dogs was strongly reactive with anti-rat ameloblastin, anti-porcine sheathlin, and anti-canine APOT amyloid and weakly reactive with anti-porcine amelogenin but negative for antibodies to cytokeratins, vimentin, desmin, alpha-smooth muscle actin, amyloid A, glial fibrillary acidic protein, or S100 protein.
  • The neoplastic epithelial cells of APOT were focally reactive with antibodies to ameloblastin, sheathlin, amelogenin, and canine APOT amyloid.
  • The similarity in amino-acid sequence of the amyloid protein of canine APOT to that of enamel proteins, such as ameloblastin, sheathlin, and amelogenin, and the expression of these antigens in both APOT amyloid and in the neoplastic cells suggest that the amyloid of canine APOT is derived from enamel proteins secreted by ameloblasts.
  • [MeSH-major] Amyloid / isolation & purification. Dog Diseases / pathology. Odontogenic Tumors / veterinary

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  • (PMID = 20651064.001).
  • [ISSN] 1544-2217
  • [Journal-full-title] Veterinary pathology
  • [ISO-abbreviation] Vet. Pathol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid
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16. Matharu B, Gibson G, Parsons R, Huckerby TN, Moore SA, Cooper LJ, Millichamp R, Allsop D, Austen B: Galantamine inhibits beta-amyloid aggregation and cytotoxicity. J Neurol Sci; 2009 May 15;280(1-2):49-58
Hazardous Substances Data Bank. GALANTAMINE .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Galantamine inhibits beta-amyloid aggregation and cytotoxicity.
  • The ability of galantamine (Reminyl) to inhibit the aggregation and toxicity of the beta-amyloid peptide (Abeta) was investigated.
  • [MeSH-major] Amyloid beta-Peptides / drug effects. Cholinesterase Inhibitors / pharmacology. Galantamine / pharmacology. Neuroprotective Agents / pharmacology. Peptide Fragments / drug effects
  • [MeSH-minor] Analysis of Variance. Apoptosis / drug effects. Cell Line, Tumor. Dose-Response Relationship, Drug. Enzyme-Linked Immunosorbent Assay. Humans. L-Lactate Dehydrogenase / metabolism. Microscopy, Electron. Models, Molecular. Nuclear Magnetic Resonance, Biomolecular

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  • (PMID = 19249060.001).
  • [ISSN] 1878-5883
  • [Journal-full-title] Journal of the neurological sciences
  • [ISO-abbreviation] J. Neurol. Sci.
  • [Language] eng
  • [Grant] United Kingdom / Wellcome Trust / / 066268/Z/01/Z
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Cholinesterase Inhibitors; 0 / Neuroprotective Agents; 0 / Peptide Fragments; 0 / amyloid beta-protein (1-40); 0 / amyloid beta-protein (1-42); 0D3Q044KCA / Galantamine; EC 1.1.1.27 / L-Lactate Dehydrogenase
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17. Uberti D, Bianchi I, Olivari L, Ferrari-Toninelli G, Canonico P, Memo M: Pramipexole prevents neurotoxicity induced by oligomers of beta-amyloid. Eur J Pharmacol; 2007 Aug 27;569(3):194-6

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Pramipexole prevents neurotoxicity induced by oligomers of beta-amyloid.
  • Here we demonstrate that pramipexole, an antiparkinsonian dopamine receptor agonist drug, exerts neuroprotective effects against beta-amyloid neurotoxicity.
  • Using a specific protocol to test individually oligomers, fibrils, or unaggregated amyloid beta-peptide, we found pramipexole able to protect cells against oligomers and fibrils.
  • Unaggregated amyloid beta-peptide was found unable to cause cell death.
  • We propose pramipexole may become in the future a coadjuvant in the treatment of neuropathologies, besides Parkinson's disease, where amyloid beta-peptide-mediated oxidative injury exerts a relevant role.
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Benzothiazoles / pharmacology. Dopamine Agonists / pharmacology. Neuroprotective Agents / pharmacology. Peptide Fragments / toxicity
  • [MeSH-minor] Amyloid / drug effects. Amyloid / toxicity. Antiparkinson Agents / administration & dosage. Antiparkinson Agents / pharmacology. Cell Death / drug effects. Cell Line, Tumor. Cell Survival / drug effects. Dose-Response Relationship, Drug. Free Radicals / metabolism. Humans. Neuroblastoma / metabolism. Reactive Oxygen Species / metabolism

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  • (PMID = 17572405.001).
  • [ISSN] 0014-2999
  • [Journal-full-title] European journal of pharmacology
  • [ISO-abbreviation] Eur. J. Pharmacol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid; 0 / Amyloid beta-Peptides; 0 / Antiparkinson Agents; 0 / Benzothiazoles; 0 / Dopamine Agonists; 0 / Free Radicals; 0 / Neuroprotective Agents; 0 / Peptide Fragments; 0 / Reactive Oxygen Species; 0 / amyloid beta-protein (1-42); 83619PEU5T / pramipexole
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18. Wang Q, Wu J, Rowan MJ, Anwyl R: Beta-amyloid inhibition of long-term potentiation is mediated via tumor necrosis factor. Eur J Neurosci; 2005 Dec;22(11):2827-32
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Beta-amyloid inhibition of long-term potentiation is mediated via tumor necrosis factor.
  • A number of recent studies have shown that beta-amyloid (Abeta) inhibits the induction of long-term potentiation (LTP) in the hippocampus.
  • In the present study, we present evidence that the cytokine tumor necrosis factor (TNF) alpha has a key role in the Abeta inhibition of LTP.
  • [MeSH-major] Amyloid beta-Peptides / pharmacology. Long-Term Potentiation / drug effects. Tumor Necrosis Factor-alpha / pharmacology
  • [MeSH-minor] Animals. Electric Stimulation. Electrophysiology. In Vitro Techniques. Male. Membrane Potentials / drug effects. Mice. Mice, Inbred C57BL. Mice, Knockout. Rats. Receptors, Tumor Necrosis Factor, Type I / genetics. Receptors, Tumor Necrosis Factor, Type I / physiology

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  • (PMID = 16324117.001).
  • [ISSN] 0953-816X
  • [Journal-full-title] The European journal of neuroscience
  • [ISO-abbreviation] Eur. J. Neurosci.
  • [Language] eng
  • [Grant] United Kingdom / Wellcome Trust / /
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] France
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Receptors, Tumor Necrosis Factor, Type I; 0 / Tumor Necrosis Factor-alpha
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19. Yang SG, Zhang X, Sun XS, Ling TJ, Feng Y, Du XY, Zhao M, Yang Y, Xue D, Wang L, Liu RT: Diverse ecdysterones show different effects on amyloid-β42 aggregation but all uniformly inhibit amyloid-β42-induced cytotoxicity. J Alzheimers Dis; 2010;22(1):107-17

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Diverse ecdysterones show different effects on amyloid-β42 aggregation but all uniformly inhibit amyloid-β42-induced cytotoxicity.
  • Amyloid-β (Aβ) plays a pivotal role in Alzheimer's disease (AD) pathogenesis and in toxic mechanisms such as oxidative stress, mitochondrial dysfunction, calcium turbulence, and apoptosis induction.
  • [MeSH-major] Amyloid beta-Peptides / antagonists & inhibitors. Amyloid beta-Peptides / toxicity. Ecdysterone / pharmacology. Peptide Fragments / antagonists & inhibitors. Peptide Fragments / toxicity. Protein Multimerization / drug effects
  • [MeSH-minor] Alzheimer Disease / drug therapy. Alzheimer Disease / metabolism. Alzheimer Disease / pathology. Cell Line, Tumor. Humans. Protein Folding / drug effects. Reactive Oxygen Species / metabolism. Structure-Activity Relationship

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  • (PMID = 20847437.001).
  • [ISSN] 1875-8908
  • [Journal-full-title] Journal of Alzheimer's disease : JAD
  • [ISO-abbreviation] J. Alzheimers Dis.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / Reactive Oxygen Species; 0 / amyloid beta-protein (1-42); 5289-74-7 / Ecdysterone
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20. Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM: Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci U S A; 2009 Dec 1;106(48):20324-9
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide.
  • One of the neuropathological hallmarks of Alzheimer's disease (AD) is the amyloid plaque, primarily composed of aggregated amyloid-beta (Abeta) peptide.
  • Homogenates from these Abeta(1-42)-loaded cells were capable of seeding amyloid fibril growth.
  • At high concentrations, vesicular Abeta aggregates to form HMW species which are capable of seeding amyloid fibril growth.
  • We speculate that extrusion of these aggregates may seed extracellular amyloid plaque formation during AD pathogenesis.

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  • (PMID = 19910533.001).
  • [ISSN] 1091-6490
  • [Journal-full-title] Proceedings of the National Academy of Sciences of the United States of America
  • [ISO-abbreviation] Proc. Natl. Acad. Sci. U.S.A.
  • [Language] ENG
  • [Grant] United States / NINDS NIH HHS / NS / R01 NS056114; United States / NINDS NIH HHS / NS / R01 NS048283; United States / NINDS NIH HHS / NS / R01 NS067905-01A2; United States / NIDDK NIH HHS / DK / R01 DK013332; United States / NINDS NIH HHS / NS / NS067905-01A2; United States / NINDS NIH HHS / NS / NS048283-05; United States / NINDS NIH HHS / NS / P01 NS032636; United States / NINDS NIH HHS / NS / P01 NS032636-149001; United States / NIA NIH HHS / AG / R01 AG027924; United States / NIA NIH HHS / AG / P01 AG030128; United States / NINDS NIH HHS / NS / R01 NS048283-05; United States / NINDS NIH HHS / NS / R01 NS067905; United States / NINDS NIH HHS / NS / R01 NS48283; United States / NIDDK NIH HHS / DK / R01 DK13332; United States / NINDS NIH HHS / NS / R01 NS67905; United States / NINDS NIH HHS / NS / P01 NS32636; United States / NINDS NIH HHS / NS / NS032636-149001
  • [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 / Amyloid beta-Peptides; 0 / Thiazoles; 2390-54-7 / thioflavin T
  • [Other-IDs] NLM/ PMC2787156
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21. Pastorino L, Sun A, Lu PJ, Zhou XZ, Balastik M, Finn G, Wulf G, Lim J, Li SH, Li X, Xia W, Nicholson LK, Lu KP: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature; 2006 Mar 23;440(7083):528-34
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production.
  • Neuropathological hallmarks of Alzheimer's disease are neurofibrillary tangles composed of tau and neuritic plaques comprising amyloid-beta peptides (Abeta) derived from amyloid precursor protein (APP), but their exact relationship remains elusive.
  • [MeSH-major] Amyloid beta-Peptides / biosynthesis. Amyloid beta-Protein Precursor / metabolism. Peptidylprolyl Isomerase / metabolism. Protein Processing, Post-Translational
  • [MeSH-minor] Alzheimer Disease / metabolism. Alzheimer Disease / pathology. Animals. CHO Cells. Catalysis. Cell Line. Cell Line, Tumor. Cricetinae. Cricetulus. Humans. Mice. Mice, Knockout. Phosphorylation. Protein Binding. Protein Structure, Tertiary. Threonine / metabolism. Transfection


22. Zeng C, Lee JT, Chen H, Chen S, Hsu CY, Xu J: Amyloid-beta peptide enhances tumor necrosis factor-alpha-induced iNOS through neutral sphingomyelinase/ceramide pathway in oligodendrocytes. J Neurochem; 2005 Aug;94(3):703-12
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid-beta peptide enhances tumor necrosis factor-alpha-induced iNOS through neutral sphingomyelinase/ceramide pathway in oligodendrocytes.
  • In order to study the roles of the amyloid-beta peptide in inducing oxidative stress damage in white matter of AD, we investigated the effects of amyloid-beta peptide 25-35 (Abeta) on proinflammatory cytokine tumor necrosis factor-alpha (TNF-alpha)-induced inducible nitric oxide synthase (iNOS) in cultured oligodendrocytes (OLGs).
  • [MeSH-major] Amyloid beta-Peptides / pharmacology. Ceramides / metabolism. Nitric Oxide Synthase / metabolism. Oligodendroglia / drug effects. Sphingomyelin Phosphodiesterase / metabolism. Tumor Necrosis Factor-alpha / pharmacology

  • Hazardous Substances Data Bank. METHYLTHIAZOLETETRAZOLIUM .
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  • (PMID = 16033420.001).
  • [ISSN] 0022-3042
  • [Journal-full-title] Journal of neurochemistry
  • [ISO-abbreviation] J. Neurochem.
  • [Language] eng
  • [Grant] United States / BHP HRSA HHS / AH / AHA 0050597N; United States / NINDS NIH HHS / NS / NS40162; United States / NINDS NIH HHS / NS / R01 NS40525
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Ceramides; 0 / Enzyme Inhibitors; 0 / NF-kappa B; 0 / Nitrites; 0 / Peptide Fragments; 0 / RNA, Messenger; 0 / Tetrazolium Salts; 0 / Thiazoles; 0 / Tumor Necrosis Factor-alpha; 147336-22-9 / Green Fluorescent Proteins; 298-93-1 / thiazolyl blue; EC 1.14.13.39 / Nitric Oxide Synthase; EC 1.14.13.39 / Nitric Oxide Synthase Type II; EC 1.14.13.39 / Nos2 protein, rat; EC 3.1.4.12 / Sphingomyelin Phosphodiesterase
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23. Lourenço FC, Galvan V, Fombonne J, Corset V, Llambi F, Müller U, Bredesen DE, Mehlen P: Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production. Cell Death Differ; 2009 May;16(5):655-63
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production.
  • The beta-amyloid precursor protein (APP) is an orphan transmembrane receptor whose physiological role is largely unknown.
  • APP is cleaved by proteases generating amyloid-beta (Abeta) peptide, the main component of the amyloid plaques that are associated with Alzheimer's disease.

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  • (PMID = 19148186.001).
  • [ISSN] 1476-5403
  • [Journal-full-title] Cell death and differentiation
  • [ISO-abbreviation] Cell Death Differ.
  • [Language] ENG
  • [Grant] United States / NINDS NIH HHS / NS / NS033376-04; United States / NINDS NIH HHS / NS / R01 NS033376-05; United States / NINDS NIH HHS / NS / NS033376-08; United States / NINDS NIH HHS / NS / R01 NS033376-09; United States / NINDS NIH HHS / NS / R01 NS033376-04; United States / NINDS NIH HHS / NS / NS033376-05; United States / NINDS NIH HHS / NS / R01 NS033376; United States / NINDS NIH HHS / NS / NS033376-06; United States / NINDS NIH HHS / NS / NS033376-09; United States / NINDS NIH HHS / NS / R01 NS033376-06; United States / NINDS NIH HHS / NS / R01 NS033376-07; United States / NINDS NIH HHS / NS / NS33376; United States / NINDS NIH HHS / NS / R01 NS033376-10; United States / NINDS NIH HHS / NS / R01 NS033376-08; United States / NINDS NIH HHS / NS / NS033376-07
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Nerve Growth Factors; 0 / Recombinant Proteins; 0 / Tumor Suppressor Proteins; 158651-98-0 / netrin-1
  • [Other-IDs] NLM/ NIHMS131138; NLM/ PMC2757418
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24. Zhu X, Mei M, Lee HG, Wang Y, Han J, Perry G, Smith MA: P38 activation mediates amyloid-beta cytotoxicity. Neurochem Res; 2005 Jun-Jul;30(6-7):791-6
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] P38 activation mediates amyloid-beta cytotoxicity.
  • Amyloid-beta is a leading candidate factor in the development of Alzheimer disease (AD), however the mechanisms involved are unclear.
  • As such, there has been considerable interest in evidence showing that the neuronal damage caused by amyloid-beta is mediated by oxidative stress.
  • One SAPK in particular, p38, appears to be crucial in AD and therefore, in the current study, we investigated the role of p38 activation in amyloid-beta cytotoxicity.
  • Our data showed p38 activation was induced by amyloid-beta in a concentration-dependent manner in M17 human neuroblastoma cells.
  • Notably, amyloid-beta toxicity was significantly decreased by inhibition of p38 activity by overexpressing dominant negative p38.
  • Consistent with this, in primary cortical neurons amyloid-beta also induced p38 activation and amyloid-beta toxicity was significantly diminished when p38 was inhibited by its specific inhibitor, SB203580.
  • Taken together, these data suggest that p38 is a key downstream effector of amyloid-beta-induced neuronal death and blocking this pathway may be of therapeutic value.
  • [MeSH-major] Amyloid beta-Peptides / physiology. p38 Mitogen-Activated Protein Kinases / metabolism
  • [MeSH-minor] Blotting, Western. Cell Line, Tumor. Enzyme Activation. Humans. Neuroblastoma / enzymology. Neuroblastoma / metabolism. Neuroblastoma / pathology. Neurons / enzymology. Neurons / metabolism. Oxidative Stress

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  • (PMID = 16187214.001).
  • [ISSN] 0364-3190
  • [Journal-full-title] Neurochemical research
  • [ISO-abbreviation] Neurochem. Res.
  • [Language] eng
  • [Grant] United States / NINDS NIH HHS / NS / NS38648
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; EC 2.7.11.24 / p38 Mitogen-Activated Protein Kinases
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25. Tsai YC, Jeng CR, Zhuo YX, Tsai YC, Liu CH, Pang VF: Amyloid-producing odontogenic tumor and its immunohistochemical characterization in a Shih Tzu dog. Vet Pathol; 2007 Mar;44(2):233-6

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid-producing odontogenic tumor and its immunohistochemical characterization in a Shih Tzu dog.
  • Histopathologically, the growth was characterized by indistinctly lobulated nests, islands, and strands of proliferating odontogenic and squamous epithelial cells, intermingled in close association with large numbers of irregular extracellular deposits of amyloid and amorphous calcified substance.
  • The amyloid deposits were AE1/AE3-negative.
  • The growth was diagnosed as an amyloid-producing odontogenic tumor.
  • [MeSH-major] Amyloid / biosynthesis. Dog Diseases / metabolism. Dog Diseases / pathology. Gingival Neoplasms / veterinary. Odontogenic Tumors / veterinary

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  • (PMID = 17317805.001).
  • [ISSN] 0300-9858
  • [Journal-full-title] Veterinary pathology
  • [ISO-abbreviation] Vet. Pathol.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid
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26. Malisauskas M, Ostman J, Darinskas A, Zamotin V, Liutkevicius E, Lundgren E, Morozova-Roche LA: Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity? J Biol Chem; 2005 Feb 25;280(8):6269-75

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity?
  • In amyloid diseases, it is not evident which protein aggregates induce cell death via specific molecular mechanisms and which cause damage because of their mass accumulation and mechanical properties.
  • We showed that equine lysozyme assembles into soluble amyloid oligomers and protofilaments at pH 2.0 and 4.5, 57 degrees C.
  • They bind thioflavin-T and Congo red similar to common amyloid structures, and their morphology was monitored by atomic force microscopy.
  • Primary cultures were more susceptible to the toxic effect induced by soluble amyloid oligomers than the neuroblastoma cell line.
  • Soluble amyloid oligomers may assemble into rings; however, there was no correlation between the quantity of rings in the sample and its toxicity.
  • The cytotoxicity of transient oligomeric species of the ubiquitous protein lysozyme indicates that this is an intrinsic feature of protein amyloid aggregation, and therefore soluble amyloid oligomers can be used as a primary therapeutic target and marker of amyloid disease.
  • [MeSH-major] Amyloid / metabolism. Muramidase / metabolism. Neurons / pathology
  • [MeSH-minor] Amyloidosis / etiology. Amyloidosis / pathology. Animals. Cell Death. Cell Line, Tumor. Cells, Cultured. Dimerization. Fibroblasts / pathology. Horses. Hydrogen-Ion Concentration. Mice. Mice, Inbred BALB C. Microscopy, Atomic Force. Neuroblastoma / pathology

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  • (PMID = 15576361.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; EC 3.2.1.17 / Muramidase
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27. Botella-López A, Cuchillo-Ibáñez I, Cotrufo T, Mok SS, Li QX, Barquero MS, Dierssen M, Soriano E, Sáez-Valero J: Beta-amyloid controls altered Reelin expression and processing in Alzheimer's disease. Neurobiol Dis; 2010 Mar;37(3):682-91
MedlinePlus Health Information. consumer health - Alzheimer's Disease.

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Beta-amyloid controls altered Reelin expression and processing in Alzheimer's disease.
  • Here we demonstrate pronounced Reelin changes at protein and mRNA levels in the frontal cortex in adult Down's syndrome (DS), where the extra copy of chromosome 21 leads to overexpression of beta-amyloid.
  • Overexpression of mutant human amyloid precursor protein also led to an increase in levels of Reelin fragments in Tg2576 transgenic mice for human beta-amyloid.
  • An altered pattern of Reelin glycosylation was detected in extracts from the frontal cortex of AD patients and in Abeta42-treated SH-SY5Y cells, supporting the notion that beta-amyloid triggers altered Reelin processing.
  • These results provide evidence that Reelin expression and processing is altered in several amyloid conditions.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Brain / metabolism. Cell Adhesion Molecules, Neuronal / metabolism. Extracellular Matrix Proteins / metabolism. Nerve Tissue Proteins / metabolism. Serine Endopeptidases / metabolism
  • [MeSH-minor] Adult. Aged. Amyloid beta-Protein Precursor / genetics. Amyloid beta-Protein Precursor / metabolism. Animals. Cell Line, Tumor. Chromosomes, Human, Pair 21 / genetics. Down Syndrome / genetics. Down Syndrome / metabolism. Down Syndrome / physiopathology. Female. Fetus. Gene Expression Regulation / physiology. Glycosylation. Humans. Male. Mice. Middle Aged. Neuronal Plasticity / genetics. Plaque, Amyloid / genetics. Plaque, Amyloid / metabolism. Plaque, Amyloid / pathology. RNA, Messenger / metabolism. Synapses / metabolism. Up-Regulation / genetics

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  • [Copyright] 2009 Elsevier Inc. All rights reserved.
  • (PMID = 20025970.001).
  • [ISSN] 1095-953X
  • [Journal-full-title] Neurobiology of disease
  • [ISO-abbreviation] Neurobiol. Dis.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Cell Adhesion Molecules, Neuronal; 0 / Extracellular Matrix Proteins; 0 / Nerve Tissue Proteins; 0 / RNA, Messenger; EC 3.4.21.- / Serine Endopeptidases; EC 3.4.21.- / reelin protein
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28. Suram A, Venugopal C, Prakasam A, Sambamurti K: Genotoxicity in Alzheimer's disease: role of amyloid. Curr Alzheimer Res; 2006 Sep;3(4):365-75
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Genotoxicity in Alzheimer's disease: role of amyloid.
  • Alzheimer's disease (AD) is a complex neurodegenerative disorder pathologically identified by the presence of extracellular senile plaques (SP) with a proteinaceous core composed of aggregates of the amyloid peptide (Abeta) and intracellular aggregates of the microtubule-associated protein tau (tau) as neurofibrillary tangles (NFTs).
  • The present review discusses various influences, in particular of amyloid, on the genetic material and their possible role in the neurodegeneration in AD.
  • [MeSH-major] Alzheimer Disease / genetics. Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Brain / metabolism. DNA Damage / physiology
  • [MeSH-minor] Animals. Apoptosis / physiology. Genes, cdc / physiology. Humans. Mutation / genetics. Oxidative Stress / physiology. Signal Transduction / physiology. Tumor Suppressor Protein p53 / genetics. Tumor Suppressor Protein p53 / metabolism

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  • (PMID = 17017867.001).
  • [ISSN] 1567-2050
  • [Journal-full-title] Current Alzheimer research
  • [ISO-abbreviation] Curr Alzheimer Res
  • [Language] eng
  • [Grant] United States / NIA NIH HHS / AG / R01AG023055
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] United Arab Emirates
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Tumor Suppressor Protein p53
  • [Number-of-references] 195
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29. Sahlin C, Lord A, Magnusson K, Englund H, Almeida CG, Greengard P, Nyberg F, Gouras GK, Lannfelt L, Nilsson LN: The Arctic Alzheimer mutation favors intracellular amyloid-beta production by making amyloid precursor protein less available to alpha-secretase. J Neurochem; 2007 May;101(3):854-62
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] The Arctic Alzheimer mutation favors intracellular amyloid-beta production by making amyloid precursor protein less available to alpha-secretase.
  • Mutations within the amyloid-beta (Abeta) domain of the amyloid precursor protein (APP) typically generate hemorrhagic strokes and vascular amyloid angiopathy.
  • [MeSH-major] Amyloid Precursor Protein Secretases / metabolism. Amyloid beta-Peptides / genetics. Mutation / physiology
  • [MeSH-minor] Cell Line, Tumor. Humans. Mutagenesis, Site-Directed / methods. Neuroblastoma. Protein Structure, Tertiary. Transfection / methods

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  • (PMID = 17448150.001).
  • [ISSN] 0022-3042
  • [Journal-full-title] Journal of neurochemistry
  • [ISO-abbreviation] J. Neurochem.
  • [Language] eng
  • [Grant] United States / NIA NIH HHS / AG / AG09464
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; EC 3.4.- / Amyloid Precursor Protein Secretases
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30. Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen PP, Kayed R, Glabe CG, Frautschy SA, Cole GM: Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem; 2005 Feb 18;280(7):5892-901
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] Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo.
  • Alzheimer's disease (AD) involves amyloid beta (Abeta) accumulation, oxidative damage, and inflammation, and risk is reduced with increased antioxidant and anti-inflammatory consumption.
  • The phenolic yellow curry pigment curcumin has potent anti-inflammatory and antioxidant activities and can suppress oxidative damage, inflammation, cognitive deficits, and amyloid accumulation.
  • AD and Tg2576 mice brain sections incubated with curcumin revealed preferential labeling of amyloid plaques.
  • When fed to aged Tg2576 mice with advanced amyloid accumulation, curcumin labeled plaques and reduced amyloid levels and plaque burden.
  • Hence, curcumin directly binds small beta-amyloid species to block aggregation and fibril formation in vitro and in vivo.

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  • (PMID = 15590663.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / R01 AG013741; United States / NIA NIH HHS / AG / P50 AG016570; United States / NINDS NIH HHS / NS / NS43946; United States / NIA NIH HHS / AG / R01 AG010685; United States / NCCIH NIH HHS / AT / R01 AT003008
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Anti-Inflammatory Agents, Non-Steroidal; 0 / Benzoates; 0 / Biphenyl Compounds; 0 / Diamines; 0 / N,N'-bis(3-hydroxyphenyl)pyridazine-3,6-diamine; 0 / Peptide Fragments; 0 / Pyridazines; 0 / Thiazoles; 2390-54-7 / thioflavin T; 3U05FHG59S / Congo Red; 57Y76R9ATQ / Naproxen; 6472-91-9 / chrysamine G; IT942ZTH98 / Curcumin; WK2XYI10QM / Ibuprofen
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31. Austen BM, Paleologou KE, Ali SA, Qureshi MM, Allsop D, El-Agnaf OM: Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide. Biochemistry; 2008 Feb 19;47(7):1984-92
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide.
  • Convergent biochemical and genetic evidence suggests that the formation of beta-amyloid (Abeta) deposits in the brain is an important and, probably, seminal step in the development of Alzheimer's disease (AD).
  • [MeSH-major] Amyloid beta-Peptides / chemistry. Amyloid beta-Peptides / toxicity. Drug Design. Peptides / chemistry. Peptides / pharmacology
  • [MeSH-minor] Amino Acid Sequence. Biopolymers. Cell Line, Tumor. Humans. Microscopy, Electron, Transmission

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  • (PMID = 18189413.001).
  • [ISSN] 0006-2960
  • [Journal-full-title] Biochemistry
  • [ISO-abbreviation] Biochemistry
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Biopolymers; 0 / Peptides
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32. Wang XC, Zhang YC, Chatterjie N, Grundke-Iqbal I, Iqbal K, Wang JZ: Effect of melatonin and melatonylvalpromide on beta-amyloid and neurofilaments in N2a cells. Neurochem Res; 2008 Jun;33(6):1138-44
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Effect of melatonin and melatonylvalpromide on beta-amyloid and neurofilaments in N2a cells.
  • In the present study, we have studied the effect of melatonin (Mt) and melatonin derivative, i.e., melatonylvalpromide (Mtv), on cell viability, beta-amyloid (Abeta) production, cell morphology, and expression and phosphorylation of neurofilament proteins in wild-type murine neuroblastoma N2a (N2a/wt) and N2a stably transfected with amyloid precursor protein (N2a/APP) cell lines.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Melatonin / analogs & derivatives. Melatonin / pharmacology. Neurofilament Proteins / metabolism. Valproic Acid / analogs & derivatives
  • [MeSH-minor] Alzheimer Disease / metabolism. Alzheimer Disease / pathology. Animals. Cell Line, Tumor. Mice. Neuroblastoma

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  • (PMID = 18231852.001).
  • [ISSN] 0364-3190
  • [Journal-full-title] Neurochemical research
  • [ISO-abbreviation] Neurochem. Res.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Neurofilament Proteins; 614OI1Z5WI / Valproic Acid; JL5DK93RCL / Melatonin; RUA6CWU76G / dipropylacetamide
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33. Takuma H, Teraoka R, Mori H, Tomiyama T: Amyloid-beta E22Delta variant induces synaptic alteration in mouse hippocampal slices. Neuroreport; 2008 Apr 16;19(6):615-9

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid-beta E22Delta variant induces synaptic alteration in mouse hippocampal slices.
  • We recently identified a novel amyloid precursor protein mutation (E693Delta) in familial Alzheimer's-type dementia.
  • This mutation produces amyloid-beta (Abeta) variant lacking glutamate-22 (E22Delta), which showed enhanced oligomerization but no fibrillization.
  • [MeSH-major] Amyloid beta-Peptides / pharmacology. Hippocampus / drug effects. Neurons / drug effects. Synapses / drug effects
  • [MeSH-minor] Amyloid beta-Protein Precursor / genetics. Animals. Blotting, Western. Cell Line, Tumor. Humans. Immunohistochemistry. Mice. Mutation. Organ Culture Techniques. Peptide Fragments. Synaptophysin / biosynthesis. Synaptophysin / drug effects

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  • (PMID = 18382273.001).
  • [ISSN] 0959-4965
  • [Journal-full-title] Neuroreport
  • [ISO-abbreviation] Neuroreport
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Peptide Fragments; 0 / Synaptophysin
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34. Patel D, Henry J, Good T: Attenuation of beta-amyloid induced toxicity by sialic acid-conjugated dendrimeric polymers. Biochim Biophys Acta; 2006 Dec;1760(12):1802-9
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Attenuation of beta-amyloid induced toxicity by sialic acid-conjugated dendrimeric polymers.
  • beta-amyloid (Abeta) is the primary protein component of senile plaques in Alzheimer's disease and is believed to be associated with neurotoxicity in the disease.

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  • (PMID = 16982154.001).
  • [ISSN] 0006-3002
  • [Journal-full-title] Biochimica et biophysica acta
  • [ISO-abbreviation] Biochim. Biophys. Acta
  • [Language] ENG
  • [Grant] United States / NINDS NIH HHS / NS / R21 NS050346-02; United States / NINDS NIH HHS / NS / NS050346-02; United States / NINDS NIH HHS / NS / R21 NS050346; United States / NINDS NIH HHS / NS / NS050346; United States / NIA NIH HHS / AG / AG025586
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Dendrimers; GZP2782OP0 / N-Acetylneuraminic Acid
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35. Suwalsky M, Bolognin S, Zatta P: Interaction between Alzheimer's amyloid-beta and amyloid-beta-metal complexes with cell membranes. J Alzheimers Dis; 2009;17(1):81-90

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Interaction between Alzheimer's amyloid-beta and amyloid-beta-metal complexes with cell membranes.
  • A number of observations indicate that the primary target of amyloid-beta (Abeta) peptide is the cellular membrane of neurons.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Cell Membrane / metabolism. Metals / metabolism
  • [MeSH-minor] Analysis of Variance. Cell Line, Tumor. Cell Survival. Humans. Lipid Bilayers. Microscopy, Electron, Scanning / methods. Neuroblastoma / ultrastructure. X-Ray Diffraction / methods

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  • (PMID = 19494433.001).
  • [ISSN] 1387-2877
  • [Journal-full-title] Journal of Alzheimer's disease : JAD
  • [ISO-abbreviation] J. Alzheimers Dis.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Lipid Bilayers; 0 / Metals
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36. Sun X, Wu WH, Liu Q, Chen MS, Yu YP, Ma Y, Zhao YF, Li YM: Hybrid peptides attenuate cytotoxicity of beta-amyloid by inhibiting its oligomerization: implication from solvent effects. Peptides; 2009 Jul;30(7):1282-7

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Hybrid peptides attenuate cytotoxicity of beta-amyloid by inhibiting its oligomerization: implication from solvent effects.
  • Abnormal assembly of monomeric beta-amyloid (Abeta) in Alzheimer's disease leads to the formation of most neurotoxic oligomers in vivo.
  • [MeSH-major] Amyloid beta-Peptides / chemistry. Amyloid beta-Peptides / toxicity. Neurons / drug effects. Peptides / chemistry. Peptides / pharmacology. Protein Multimerization / drug effects
  • [MeSH-minor] Amino Acid Motifs. Amino Acid Sequence. Animals. Cell Line, Tumor. Mice. Microscopy, Electron, Transmission. Molecular Sequence Data

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  • (PMID = 19397942.001).
  • [ISSN] 1873-5169
  • [Journal-full-title] Peptides
  • [ISO-abbreviation] Peptides
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Peptides
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37. Bu G, Cam J, Zerbinatti C: LRP in amyloid-beta production and metabolism. Ann N Y Acad Sci; 2006 Nov;1086:35-53
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] LRP in amyloid-beta production and metabolism.
  • Amyloid-beta peptide (Abeta) production and accumulation in the brain is a central event in the pathogenesis of Alzheimer's disease (AD).
  • Abeta is derived from proteolytic processing of the amyloid precursor protein (APP), which interacts with several members of the LDLR family.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Brain / metabolism. LDL-Receptor Related Proteins / metabolism. Receptors, LDL / metabolism. Tumor Suppressor Proteins / metabolism
  • [MeSH-minor] Alzheimer Disease / metabolism. Amyloid beta-Protein Precursor / metabolism. Animals. Endocytosis / physiology. Endosomes / metabolism. Humans. Mice. Mice, Transgenic. Neurons / metabolism

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  • (PMID = 17185504.001).
  • [ISSN] 0077-8923
  • [Journal-full-title] Annals of the New York Academy of Sciences
  • [ISO-abbreviation] Ann. N. Y. Acad. Sci.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / LDL-Receptor Related Proteins; 0 / LRP1B protein, human; 0 / Lrp1b protein, mouse; 0 / Receptors, LDL; 0 / Tumor Suppressor Proteins
  • [Number-of-references] 149
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38. Thomas RS, Liddell JE, Murphy LS, Pache DM, Kidd EJ: An antibody to the beta-secretase cleavage site on amyloid-beta-protein precursor inhibits amyloid-beta production. J Alzheimers Dis; 2006 Dec;10(4):379-90
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] An antibody to the beta-secretase cleavage site on amyloid-beta-protein precursor inhibits amyloid-beta production.
  • Proteolytic cleavage of amyloid-beta-protein precursor (AbetaPP) by beta- and gamma-secretases results in production of the amyloid-beta peptide (Abeta) that accumulates in the brains of sufferers of Alzheimer's disease (AD).
  • [MeSH-major] Amyloid Precursor Protein Secretases / immunology. Amyloid beta-Peptides / metabolism. Amyloid beta-Protein Precursor / immunology. Antibodies, Monoclonal / pharmacology
  • [MeSH-minor] Astrocytoma / metabolism. Binding Sites, Antibody / immunology. Brain Neoplasms / metabolism. Cell Line, Tumor. Dose-Response Relationship, Drug. Enzyme-Linked Immunosorbent Assay. Humans. In Vitro Techniques. Neuroblastoma / metabolism. Peptide Fragments / metabolism

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  • (PMID = 17183149.001).
  • [ISSN] 1387-2877
  • [Journal-full-title] Journal of Alzheimer's disease : JAD
  • [ISO-abbreviation] J. Alzheimers Dis.
  • [Language] eng
  • [Grant] United Kingdom / Alzheimer's Society / / 79
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Antibodies, Monoclonal; 0 / Peptide Fragments; EC 3.4.- / Amyloid Precursor Protein Secretases
  • [Other-IDs] NLM/ EMS63783; NLM/ PMC4492742
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39. Uberti D, Ferrari-Toninelli G, Bonini SA, Sarnico I, Benarese M, Pizzi M, Benussi L, Ghidoni R, Binetti G, Spano P, Facchetti F, Memo M: Blockade of the tumor necrosis factor-related apoptosis inducing ligand death receptor DR5 prevents beta-amyloid neurotoxicity. Neuropsychopharmacology; 2007 Apr;32(4):872-80
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  • [Title] Blockade of the tumor necrosis factor-related apoptosis inducing ligand death receptor DR5 prevents beta-amyloid neurotoxicity.
  • We originally suggested that inhibition of tumor necrosis factor-related apoptosis inducing ligand (TRAIL) death pathway could be taken into consideration as a potential therapeutic strategy for Alzheimer's disease (AD).
  • Here, we demonstrated that the blockade of the TRAIL death receptor DR5 with a specific antibody completely prevented amyloid beta peptide (A beta) neurotoxicity in both neuronal cell line and primary cortical neurons.
  • In fact, whereas TRAIL expression was enhanced dose-dependently by concentrations of beta amyloid ranging from 10 nM to 1 microM, only the highest toxic dose of A beta (25 microM) induced the increased expression of DR5 and neuronal cell death.
  • In addition, the increased expression of DR5 receptor after beta amyloid treatment was sustained by p53 transcriptional activity, as demonstrated by the data showing that the p53 inhibitor Pifithrin alpha prevented both beta amyloid-induced DR5 induction and cell death.
  • These data suggest a sequential activation of p53 and DR5 upon beta amyloid exposure.
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Apoptosis / drug effects. Neurons / drug effects. Receptors, TNF-Related Apoptosis-Inducing Ligand / metabolism. TNF-Related Apoptosis-Inducing Ligand / physiology

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  • (PMID = 16936710.001).
  • [ISSN] 0893-133X
  • [Journal-full-title] Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology
  • [ISO-abbreviation] Neuropsychopharmacology
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Receptors, TNF-Related Apoptosis-Inducing Ligand; 0 / TNF-Related Apoptosis-Inducing Ligand
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40. Zheng L, Kågedal K, Dehvari N, Benedikz E, Cowburn R, Marcusson J, Terman A: Oxidative stress induces macroautophagy of amyloid beta-protein and ensuing apoptosis. Free Radic Biol Med; 2009 Feb 1;46(3):422-9
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  • [Title] Oxidative stress induces macroautophagy of amyloid beta-protein and ensuing apoptosis.
  • There is increasing evidence for the toxicity of intracellular amyloid beta-protein (Abeta) to neurons and the involvement of lysosomes in this process in Alzheimer disease (AD).
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Lysosomes / metabolism. Mutant Proteins / metabolism. Neurons / metabolism
  • [MeSH-minor] Apoptosis / genetics. Autophagy / drug effects. Autophagy / genetics. Cell Line, Tumor. Cell Membrane Permeability / genetics. Humans. Intracellular Membranes / metabolism. Oxidative Stress. Oxygen / pharmacology. Transfection. Transgenes

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  • (PMID = 19038331.001).
  • [ISSN] 1873-4596
  • [Journal-full-title] Free radical biology & medicine
  • [ISO-abbreviation] Free Radic. Biol. Med.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Mutant Proteins; S88TT14065 / Oxygen
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41. Bolognin S, Zatta P, Drago D, Tognon G, Parnigotto PP, Ricchelli F: Mutual stimulation of beta-amyloid fibrillogenesis by clioquinol and divalent metals. Neuromolecular Med; 2008;10(4):322-32
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  • [Title] Mutual stimulation of beta-amyloid fibrillogenesis by clioquinol and divalent metals.
  • Its biological effects are most likely ascribed to complexation of specific metal ions, such as copper (II) and zinc (II), critically associated with beta-amyloid (A beta) aggregation/fibrillogenesis and degeneration processes in the brain.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / drug effects. Clioquinol / pharmacology. Metals / toxicity. Plaque, Amyloid / drug effects
  • [MeSH-minor] Amino Acid Substitution / drug effects. Amino Acid Substitution / physiology. Animals. Cell Line, Tumor. Chelation Therapy / adverse effects. Chelation Therapy / methods. Copper / toxicity. Drug Synergism. Humans. Neurotoxins / toxicity. Rats. Species Specificity. Zinc / toxicity

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  • [ErratumIn] Neuromolecular Med. 2008;10(4):393
  • (PMID = 18712494.001).
  • [ISSN] 1559-1174
  • [Journal-full-title] Neuromolecular medicine
  • [ISO-abbreviation] Neuromolecular Med.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Metals; 0 / Neurotoxins; 789U1901C5 / Copper; 7BHQ856EJ5 / Clioquinol; J41CSQ7QDS / Zinc
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42. Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y, Nomura Y: Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J Neurosci; 2010 Mar 17;30(11):3924-32
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation.
  • Amyloid precursor protein (APP) is processed into amyloid-beta peptides (Abetas) that form plaque deposits in the brains of Alzheimer's disease (AD) patients.
  • [MeSH-major] Amyloid beta-Peptides / biosynthesis. Amyloid beta-Protein Precursor / metabolism. Ubiquitin-Protein Ligases / antagonists & inhibitors. Ubiquitin-Protein Ligases / physiology
  • [MeSH-minor] Aged. Aged, 80 and over. Alzheimer Disease / enzymology. Alzheimer Disease / metabolism. Alzheimer Disease / pathology. Animals. Apoptosis / physiology. Cell Line. Cell Line, Tumor. Cerebral Cortex / enzymology. Cerebral Cortex / metabolism. Cerebral Cortex / pathology. Endoplasmic Reticulum / enzymology. Endoplasmic Reticulum / metabolism. Endoplasmic Reticulum / pathology. Female. Humans. Male. Mice. Middle Aged. Oxidative Stress / physiology. Ubiquitination

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  • (PMID = 20237263.001).
  • [ISSN] 1529-2401
  • [Journal-full-title] The Journal of neuroscience : the official journal of the Society for Neuroscience
  • [ISO-abbreviation] J. Neurosci.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; EC 6.3.2.19 / SYVN1 protein, human; EC 6.3.2.19 / Ubiquitin-Protein Ligases
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43. Sandberg A, Luheshi LM, Söllvander S, Pereira de Barros T, Macao B, Knowles TP, Biverstål H, Lendel C, Ekholm-Petterson F, Dubnovitsky A, Lannfelt L, Dobson CM, Härd T: Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering. Proc Natl Acad Sci U S A; 2010 Aug 31;107(35):15595-600
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  • [Title] Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering.
  • Soluble oligomeric aggregates of the amyloid-beta peptide (Abeta) have been implicated in the pathogenesis of Alzheimer's disease (AD).
  • Abeta(40)cc and Abeta(42)cc both spontaneously form stable oligomeric species with distinct molecular weights and secondary-structure content, but both are unable to convert into amyloid fibrils.
  • Stable oligomers are expected to become highly toxic and, accordingly, we find that beta-sheet-containing Abeta(42)cc oligomers or protofibrillar species formed by these oligomers are 50 times more potent inducers of neuronal apoptosis than amyloid fibrils or samples of monomeric wild-type Abeta(42), in which toxic aggregates are only transiently formed.
  • [MeSH-major] Amyloid beta-Peptides / chemistry. Peptide Fragments / chemistry. Protein Engineering / methods
  • [MeSH-minor] Alzheimer Disease / metabolism. Amyloid / chemistry. Amyloid / ultrastructure. Cell Line, Tumor. Cell Survival / drug effects. Circular Dichroism. Electrophoresis, Polyacrylamide Gel. Escherichia coli / genetics. Humans. Kinetics. Microscopy, Atomic Force. Microscopy, Electron, Transmission. Models, Molecular. Molecular Weight. Protein Conformation. Protein Multimerization. Recombinant Proteins / chemistry. Recombinant Proteins / pharmacology. Spectroscopy, Fourier Transform Infrared

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  • (PMID = 20713699.001).
  • [ISSN] 1091-6490
  • [Journal-full-title] Proceedings of the National Academy of Sciences of the United States of America
  • [ISO-abbreviation] Proc. Natl. Acad. Sci. U.S.A.
  • [Language] eng
  • [Grant] United Kingdom / Medical Research Council / / G0700990; United Kingdom / Wellcome Trust / /
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / Recombinant Proteins; 0 / amyloid beta-protein (1-40); 0 / amyloid beta-protein (1-42)
  • [Other-IDs] NLM/ PMC2932621
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44. Zhang J, Mori A, Chen Q, Zhao B: Fermented papaya preparation attenuates beta-amyloid precursor protein: beta-amyloid-mediated copper neurotoxicity in beta-amyloid precursor protein and beta-amyloid precursor protein Swedish mutation overexpressing SH-SY5Y cells. Neuroscience; 2006 Nov 17;143(1):63-72
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Fermented papaya preparation attenuates beta-amyloid precursor protein: beta-amyloid-mediated copper neurotoxicity in beta-amyloid precursor protein and beta-amyloid precursor protein Swedish mutation overexpressing SH-SY5Y cells.
  • Recent studies indicate that the deposition of beta-amyloid (Abeta) is related in the pathogenesis of Alzheimer's disease (AD), but the underlying mechanism is still not clear.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Amyloid beta-Protein Precursor / genetics. Carica / chemistry. Copper / metabolism. Mutation. Plant Proteins / pharmacology
  • [MeSH-minor] Analysis of Variance. Apoptosis / drug effects. Blotting, Western / methods. Calcium / metabolism. Cell Line, Tumor. Cell Survival / drug effects. Cell Survival / genetics. Dose-Response Relationship, Drug. Drug Interactions. Enzyme-Linked Immunosorbent Assay / methods. Gene Expression Regulation / genetics. Humans. Neuroblastoma. Nitric Oxide Synthase / metabolism. RNA, Messenger / metabolism. Reactive Oxygen Species / metabolism. Reverse Transcriptase Polymerase Chain Reaction / methods. Thiobarbituric Acid Reactive Substances / metabolism. Transfection / methods

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  • (PMID = 16962711.001).
  • [ISSN] 0306-4522
  • [Journal-full-title] Neuroscience
  • [ISO-abbreviation] Neuroscience
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Plant Proteins; 0 / RNA, Messenger; 0 / Reactive Oxygen Species; 0 / Thiobarbituric Acid Reactive Substances; 789U1901C5 / Copper; EC 1.14.13.39 / Nitric Oxide Synthase; SY7Q814VUP / Calcium
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45. Eggert S, Midthune B, Cottrell B, Koo EH: Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production. J Biol Chem; 2009 Oct 16;284(42):28943-52

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production.
  • The amyloid precursor protein (APP) plays a central role in Alzheimer disease (AD) pathogenesis because sequential cleavages by beta- and gamma-secretase lead to the generation of the amyloid-beta (Abeta) peptide, a key constituent in the amyloid plaques present in brains of AD individuals.

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  • (PMID = 19596858.001).
  • [ISSN] 1083-351X
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / R01 AG012376; United States / NIA NIH HHS / AG / AG 12376
  • [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 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor
  • [Other-IDs] NLM/ PMC2781440
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46. Noonan J, Tanveer R, Klompas A, Gowran A, McKiernan J, Campbell VA: Endocannabinoids prevent β-amyloid-mediated lysosomal destabilization in cultured neurons. J Biol Chem; 2010 Dec 3;285(49):38543-54
NCI CPTAC Assay Portal. NCI CPTAC Assay Portal .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Endocannabinoids prevent β-amyloid-mediated lysosomal destabilization in cultured neurons.
  • Elucidation of the apoptotic pathway evoked by β-amyloid (Aβ) is thus important for the development of therapeutic strategies that can thwart Aβ toxicity and preserve cell viability.
  • We report that endocannabinoids stabilize lysosomes by preventing the Aβ-induced up-regulation of the tumor suppressor protein, p53, and its interaction with the lysosomal membrane.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Cannabinoid Receptor Modulators / metabolism. Endocannabinoids. Intracellular Membranes / metabolism. Lysosomes / metabolism. Neurons / metabolism
  • [MeSH-minor] Animals. Apoptosis. Cell Survival. Cells, Cultured. Male. Permeability. Rats. Rats, Wistar. Receptors, Cannabinoid. Tumor Suppressor Protein p53 / metabolism. Up-Regulation

  • MedlinePlus Health Information. consumer health - Alzheimer's Disease.
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  • (PMID = 20923768.001).
  • [ISSN] 1083-351X
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Cannabinoid Receptor Modulators; 0 / Endocannabinoids; 0 / Receptors, Cannabinoid; 0 / Tumor Suppressor Protein p53
  • [Other-IDs] NLM/ PMC2992287
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47. Gralle M, Botelho MG, Wouters FS: Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. J Biol Chem; 2009 May 29;284(22):15016-25
Hazardous Substances Data Bank. HEPARIN .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers.
  • The amyloid precursor protein (APP) is implied both in cell growth and differentiation and in neurodegenerative processes in Alzheimer disease.
  • Regulated proteolysis of APP generates biologically active fragments such as the neuroprotective secreted ectodomain sAPPalpha and the neurotoxic beta-amyloid peptide.
  • [MeSH-major] Amyloid beta-Protein Precursor / chemistry. Amyloid beta-Protein Precursor / secretion. Neuroprotective Agents / metabolism. Protein Multimerization
  • [MeSH-minor] Acyl Carrier Protein. Animals. Cell Line, Tumor. Cell Membrane / drug effects. Cell Membrane / metabolism. Cell Survival. Green Fluorescent Proteins / metabolism. Heparin / metabolism. Heparin / pharmacology. Models, Biological. Neuroblastoma / pathology. Quantum Dots

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  • (PMID = 19336403.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Acyl Carrier Protein; 0 / Amyloid beta-Protein Precursor; 0 / Neuroprotective Agents; 147336-22-9 / Green Fluorescent Proteins; 9005-49-6 / Heparin
  • [Other-IDs] NLM/ PMC2685684
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48. Tamboli IY, Prager K, Barth E, Heneka M, Sandhoff K, Walter J: Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J Biol Chem; 2005 Jul 29;280(30):28110-7
Hazardous Substances Data Bank. CHOLESTEROL .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide.
  • Alzheimer disease is associated with extracellular deposits of amyloid beta-peptides in the brain.
  • Amyloid beta-peptides are generated by proteolytic processing of the beta-amyloid precursor protein by beta- and gamma-secretases.
  • The cleavage by secretases occurs predominantly in post-Golgi secretory and endocytic compartments and is influenced by cholesterol, indicating a role of the membrane lipid composition in proteolytic processing of the beta-amyloid precursor protein.
  • The depletion of glycosphingolipids markedly reduced the secretion of endogenous beta-amyloid precursor protein in different cell types, including human neuroblastoma SH-SY5Y cells.
  • Importantly, secretion of amyloid beta-peptides was also strongly decreased by inhibition of glycosphingolipid biosynthesis.
  • Biochemical and cell biological experiments demonstrate that the pharmacological reduction of cellular glycosphingolipid levels inhibited maturation and cell surface transport of the beta-amyloid precursor protein.
  • In the glycosphingolipid-deficient cell line GM95, cellular levels and maturation of beta-amyloid precursor protein were also significantly reduced as compared with normal B16 cells.
  • Together, these data demonstrate that glycosphingolipids are implicated in the regulation of the subcellular transport of the beta-amyloid precursor protein in the secretory pathway and its proteolytic processing.
  • Thus, enzymes involved in glycosphingolipid metabolism might represent targets to inhibit the production of amyloid beta-peptides.
  • [MeSH-major] Amyloid beta-Peptides / secretion. Glycosphingolipids / metabolism
  • [MeSH-minor] Alzheimer Disease / metabolism. Animals. Biological Transport. Biotinylation. Blotting, Western. Brain / metabolism. Cell Line. Cell Line, Tumor. Cell Membrane / metabolism. Cholesterol / metabolism. Endocytosis. Gangliosides / metabolism. Golgi Apparatus / metabolism. HeLa Cells. Humans. Immunoprecipitation. Lipid Metabolism. Melanoma, Experimental. Mice. Peptides / chemistry. Rhodamines / pharmacology. Time Factors

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  • (PMID = 15923191.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Gangliosides; 0 / Glycosphingolipids; 0 / Peptides; 0 / Rhodamines; 4158-89-8 / tetramethylrhodamine isothiocyanate; 97C5T2UQ7J / Cholesterol
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49. Zhao H, Zhu J, Cui K, Xu X, O'Brien M, Wong KK, Kesari S, Xia W, Wong ST: Bioluminescence imaging reveals inhibition of tumor cell proliferation by Alzheimer's amyloid beta protein. Cancer Cell Int; 2009 Jun 01;9:15
COS Scholar Universe. author profiles.

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Bioluminescence imaging reveals inhibition of tumor cell proliferation by Alzheimer's amyloid beta protein.
  • To explore molecular determinants differentiating pathogenic routes towards AD or cancer, we investigate the role of amyloid beta protein (Abeta) on multiple tumor cell lines that are stably expressing luciferase (human glioblastoma U87; human breast adenocarcinoma MDA-MB231; and mouse melanoma B16F).
  • RESULTS: Quantification of the photons emitted from the MDA-MB231 or B16F cells revealed a significant inhibition of cell proliferation by the conditioning media (CM) derived from amyloid precursor protein (APP) over-expressing cells.
  • CONCLUSION: Our results suggest that Abeta plays an inhibitory role in tumor cell proliferation; this effect could depend on the type of tumor cells and amount of Abeta.

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  • (PMID = 19480719.001).
  • [ISSN] 1475-2867
  • [Journal-full-title] Cancer cell international
  • [ISO-abbreviation] Cancer Cell Int.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / P01 AG015379; United States / NIA NIH HHS / AG / R01 AG028928; United States / NLM NIH HHS / LM / R01 LM009161
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Other-IDs] NLM/ PMC2701410
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50. Habib LK, Lee MT, Yang J: Inhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity. J Biol Chem; 2010 Dec 10;285(50):38933-43
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Inhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity.
  • Compelling evidence shows a strong correlation between accumulation of neurotoxic β-amyloid (Aβ) peptides and oxidative stress in the brains of patients afflicted with Alzheimer disease (AD).
  • Furthermore, small molecule inhibitors of catalase-amyloid interactions protect the hydrogen peroxide-degrading activity of catalase in Aβ-rich environments, leading to reduction of the co-localization of catalase and Aβ in cells, inhibition of Aβ-induced increases in cellular levels of H(2)O(2), and reduction of the toxicity of Aβ peptides.
  • These studies, thus, provide evidence for the important role of intracellular catalase-amyloid interactions in Aβ-induced oxidative stress and propose a novel molecular strategy to inhibit such harmful interactions in AD.

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  • (PMID = 20923778.001).
  • [ISSN] 1083-351X
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / 3P50 AG005131; United States / NCI NIH HHS / CA / P30 CA23100; United States / NIA NIH HHS / AG / P50 AG005131; United States / NINDS NIH HHS / NS / P30 NS047101; United States / NCI NIH HHS / CA / P30 CA023100
  • [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 / Amyloid; 0 / Amyloid beta-Protein Precursor; 0 / Reactive Oxygen Species; BBX060AN9V / Hydrogen Peroxide; EC 1.11.1.6 / Catalase
  • [Other-IDs] NLM/ PMC2998107
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51. Pajak B, Songin M, Strosznajder JB, Orzechowski A, Gajkowska B: Ultrastructural evidence of amyloid beta-induced autophagy in PC12 cells. Folia Neuropathol; 2009;47(3):252-8

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Ultrastructural evidence of amyloid beta-induced autophagy in PC12 cells.
  • Herein we demonstrate that PC12 cells overexpress human amyloid beta precursor protein bearing double Swedish mutation(AbetaPPsw), showing the phenotype characteristic for Alzheimer's disease (AD).
  • Furthermore, autophagy induction was found to be a hallmark of amyloid beta-induced cytotoxicity.
  • Importantly, autophagic vacuoles were co-localized within amyloid beta (Abeta) deposits.
  • This suggests the involvement of autophagy in amyloid beta-elicited cell degeneration.

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  • (PMID = 19813145.001).
  • [ISSN] 1641-4640
  • [Journal-full-title] Folia neuropathologica
  • [ISO-abbreviation] Folia Neuropathol
  • [Language] ENG
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Poland
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor
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52. Alkam T, Nitta A, Mizoguchi H, Saito K, Seshima M, Itoh A, Yamada K, Nabeshima T: Restraining tumor necrosis factor-alpha by thalidomide prevents the amyloid beta-induced impairment of recognition memory in mice. Behav Brain Res; 2008 May 16;189(1):100-6
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Restraining tumor necrosis factor-alpha by thalidomide prevents the amyloid beta-induced impairment of recognition memory in mice.
  • The interruption of the toxic pathways of amyloid beta peptide (Abeta) still remains promising for the treatment.
  • The involvement of tumor necrosis factor-alpha (TNF-alpha) in the toxicity of Abeta(1-40) in recent reports provide a fresh target for the interruption.
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Neurotoxins / toxicity. Peptide Fragments / toxicity. Recognition (Psychology) / physiology. Tumor Necrosis Factor-alpha / metabolism

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  • (PMID = 18325608.001).
  • [ISSN] 0166-4328
  • [Journal-full-title] Behavioural brain research
  • [ISO-abbreviation] Behav. Brain Res.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Immunosuppressive Agents; 0 / Neurotoxins; 0 / Peptide Fragments; 0 / RNA, Messenger; 0 / Tumor Necrosis Factor-alpha; 0 / amyloid beta-protein (25-35); 4Z8R6ORS6L / Thalidomide; EC 1.14.13.39 / Nitric Oxide Synthase Type II
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53. Malisauskas M, Darinskas A, Zamotin VV, Gharibyan A, Kostanyan IA, Morozova-Roche LA: Intermediate amyloid oligomers of lysozyme: Is their cytotoxicity a particular case or general rule for amyloid? Biochemistry (Mosc); 2006 May;71(5):505-12
Hazardous Substances Data Bank. C.I. DIRECT RED 28 .

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Intermediate amyloid oligomers of lysozyme: Is their cytotoxicity a particular case or general rule for amyloid?
  • In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme.
  • We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees C.
  • These structures bind the amyloid-specific dyes thioflavin T and Congo Red, and their morphology and size were analyzed by atomic force microscopy.
  • However, soluble amyloid oligomers of lysozyme caused death of all these cell types, as estimated by flow-cytometry counting dead cells stained with ethidium bromide.
  • The primary cell cultures appeared to be more sensitive to amyloid than neuroblastoma cell line IMR-32.
  • Amyloid cytotoxicity depends on the size of oligomeric particles: samples containing 20-mers formed at pH 4.5 were more toxic than tetramers and octamers present in the solution at pH 2.0.
  • Soluble amyloid oligomers can self-assemble into doughnut-like structures; however, no correlation was observed between the amount of the doughnut-like structures in the sample and its cytotoxicity.
  • The fact that the intermediate oligomers of such an abundant protein as lysozyme display cytotoxicity confirms a hypothesis that cytotoxicity is a common feature of protein amyloid.
  • Inhibition of intermediate oligomer formation is crucial in preventing amyloid pathogeneses.
  • [MeSH-major] Amyloid / metabolism. Muramidase / metabolism
  • [MeSH-minor] Amyloid beta-Peptides / chemistry. Amyloid beta-Peptides / metabolism. Amyloidosis / etiology. Amyloidosis / metabolism. Amyloidosis / pathology. Animals. Cell Line, Tumor. Cell Survival / drug effects. Cells, Cultured. Congo Red / chemistry. Dimerization. Female. Horses. Humans. Hydrogen-Ion Concentration. Kinetics. Macromolecular Substances / chemistry. Macromolecular Substances / metabolism. Mice. Mice, Inbred BALB C. Microscopy, Atomic Force / methods. Models, Molecular. Protein Structure, Secondary. Thiazoles / chemistry

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  • (PMID = 16732728.001).
  • [ISSN] 0006-2979
  • [Journal-full-title] Biochemistry. Biokhimii︠a︡
  • [ISO-abbreviation] Biochemistry Mosc.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; 0 / Amyloid beta-Peptides; 0 / Macromolecular Substances; 0 / Thiazoles; 2390-54-7 / thioflavin T; 3U05FHG59S / Congo Red; EC 3.2.1.17 / Muramidase
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54. Akasaka-Manya K, Manya H, Sakurai Y, Wojczyk BS, Kozutsumi Y, Saito Y, Taniguchi N, Murayama S, Spitalnik SL, Endo T: Protective effect of N-glycan bisecting GlcNAc residues on beta-amyloid production in Alzheimer's disease. Glycobiology; 2010 Jan;20(1):99-106
COS Scholar Universe. author profiles.

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Protective effect of N-glycan bisecting GlcNAc residues on beta-amyloid production in Alzheimer's disease.
  • Here, we focused on the N-glycans of amyloid precursor protein whose cleaved fragment, beta-amyloid, is thought to cause much of the pathology of Alzheimer's disease (AD).
  • We previously determined the N-glycan structures of normal and mutant amyloid precursor proteins (the Swedish type and the London type).
  • In comparison with normal amyloid precursor protein, mutant amyloid precursor proteins had higher contents of bisecting GlcNAc residues.
  • Furthermore, beta-amyloid treatment increased GnT-III mRNA expression in Neuro2a mouse neuroblastoma cells.
  • We then examined the influence of bisecting GlcNAc on the production of beta-amyloid.
  • Both beta-amyloid 40 and beta-amyloid 42 were significantly decreased in GnT-III-transfected cells.
  • Taken together, these results suggest that upregulation of GnT-III in AD brains may represent an adaptive response to protect them from additional beta-amyloid production.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / chemistry. N-Acetylglucosaminyltransferases / chemistry. Polysaccharides / chemistry
  • [MeSH-minor] Aging. Animals. Brain / metabolism. Cell Line, Tumor. Humans. Mice. Mice, Inbred C57BL. Models, Biological. RNA, Messenger / metabolism. Time Factors. Up-Regulation

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  • (PMID = 19776078.001).
  • [ISSN] 1460-2423
  • [Journal-full-title] Glycobiology
  • [ISO-abbreviation] Glycobiology
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Polysaccharides; 0 / RNA, Messenger; EC 2.4.1.- / N-Acetylglucosaminyltransferases; EC 2.4.1.150 / N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase
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55. Drut R, Giménez PO: Acinic cell carcinoma of salivary gland with massive deposits of globular amyloid. Int J Surg Pathol; 2008 Apr;16(2):202-7
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Acinic cell carcinoma of salivary gland with massive deposits of globular amyloid.
  • We present the case of a 23-year-old woman with a parotid gland tumor, the fine-needle aspiration biopsy smears of which showed epithelial cells with wide cytoplasm, isolated or arranged in micropapillary groups together with psammoma bodies.
  • The surgical specimen contained a 5-cm tumor with the histologic features of an acinic cell carcinoma (ACC) with papillary areas.
  • Notably, the cells of the tumor seemed to follow a sequence from large cells with rounded nuclei with open chromatin and prominent nucleoli to vacuolated cells with granular material, and finally to cells undergoing apoptosis.
  • The picture suggested that those amyloid bodies (psammoma bodies) resulted from the accumulation of residual masses of apoptotic cells.
  • Huge globular amyloid deposits, the suggested name for this material irrespective of the type of amyloid, have not been previously reported in ACC of salivary gland.
  • [MeSH-major] Amyloid / metabolism. Carcinoma, Acinar Cell / pathology. Parotid Neoplasms / pathology
  • [MeSH-minor] Adult. Biomarkers, Tumor / metabolism. Biopsy, Fine-Needle. Birefringence. Cellular Structures / pathology. Coloring Agents. Congo Red. Female. Humans

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  • (PMID = 18417682.001).
  • [ISSN] 1066-8969
  • [Journal-full-title] International journal of surgical pathology
  • [ISO-abbreviation] Int. J. Surg. Pathol.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; 0 / Biomarkers, Tumor; 0 / Coloring Agents; 3U05FHG59S / Congo Red
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56. Chang ES, Liao TY, Lim TS, Fann W, Chen RP: A new amyloid-like beta-aggregate with amyloid characteristics, except fibril morphology. J Mol Biol; 2009 Jan 30;385(4):1257-65
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  • [Title] A new amyloid-like beta-aggregate with amyloid characteristics, except fibril morphology.
  • Amyloid plaques, formed from amyloid beta (Abeta) peptides (mainly Abeta40 or Abeta42), are one of the most important pathological characteristics of Alzheimer's disease.
  • The mutant peptide with Val24-to-(D)Pro substitution, named V24P, formed a new amyloid-like beta-aggregate at high peptide concentration.
  • The aggregate has most of the characteristics of amyloid fibrils, except fibril morphology.
  • [MeSH-major] Amyloid beta-Peptides / chemistry
  • [MeSH-minor] Amino Acid Substitution. Animals. Cell Death / drug effects. Cell Line, Tumor. Congo Red. Mice. Models, Biological. Mutant Proteins / chemistry. Mutant Proteins / pharmacology. Mutant Proteins / ultrastructure. Mutation / genetics. Peptides / chemistry. Peptides / pharmacology. Proline / genetics. Protein Structure, Quaternary. Protein Structure, Secondary. Thiazoles / metabolism. Time Factors. Valine / genetics

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  • (PMID = 19041877.001).
  • [ISSN] 1089-8638
  • [Journal-full-title] Journal of molecular biology
  • [ISO-abbreviation] J. Mol. Biol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Mutant Proteins; 0 / Peptides; 0 / Thiazoles; 2390-54-7 / thioflavin T; 3U05FHG59S / Congo Red; 9DLQ4CIU6V / Proline; HG18B9YRS7 / Valine
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57. Mina EW, Lasagna-Reeves C, Glabe CG, Kayed R: Poloxamer 188 copolymer membrane sealant rescues toxicity of amyloid oligomers in vitro. J Mol Biol; 2009 Aug 21;391(3):577-85
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  • [Title] Poloxamer 188 copolymer membrane sealant rescues toxicity of amyloid oligomers in vitro.
  • Amyloid oligomers and protofibrils increase cell membrane permeability, eventually leading to cell death.
  • Here, we demonstrate that amyloid oligomer toxicity and membrane permeabilization can be reversed using the membrane sealant copolymer poloxamer 188.
  • The data indicate that amyloid oligomer toxicity is caused by defects in the lipid bilayer of the type that are sealed by poloxamer 188.
  • Our results also suggest the possibility of using polymer-based membrane sealants to prevent or reverse amyloid oligomer toxicity in vivo.
  • Because the ability to permeabilize membranes is a generic property of amyloid oligomers, this therapeutic approach may be effective for the treatment of many degenerative diseases caused in part by the interaction of misfolded proteins with cell membranes, as in Alzheimer's disease, type II diabetes, and a host of others.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Cell Membrane / drug effects. Oligopeptides / toxicity. Poloxamer / pharmacology
  • [MeSH-minor] Cell Line, Tumor. Cell Membrane Permeability. Cell Survival / drug effects. Humans. Lipid Bilayers / metabolism. Membrane Fluidity

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  • (PMID = 19524592.001).
  • [ISSN] 1089-8638
  • [Journal-full-title] Journal of molecular biology
  • [ISO-abbreviation] J. Mol. Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Lipid Bilayers; 0 / Oligopeptides; 106392-12-5 / Poloxamer
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58. Patel JR, Brewer GJ: Age-related changes to tumor necrosis factor receptors affect neuron survival in the presence of beta-amyloid. J Neurosci Res; 2008 Aug 1;86(10):2303-13
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  • [Title] Age-related changes to tumor necrosis factor receptors affect neuron survival in the presence of beta-amyloid.
  • Inflammation including local accumulations of tumor necrosis factor alpha (TNF-alpha) is a part of Alzheimer's disease pathology and may exacerbate age-related neurodegeneration.
  • Age-related changes in susceptibility to TNF-alpha through TNF receptor 1 (TNFR1) and receptor 2 (TNFR2) expression could increase susceptibility to beta-amyloid (1-42, Abeta42).

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  • (PMID = 18418902.001).
  • [ISSN] 1097-4547
  • [Journal-full-title] Journal of neuroscience research
  • [ISO-abbreviation] J. Neurosci. Res.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / AG013435-09; United States / NIA NIH HHS / AG / R01 AG013435; United States / NIA NIH HHS / AG / AG13435; United States / NIA NIH HHS / AG / R01 AG013435-09
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / RNA, Messenger; 0 / Receptors, Tumor Necrosis Factor
  • [Other-IDs] NLM/ NIHMS36233; NLM/ PMC2562897
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59. Bucciantini M, Cecchi C: Biological membranes as protein aggregation matrices and targets of amyloid toxicity. Methods Mol Biol; 2010;648:231-43
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  • [Title] Biological membranes as protein aggregation matrices and targets of amyloid toxicity.
  • Aberrantly folded proteins and peptides are hallmarks of amyloid diseases.
  • A deeper knowledge of the pathways leading to the formation of amyloid protein aggregates and of the mechanisms of their cytotoxicity is fundamental for a better understanding of several human diseases with amyloid deposition.
  • In general, different cell susceptibility to toxic protein aggregates depends on the efficiency of different cell types to accumulate amyloid precursors at their plasma membrane with subsequent growth of pre-fibrillar and fibrillar entities, resulting in membrane perturbation and cell damage.
  • [MeSH-major] Amyloid / chemistry. Amyloid / toxicity. Microscopy / methods
  • [MeSH-minor] Cell Line, Tumor. Flow Cytometry. Fluorescent Antibody Technique. Humans. Membranes / drug effects. Membranes / ultrastructure. Microscopy, Atomic Force. Microscopy, Confocal. Protein Structure, Quaternary

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  • (PMID = 20700716.001).
  • [ISSN] 1940-6029
  • [Journal-full-title] Methods in molecular biology (Clifton, N.J.)
  • [ISO-abbreviation] Methods Mol. Biol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid
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60. Corrêa DH, Ramos CH: Insights on the structure of amyloid fibrils from site-directed mutagenesis. Protein Pept Lett; 2009;16(12):1519-25
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  • [Title] Insights on the structure of amyloid fibrils from site-directed mutagenesis.
  • To test the hypothesis that the ability to form ordered beta-rich amyloid fibers with identical structures is a generic property of proteins we present a study on the overall structures of fibers formed by apomyoglobin mutants that either stabilize or destabilize the native state or the intermediate.
  • Our results indicate that, at least at the macroscopic level, ordered beta-rich amyloid fibers have similar structures.
  • [MeSH-major] Amyloid beta-Peptides / chemistry. Apoproteins / chemistry. Myoglobin / chemistry
  • [MeSH-minor] Animals. Cell Line, Tumor. Cell Survival. Circular Dichroism. Mice. Mutagenesis, Site-Directed. Mutation / genetics. Protein Conformation. Protein Folding. Sperm Whale

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  • (PMID = 20001915.001).
  • [ISSN] 1875-5305
  • [Journal-full-title] Protein and peptide letters
  • [ISO-abbreviation] Protein Pept. Lett.
  • [Language] eng
  • [Grant] United States / FIC NIH HHS / TW / R03 TW 007437
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Apoproteins; 0 / Myoglobin; 0 / apomyoglobin
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61. Posthuma D, Meulenbelt I, de Craen AJ, de Geus EJ, Slagboom PE, Boomsma DI, Westendorp RG: Human cytokine response to ex vivo amyloid-beta stimulation is mediated by genetic factors. Twin Res Hum Genet; 2005 Apr;8(2):132-7
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  • [Title] Human cytokine response to ex vivo amyloid-beta stimulation is mediated by genetic factors.
  • Through its ability to induce the enhanced release and production of cytokines, amyloid-beta is responsible for the chronic inflammatory response that contributes to Alzheimer's disease (AD).
  • Determining whether the response of monocytes to amyloid-beta stimulation is under genetic control may help understand the basis of why some people are more prone to develop neuronal degeneration than others.
  • In the current study we investigated the heritability of the cytokine (IL-10, IL-6, IL-1beta, IL-1ra, TNF-alpha) production capacity upon ex vivo stimulation with amyloid-beta in whole blood samples of 222 twins and 85 singleton siblings from 139 extended twin families.
  • It was found that individual differences in amyloid-beta induced cytokine production capacity are to a large extent of genetic origin, with heritability estimates ranging from 55% (IL-1beta) to 68% (IL-6).
  • We conclude that genes influencing amyloid-beta-induced cytokine response may provide clues to the progression of AD pathology.
  • [MeSH-major] Amyloid beta-Peptides / pharmacology. Cytokines / drug effects
  • [MeSH-minor] Adolescent. Adult. Aged. Environment. Escherichia coli. Female. Genetic Variation / genetics. Humans. Interleukin-1 / genetics. Interleukin-10 / genetics. Interleukin-6 / genetics. Lipopolysaccharides / pharmacology. Male. Middle Aged. Monocytes / drug effects. Monocytes / metabolism. Receptors, Interleukin-1 / antagonists & inhibitors. Sex Factors. Tumor Necrosis Factor-alpha / drug effects. Tumor Necrosis Factor-alpha / genetics. Twins, Dizygotic / genetics. Twins, Monozygotic / genetics

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  • (PMID = 15901476.001).
  • [ISSN] 1832-4274
  • [Journal-full-title] Twin research and human genetics : the official journal of the International Society for Twin Studies
  • [ISO-abbreviation] Twin Res Hum Genet
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Twin Study
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Cytokines; 0 / Interleukin-1; 0 / Interleukin-6; 0 / Lipopolysaccharides; 0 / Receptors, Interleukin-1; 0 / Tumor Necrosis Factor-alpha; 130068-27-8 / Interleukin-10
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62. Huang J, May JM: Ascorbic acid protects SH-SY5Y neuroblastoma cells from apoptosis and death induced by beta-amyloid. Brain Res; 2006 Jun 30;1097(1):52-8
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  • [Title] Ascorbic acid protects SH-SY5Y neuroblastoma cells from apoptosis and death induced by beta-amyloid.
  • beta-Amyloid causes apoptosis and death in cultured neurons that may be mediated by generation of reactive oxygen species.
  • Treatment of cells with 2-10 microM beta-amyloid(25-35) decreased both intracellular ascorbate and GSH without affecting rates of ascorbate transport, which suggests that the peptide induces an oxidant stress in the cells.
  • Overnight culture of cells with 10-20 microM beta-amyloid(25-35) induced apoptosis in SH-SY5Y cells when measured as externalization of phosphatidylserine by annexin V binding, as DNA fragmentation in the TUNEL assay, and as caspase-3 activity in cell lysates.
  • In addition to preventing apoptosis, ascorbate loading of SH-SY5Y cells also decreased basal rates of generation of endogenous beta-amyloid.
  • Together, these results support the notion that beta-amyloid induces apoptosis and death in neurons due to oxidant stress and suggest that intracellular ascorbate effectively prevents this toxicity.
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Apoptosis / drug effects. Ascorbic Acid / therapeutic use. Neuroblastoma / drug therapy. Neuroprotective Agents / therapeutic use
  • [MeSH-minor] Cell Death / drug effects. Cell Death / physiology. Cell Line, Tumor. Dose-Response Relationship, Drug. Humans

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  • (PMID = 16725131.001).
  • [ISSN] 0006-8993
  • [Journal-full-title] Brain research
  • [ISO-abbreviation] Brain Res.
  • [Language] eng
  • [Grant] United States / NIA NIH HHS / AG / AG 23138; United States / NIDDK NIH HHS / DK / DK 20593
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Neuroprotective Agents; PQ6CK8PD0R / Ascorbic Acid
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63. Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR: The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J; 2007 Aug;21(10):2312-22
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  • [Title] The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.
  • Clusterin is an extracellular chaperone present in all disease-associated extracellular amyloid deposits, but its roles in amyloid formation and protein deposition in vivo are poorly understood.
  • The current study initially aimed to characterize the effects of clusterin on amyloid formation in vitro by a panel of eight protein substrates.
  • Two of the substrates (Alzheimer's beta peptide and a PI3-SH3 domain) were then used in further experiments to examine the effects of clusterin on amyloid cytotoxicity and to probe the mechanism of clusterin action.
  • We show that clusterin exerts potent effects on amyloid formation, the nature and extent of which vary greatly with the clusterin:substrate ratio, and provide evidence that these effects are exerted via interactions with prefibrillar species that share common structural features.
  • However, when clusterin is present at much higher but still substoichiometric levels (e.g., a molar ratio of clusterin:substrate=1:10), it potently inhibits amyloid formation and provides substantial cytoprotection.
  • [MeSH-minor] Amyloid / drug effects. Amyloid / metabolism. Animals. Cattle. Cell Line, Tumor. Humans. Microscopy, Fluorescence. Neuroblastoma. Phosphatidylinositol 3-Kinases / metabolism. Recombinant Fusion Proteins / metabolism. Recombinant Fusion Proteins / pharmacology

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  • (PMID = 17412999.001).
  • [ISSN] 1530-6860
  • [Journal-full-title] FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • [ISO-abbreviation] FASEB J.
  • [Language] eng
  • [Grant] United Kingdom / Biotechnology and Biological Sciences Research Council / / BB/E019927/1; United Kingdom / Wellcome Trust / /
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; 0 / CLU protein, human; 0 / Clusterin; 0 / Recombinant Fusion Proteins; EC 2.7.1.- / Phosphatidylinositol 3-Kinases
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64. Talab R, Valis M, Rehak S, Krejsek J: Abnormalities of tau-protein and beta-amyloid in brain ventricle cerebrospinal fluid. Neuro Endocrinol Lett; 2009;30(5):647-51
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  • [Title] Abnormalities of tau-protein and beta-amyloid in brain ventricle cerebrospinal fluid.
  • OBJECTIVE: Determination of various biomarkers, such as beta-amyloid, tau-protein, phosphorylated tau-protein in CSF and their sensitivity and specificity in neurodegenerative brain processes, in particular Alzheimer Dementia (AD), has been recently investigated to monitor their abnormalities in the CSF at early stages of diseases before the clinical manifestation.
  • DESIGN AND SETTING: In the pilot group of our patients (10 men / 5 women) who underwent a drainage neurosurgical procedure for diagnosis of hydrocephalus, CSF was obtained from the brain ventricles and the influence of a different compartment of the CSF on the level of biomarkers, tau-protein and beta-amyloid, was investigated.
  • RESULTS: The mean tau-protein level for all 15 patients was 812.0 pg/ml, with median value 363.7 pg/ml; while mean beta-amyloid level for all 15 patients was 526.7 pg/ml, with median value 239.5 pg/ml, respectively.
  • The abnormal tau-protein and beta-amyloid levels were found in the subgroup of patients in whom hydrocephalus was caused by a severe pathological process, such as brain tumor.
  • The beta-amyloid values were significantly lower also in comparison with our previously published results in patients with AD in the CSF obtained by lumbar puncture in the spinal canal.
  • [MeSH-major] Amyloid beta-Peptides / cerebrospinal fluid. tau Proteins / cerebrospinal fluid

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  • (PMID = 20035270.001).
  • [ISSN] 0172-780X
  • [Journal-full-title] Neuro endocrinology letters
  • [ISO-abbreviation] Neuro Endocrinol. Lett.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] Sweden
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Biomarkers; 0 / tau Proteins
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65. Wang C, Wang J, Liu D, Wang Z: Gold nanoparticle-based colorimetric sensor for studying the interactions of beta-amyloid peptide with metallic ions. Talanta; 2010 Mar 15;80(5):1626-31
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  • [Title] Gold nanoparticle-based colorimetric sensor for studying the interactions of beta-amyloid peptide with metallic ions.
  • In this paper, a kind of beta-amyloid peptide (Abeta1-16) conjugated gold nanoparticles (Abeta1-16@GNPs) are prepared and employed as colorimetric indicator for studying the interaction of beta-amyloid peptide with metallic ions (e.g.
  • The experimental results indicate that Zn(2+) can interact with Abeta1-16 and form Zn(2+)-beta-amyloid peptide complexes.
  • In particular, in the presence of Zn(2+), a time-dependent interaction of cells with Abeta1-16@GNPs has been observed that may suggest different expression levels of beta-amyloid peptide related proteins in various cell cycles.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Calcium / metabolism. Colorimetry / methods. Gold / chemistry. Metal Nanoparticles / chemistry. Zinc / metabolism
  • [MeSH-minor] Biosensing Techniques / methods. Cell Line, Tumor. Cell Survival. Humans. Ions / metabolism. Peptide Fragments / chemistry. Peptide Fragments / metabolism

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  • [Copyright] Copyright (c) 2009 Elsevier B.V. All rights reserved.
  • (PMID = 20152387.001).
  • [ISSN] 1873-3573
  • [Journal-full-title] Talanta
  • [ISO-abbreviation] Talanta
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Ions; 0 / Peptide Fragments; 7440-57-5 / Gold; J41CSQ7QDS / Zinc; SY7Q814VUP / Calcium
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66. Menéndez-González M, Pérez-Pinera P, Martínez-Rivera M, Calatayud MT, Blázquez Menes B: APP processing and the APP-KPI domain involvement in the amyloid cascade. Neurodegener Dis; 2005;2(6):277-83
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  • [Title] APP processing and the APP-KPI domain involvement in the amyloid cascade.
  • Protein and mRNA KPI(+)APP levels are elevated in Alzheimer's disease (AD) brain and are associated with increased amyloid beta deposition.
  • In the last years increasing evidence on multiple points in the amyloid cascade where KPI(+)APP is involved has been accumulated, admitting an outstanding position in the pathogenesis of AD to the KPI domain.
  • This review focuses on the APP processing, the molecular activity of KPI and its physiological and pathological roles and the KPI involvement in the amyloid cascade through the nerve growth factor, the lipoprotein receptor-related protein, the tumor necrosis factor-alpha converting enzyme and the Notch1 protein.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid / metabolism. Amyloid beta-Peptides / metabolism. Protease Inhibitors / metabolism

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  • (PMID = 16909010.001).
  • [ISSN] 1660-2854
  • [Journal-full-title] Neuro-degenerative diseases
  • [ISO-abbreviation] Neurodegener Dis
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] Switzerland
  • [Chemical-registry-number] 0 / Amyloid; 0 / Amyloid beta-Peptides; 0 / Protease Inhibitors
  • [Number-of-references] 68
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67. Kim EA, Hahn HG, Kim TU, Choi SY, Cho SW: Attenuation of beta-amyloid-induced neuroinflammation by KHG21834 in vivo. BMB Rep; 2010 Jun;43(6):413-8

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  • [Title] Attenuation of beta-amyloid-induced neuroinflammation by KHG21834 in vivo.
  • Beta-Amyloid (ABeta)-induced neuroinflammation is one of the key events in the development of neurodegenerative disease.
  • In vivo intracerebroventricular infusion of KHG21834 leads to decreases in the numbers of activated astrocytes and microglia and level of proinflammatory cytokines such as interleukin- 1Beta and tumor necrosis factor-alpha induced by ABeta in the hippocampus.
  • This suppression of neuroinflammation is associated with decreased neuron loss, restoration of synaptic dysfunction biomarkers in the hippocampus to control level, and diminished amyloid deposition.
  • [MeSH-major] Amyloid beta-Peptides / physiology. Benzothiazoles / pharmacology. Cerebral Cortex / drug effects. Inflammation / prevention & control. Mesencephalon / drug effects

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  • (PMID = 20587331.001).
  • [ISSN] 1976-670X
  • [Journal-full-title] BMB reports
  • [ISO-abbreviation] BMB Rep
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Korea (South)
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Benzothiazoles; 0 / KHG21834
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68. Ohyagi Y, Tabira T: Intracellular amyloid beta-protein and its associated molecules in the pathogenesis of Alzheimer's disease. Mini Rev Med Chem; 2006 Oct;6(10):1075-80
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Intracellular amyloid beta-protein and its associated molecules in the pathogenesis of Alzheimer's disease.
  • Amyloid beta-protein (Abeta) plays a pivotal role in Alzheimer's disease (AD).
  • [MeSH-major] Alzheimer Disease / genetics. Alzheimer Disease / physiopathology. Amyloid beta-Peptides / metabolism. Intracellular Space / metabolism. Peptide Fragments / metabolism
  • [MeSH-minor] Amino Acid Sequence. Animals. Apoptosis / physiology. Humans. Molecular Sequence Data. Neurons / metabolism. Tumor Suppressor Protein p53 / metabolism

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  • (PMID = 17073707.001).
  • [ISSN] 1389-5575
  • [Journal-full-title] Mini reviews in medicinal chemistry
  • [ISO-abbreviation] Mini Rev Med Chem
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / Tumor Suppressor Protein p53; 0 / amyloid beta-protein (1-42)
  • [Number-of-references] 65
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69. Sommer G, Kralisch S, Lipfert J, Weise S, Krause K, Jessnitzer B, Lössner U, Blüher M, Stumvoll M, Fasshauer M: Amyloid precursor protein expression is induced by tumor necrosis factor alpha in 3T3-L1 adipocytes. J Cell Biochem; 2009 Dec 15;108(6):1418-22

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid precursor protein expression is induced by tumor necrosis factor alpha in 3T3-L1 adipocytes.
  • Amyloid precursor protein (APP) has been characterized as an adipocyte-secreted protein that might contribute to obesity-related insulin resistance, inflammation, and dementia.
  • In the current study, regulation of APP by the proinflammatory and insulin resistance-inducing cytokine tumor necrosis factor (TNF) alpha was determined in 3T3-L1 adipocytes.
  • [MeSH-major] Adipocytes / metabolism. Amyloid beta-Protein Precursor / metabolism. Tumor Necrosis Factor-alpha / pharmacology

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  • (PMID = 19862700.001).
  • [ISSN] 1097-4644
  • [Journal-full-title] Journal of cellular biochemistry
  • [ISO-abbreviation] J. Cell. Biochem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor; 0 / RNA, Messenger; 0 / Tumor Necrosis Factor-alpha
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70. Awasthi A, Matsunaga Y, Yamada T: Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides. Exp Neurol; 2005 Dec;196(2):282-9
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  • [Title] Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides.
  • Amyloid beta 1-42 (Abeta42) and Abeta17-42 are major constituents of diffuse plaque in brains with Alzheimer's disease (AD).
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Apoptosis / drug effects. Caspases / metabolism. Neurons / drug effects. Peptide Fragments / pharmacology
  • [MeSH-minor] Analysis of Variance. Cell Line, Tumor. Cell Proliferation / drug effects. Dose-Response Relationship, Drug. Drug Interactions. Enzyme Activation / drug effects. Enzyme Inhibitors / pharmacology. Flow Cytometry / methods. Humans. Lysosomes / drug effects. Neuroblastoma. Tetrazolium Salts. Thiazoles

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  • (PMID = 16137679.001).
  • [ISSN] 0014-4886
  • [Journal-full-title] Experimental neurology
  • [ISO-abbreviation] Exp. Neurol.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Enzyme Inhibitors; 0 / Peptide Fragments; 0 / Tetrazolium Salts; 0 / Thiazoles; 298-93-1 / thiazolyl blue; EC 3.4.22.- / Caspases
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71. Kudo T, Okumura M, Imaizumi K, Araki W, Morihara T, Tanimukai H, Kamagata E, Tabuchi N, Kimura R, Kanayama D, Fukumori A, Tagami S, Okochi M, Kubo M, Tanii H, Tohyama M, Tabira T, Takeda M: Altered localization of amyloid precursor protein under endoplasmic reticulum stress. Biochem Biophys Res Commun; 2006 Jun 2;344(2):525-30
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  • [Title] Altered localization of amyloid precursor protein under endoplasmic reticulum stress.
  • Following the amyloid cascade hypothesis, we therefore attempted to investigate the effects of ER stress on amyloid-beta peptide (Abeta) generation.
  • In this study, we found that ER stress altered the localization of amyloid precursor protein (APP) from late compartments to early compartments of the secretory pathway, and decreased the level of Abeta 40 and Abeta 42 release by beta- and gamma-cutting.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Endoplasmic Reticulum / metabolism. Endoplasmic Reticulum / pathology. Neuroblastoma / metabolism. Neuroblastoma / pathology. Oxidative Stress
  • [MeSH-minor] Cell Line, Tumor. Humans. Tissue Distribution

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  • (PMID = 16630560.001).
  • [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 / Amyloid beta-Peptides
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72. Xie Z, Romano DM, Tanzi RE: RNA interference-mediated silencing of X11alpha and X11beta attenuates amyloid beta-protein levels via differential effects on beta-amyloid precursor protein processing. J Biol Chem; 2005 Apr 15;280(15):15413-21
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] RNA interference-mediated silencing of X11alpha and X11beta attenuates amyloid beta-protein levels via differential effects on beta-amyloid precursor protein processing.
  • Processing of the beta-amyloid precursor protein (APP) plays a key role in Alzheimer disease neuropathogenesis.
  • APP is cleaved by beta- and alpha-secretase to produce APP-C99 and APP-C83, which are further cleaved by gamma-secretase to produce amyloid beta-protein (Abeta) and p3, respectively.
  • [MeSH-major] Adaptor Proteins, Signal Transducing / genetics. Amyloid beta-Peptides / chemistry. Amyloid beta-Protein Precursor / chemistry. Carrier Proteins / genetics. Gene Silencing. Nerve Tissue Proteins / genetics. RNA Interference
  • [MeSH-minor] Amino Acid Motifs. Blotting, Western. Cadherins. Cell Line, Tumor. Electroporation. Enzyme-Linked Immunosorbent Assay. Humans. Protein Binding. RNA, Small Interfering / metabolism. Time Factors. Transfection

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  • (PMID = 15699037.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Grant] United States / NIA NIH HHS / AG / AG 00294-17; United States / NIA NIH HHS / AG / AG 014713-07; United States / NIMH NIH HHS / MH / MH 60009-03; United States / NIA NIH HHS / AG / P50 AG05134
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / APBA1 protein, human; 0 / APBA2 protein, human; 0 / Adaptor Proteins, Signal Transducing; 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Cadherins; 0 / Carrier Proteins; 0 / Nerve Tissue Proteins; 0 / RNA, Small Interfering
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73. Janusz M, Woszczyna M, Lisowski M, Kubis A, Macała J, Gotszalk T, Lisowski J: Ovine colostrum nanopeptide affects amyloid beta aggregation. FEBS Lett; 2009 Jan 5;583(1):190-6
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  • [Title] Ovine colostrum nanopeptide affects amyloid beta aggregation.
  • The aim of the present studies was to investigate whether nanopeptide fragment of PRP (NP) - one of the PRP complex components can affect aggregation of amyloid beta (Abeta1-42).
  • Results presented suggest that NP can directly interact with amyloid beta, inhibit its aggregation and disrupt existing aggregates acting as a beta sheet breaker and reduce toxicity induced by aggregated forms of Abeta.
  • [MeSH-major] Amyloid beta-Peptides / drug effects. Nanostructures. Oligopeptides / pharmacology. Peptide Fragments / drug effects. Sheep, Domestic / metabolism
  • [MeSH-minor] Animals. Cell Line, Tumor. Cell Survival / drug effects. Circular Dichroism. Fluorescent Dyes / chemistry. Microscopy, Atomic Force. Protein Structure, Secondary / drug effects. Rats. Thiazoles / chemistry

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  • (PMID = 19084010.001).
  • [ISSN] 1873-3468
  • [Journal-full-title] FEBS letters
  • [ISO-abbreviation] FEBS Lett.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Fluorescent Dyes; 0 / Oligopeptides; 0 / Peptide Fragments; 0 / Thiazoles; 0 / amyloid beta-protein (1-42); 0 / valyl-glutamyl-seryl-tyrosyl-valyl-prolyl-leucyl-phenylalanylproline; 2390-54-7 / thioflavin T
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74. Matharu B, El-Agnaf O, Razvi A, Austen BM: Development of retro-inverso peptides as anti-aggregation drugs for β-amyloid in Alzheimer's disease. Peptides; 2010 Oct;31(10):1866-72
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Development of retro-inverso peptides as anti-aggregation drugs for β-amyloid in Alzheimer's disease.
  • There is much evidence to suggest that β-amyloid protein (Aβ) aggregation in the brain leading to deposits is an important step in the development of AD.
  • Here we report that retro-inversion of these sequences increases efficacy of the peptides in the inhibition of aggregation and toxicity of β-amyloid.
  • [MeSH-major] Alzheimer Disease / pathology. Amyloid beta-Peptides / chemistry. Amyloid beta-Peptides / metabolism. Peptides / chemistry. Peptides / metabolism
  • [MeSH-minor] Amino Acid Sequence. Animals. Cell Line, Tumor. Humans. Molecular Sequence Data. Neurons / cytology. Neurons / drug effects. Neuroprotective Agents / chemistry. Neuroprotective Agents / metabolism. Neuroprotective Agents / therapeutic use. Peptide Fragments / toxicity. Protein Binding

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  • [Copyright] Copyright © 2010 Elsevier Inc. All rights reserved.
  • (PMID = 20633587.001).
  • [ISSN] 1873-5169
  • [Journal-full-title] Peptides
  • [ISO-abbreviation] Peptides
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Neuroprotective Agents; 0 / Peptide Fragments; 0 / Peptides; 0 / amyloid beta-protein (1-40)
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75. Zampagni M, Evangelisti E, Cascella R, Liguri G, Becatti M, Pensalfini A, Uberti D, Cenini G, Memo M, Bagnoli S, Nacmias B, Sorbi S, Cecchi C: Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane. J Mol Med (Berl); 2010 Jun;88(6):597-608
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  • [Title] Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane.
  • Here, we report that lipid rafts, ordered membrane microdomains, are chronic mediators of Abeta-induced lipid peroxidation in SH-SY5Y human neuroblastoma cells overexpressing amyloid precursor protein (APPwt) and APPV717G genes and in fibroblasts bearing the APPV717I gene mutation.
  • Moreover, amyloid pickup at the oxidative-damaged domains was prevented by enhanced cholesterol levels, anti-ganglioside (GM1) antibodies, the B subunit of cholera toxin and lipid raft structure alteration.
  • An enhanced structural rigidity of the detergent-resistant domains, isolated from APPwt and APPV717G cells and exposed to ADDLs, indicates a specific perturbation of raft physicochemical features in cells facing increased amyloid assembly at the membrane surface.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Amyloid beta-Protein Precursor / metabolism. Lipid Peroxidation. Membrane Microdomains / metabolism
  • [MeSH-minor] Animals. Cell Line, Tumor. Cholesterol / chemistry. Cholesterol / metabolism. Fibroblasts / cytology. Fibroblasts / physiology. Humans. Mutation. Oxidation-Reduction

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  • (PMID = 20217034.001).
  • [ISSN] 1432-1440
  • [Journal-full-title] Journal of molecular medicine (Berlin, Germany)
  • [ISO-abbreviation] J. Mol. Med.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 97C5T2UQ7J / Cholesterol
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76. Lee EK, Park YW, Shin DY, Mook-Jung I, Yoo YJ: Cytosolic amyloid-beta peptide 42 escaping from degradation induces cell death. Biochem Biophys Res Commun; 2006 Jun 2;344(2):471-7
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  • [Title] Cytosolic amyloid-beta peptide 42 escaping from degradation induces cell death.
  • Accumulating evidence suggests that intracellular amyloid-beta (Abeta) peptide triggers the early pathological events in Alzheimer's disease (AD).
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Apoptosis. Cytosol / metabolism. Neuroblastoma / metabolism. Neuroblastoma / pathology. Peptide Fragments / metabolism
  • [MeSH-minor] Cell Line, Tumor. Humans

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  • (PMID = 16630565.001).
  • [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 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / amyloid beta-protein (1-42)
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77. Morihara T, Teter B, Yang F, Lim GP, Boudinot S, Boudinot FD, Frautschy SA, Cole GM: Ibuprofen suppresses interleukin-1beta induction of pro-amyloidogenic alpha1-antichymotrypsin to ameliorate beta-amyloid (Abeta) pathology in Alzheimer's models. Neuropsychopharmacology; 2005 Jun;30(6):1111-20
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  • [Title] Ibuprofen suppresses interleukin-1beta induction of pro-amyloidogenic alpha1-antichymotrypsin to ameliorate beta-amyloid (Abeta) pathology in Alzheimer's models.
  • Ibuprofen reduces amyloid (Abeta) pathology in some transgenic models, but the precise mechanisms remain unclear.
  • Although some reports show select NSAIDs inhibit amyloid production in vitro, the possibility that in vivo suppression of amyloid pathology occurs independent of Abeta production has not been ruled out.
  • Among these, ACT, a factor whose overexpression accelerates amyloid pathology, was reduced by ibuprofen both in vivo and in vitro.
  • We present evidence supporting the hypothesis that ibuprofen-dependent amyloid reduction is mediated by inhibition of an alternate pathway (IL-1beta and its downstream target ACT).

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  • (PMID = 15688088.001).
  • [ISSN] 0893-133X
  • [Journal-full-title] Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology
  • [ISO-abbreviation] Neuropsychopharmacology
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / AG10685; United States / NIA NIH HHS / AG / AG16793; United States / NIA NIH HHS / AG / R01 AG013741; United States / NIA NIH HHS / AG / P50 AG016570; United States / NIA NIH HHS / AG / AG13471; United States / NINDS NIH HHS / NS / NS43946; United States / NIA NIH HHS / AG / R01 AG010685; United States / NCCIH NIH HHS / AT / R01 AT003008; United States / NIA NIH HHS / AG / AG00962
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Acute-Phase Proteins; 0 / Anti-Inflammatory Agents, Non-Steroidal; 0 / Apolipoproteins E; 0 / Interleukin-1; 0 / Serine Proteinase Inhibitors; 0 / alpha 1-Antichymotrypsin; EC 3.4.- / Amyloid Precursor Protein Secretases; EC 3.4.- / Endopeptidases; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC 3.4.23.46 / Bace1 protein, mouse; WK2XYI10QM / Ibuprofen
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78. Moussa CE: Parkin attenuates wild-type tau modification in the presence of beta-amyloid and alpha-synuclein. J Mol Neurosci; 2009 Jan;37(1):25-36
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  • [Title] Parkin attenuates wild-type tau modification in the presence of beta-amyloid and alpha-synuclein.
  • Deposits of amyloid proteins, including Abeta and alpha-synuclein coexist in the brains of patients with dementia with Lewy bodies; however, it is not known how either of them interacts with tau to provoke neurofibrillary tangle formation across the tauopathies.
  • Parkin attenuates four-repeat human tau, but not mutant P301L, hyperphosphorylation in the presence of intracellular Abeta(1-42), or alpha-synuclein and decreases GSK-3beta activity in amyloid-stressed M17 human neuroblastoma cells.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. Peptide Fragments / metabolism. Tauopathies / metabolism. Ubiquitin-Protein Ligases / metabolism. alpha-Synuclein / metabolism. tau Proteins / metabolism
  • [MeSH-minor] Cell Line, Tumor. Glycogen Synthase Kinase 3 / metabolism. Humans. Neuroblastoma. Parkinson Disease / metabolism. Phosphorylation / physiology

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  • [ErratumIn] J Mol Neurosci. 2009 Mar;37(3):301
  • (PMID = 18561034.001).
  • [ISSN] 0895-8696
  • [Journal-full-title] Journal of molecular neuroscience : MN
  • [ISO-abbreviation] J. Mol. Neurosci.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / alpha-Synuclein; 0 / amyloid beta-protein (1-42); 0 / tau Proteins; EC 2.7.11.1 / glycogen synthase kinase 3 beta; EC 2.7.11.26 / Glycogen Synthase Kinase 3; EC 6.3.2.19 / Ubiquitin-Protein Ligases; EC 6.3.2.19 / parkin protein
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79. Gamerdinger M, Clement AB, Behl C: Cholesterol-like effects of selective cyclooxygenase inhibitors and fibrates on cellular membranes and amyloid-beta production. Mol Pharmacol; 2007 Jul;72(1):141-51
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Cholesterol-like effects of selective cyclooxygenase inhibitors and fibrates on cellular membranes and amyloid-beta production.
  • Strong evidence suggests a mechanistic link between cholesterol metabolism and the formation of amyloid-beta peptides, the principal constituents of senile plaques found in the brains of patients with Alzheimer's disease.
  • Here, we show that several fibrates and diaryl heterocycle cyclooxygenase inhibitors, among them the commonly used drugs fenofibrate and celecoxib, exhibit effects similar to those of cholesterol on cellular membranes and amyloid precursor protein (APP) processing.
  • According to this hypothesis, both cholesterol and the examined compounds stimulated the beta-secretase cleavage of APP, resulting in a massive increase of secreted amyloid-beta peptides.
  • The membrane-ordering potential of the drugs was observed in a cell-free assay, suggesting that the amyloid-beta promoting effect was analog to cholesterol due to primary effect on membrane rigidity.
  • [MeSH-major] Amyloid beta-Peptides / biosynthesis. Cell Membrane / drug effects. Cholesterol / pharmacology. Clofibrate / pharmacology. Cyclooxygenase Inhibitors / pharmacology. Fenofibrate / pharmacology
  • [MeSH-minor] Amyloid Precursor Protein Secretases / metabolism. Amyloid beta-Protein Precursor / metabolism. Animals. Aspartic Acid Endopeptidases / metabolism. CHO Cells. Celecoxib. Cell Line, Tumor. Cricetinae. Cricetulus. Mice. Pyrazoles / pharmacology. Sulfonamides / pharmacology

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  • (PMID = 17395689.001).
  • [ISSN] 0026-895X
  • [Journal-full-title] Molecular pharmacology
  • [ISO-abbreviation] Mol. Pharmacol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Cyclooxygenase Inhibitors; 0 / Pyrazoles; 0 / Sulfonamides; 97C5T2UQ7J / Cholesterol; EC 3.4.- / Amyloid Precursor Protein Secretases; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC 3.4.23.46 / BACE1 protein, human; HPN91K7FU3 / Clofibrate; JCX84Q7J1L / Celecoxib; U202363UOS / Fenofibrate
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80. Shimada S, Harada H, Ishizawa K, Hirose T: Retroperitoneal lipomatous angiomyolipoma associated with amyloid deposition masquerading as well-differentiated liposarcoma. Pathol Int; 2006 Oct;56(10):638-41
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  • [Title] Retroperitoneal lipomatous angiomyolipoma associated with amyloid deposition masquerading as well-differentiated liposarcoma.
  • Reported herein is a case of retroperitoneal angiomyolipoma associated with amyloid deposition, masquerading as well-differentiated liposarcoma.
  • A 16 x 13 cm lipomatous tumor was resected from the perirenal retroperitoneum of a 71-year-old woman.
  • Microscopically, the tumor was exclusively composed of mature adipose tissue and abnormal thick blood vessels, but bundles of smooth muscle were lacking.
  • In addition, amyloid was deposited between fat cells.
  • Real-time polymerase chain reaction failed to demonstrate the amplification of the murine double-minute type 2 gene and cyclin-dependent kinase 4 gene in this tumor.
  • Therefore, the tumor was diagnosed as lipomatous angiomyolipoma.
  • After the diagnosis, it was found that the patient had multiple myeloma and cardiac amyloidosis, suggesting that the amyloid deposition within the tumor was a complication of the myeloma.
  • [MeSH-major] Amyloid / metabolism. Angiomyolipoma / diagnosis. Angiomyolipoma / metabolism. Liposarcoma / diagnosis. Liposarcoma / metabolism. Retroperitoneal Neoplasms / diagnosis. Retroperitoneal Neoplasms / metabolism

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  • (PMID = 16984623.001).
  • [ISSN] 1320-5463
  • [Journal-full-title] Pathology international
  • [ISO-abbreviation] Pathol. Int.
  • [Language] eng
  • [Publication-type] Case Reports; Journal Article
  • [Publication-country] Australia
  • [Chemical-registry-number] 0 / Amyloid; EC 2.7.11.22 / Cyclin-Dependent Kinase 4; EC 6.3.2.19 / Proto-Oncogene Proteins c-mdm2
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81. Culicchia F, Cui JG, Li YY, Lukiw WJ: Upregulation of beta-amyloid precursor protein expression in glioblastoma multiforme. Neuroreport; 2008 Jun 11;19(9):981-5
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  • [Title] Upregulation of beta-amyloid precursor protein expression in glioblastoma multiforme.
  • This study examined proinflammatory and neurodegenerative gene expression in five American Tissue Culture Collection glioma and glioblastoma multiforme tumor cell lines and in 14 glioma and glioblastoma samples obtained from human brain biopsy.
  • In contrast, proinflammatory cyclooxygenase-2, cytosolic phospholipase A2, IL-1beta, and beta-amyloid precursor protein expression levels were found to be significantly upregulated.
  • [MeSH-major] Amyloid beta-Protein Precursor / metabolism. Brain Neoplasms / metabolism. Glioblastoma / metabolism. Up-Regulation / physiology
  • [MeSH-minor] Adult. Antigens, Human Platelet / genetics. Antigens, Human Platelet / metabolism. Cell Line, Tumor. Cyclooxygenase 2 / genetics. Cyclooxygenase 2 / metabolism. Female. Humans. Interleukin-1beta / metabolism. Male. Middle Aged. RNA, Messenger / metabolism

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  • (PMID = 18521005.001).
  • [ISSN] 0959-4965
  • [Journal-full-title] Neuroreport
  • [ISO-abbreviation] Neuroreport
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor; 0 / Antigens, Human Platelet; 0 / Interleukin-1beta; 0 / RNA, Messenger; 0 / human platelet antigen 1b; EC 1.14.99.1 / Cyclooxygenase 2
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82. Laporte V, Ait-Ghezala G, Volmar CH, Ganey C, Ganey N, Wood M, Mullan M: CD40 ligation mediates plaque-associated tau phosphorylation in beta-amyloid overproducing mice. Brain Res; 2008 Sep 22;1231:132-42
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  • [Title] CD40 ligation mediates plaque-associated tau phosphorylation in beta-amyloid overproducing mice.
  • Neuritic dystrophy with amyloid burden and neurofibrillary tangles are pathological hallmarks of Alzheimer's disease.
  • Genetic disruption of CD40 or CD40L alleviates amyloid burden, astrocytosis, and microgliosis in transgenic animal models of Alzheimer's disease.
  • It has been reported that phosphorylated tau-positive dystrophic neurites are observed in transgenic mice over-expressing human mutant beta-amyloid precursor protein (Tg2576).
  • Together, our data suggest that CD40-CD40L interaction has an effect on tau phosphorylation independent of beta-amyloid pathology, and that this effect may occur through a decrease of cdk5 and p35/p25.
  • [MeSH-major] Alzheimer Disease / metabolism. Antigens, CD40 / metabolism. Brain / metabolism. CD40 Ligand / metabolism. Plaque, Amyloid / metabolism. tau Proteins / metabolism
  • [MeSH-minor] Amyloid beta-Peptides / genetics. Amyloid beta-Peptides / metabolism. Amyloid beta-Protein Precursor / genetics. Amyloid beta-Protein Precursor / metabolism. Animals. Cell Line, Tumor. Coloring Agents. Congo Red. Cyclin-Dependent Kinase 5 / drug effects. Cyclin-Dependent Kinase 5 / metabolism. Disease Models, Animal. Down-Regulation / drug effects. Down-Regulation / physiology. Humans. Mice. Mice, Inbred C57BL. Mice, Knockout. Neurites / drug effects. Neurites / immunology. Neurites / metabolism. Neurofibrillary Tangles / genetics. Neurofibrillary Tangles / immunology. Neurofibrillary Tangles / metabolism. Phosphorylation / drug effects. Phosphotransferases / drug effects. Phosphotransferases / metabolism

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  • (PMID = 18606155.001).
  • [ISSN] 0006-8993
  • [Journal-full-title] Brain research
  • [ISO-abbreviation] Brain Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Antigens, CD40; 0 / Cdk5r1 protein, mouse; 0 / Coloring Agents; 0 / tau Proteins; 147205-72-9 / CD40 Ligand; 3U05FHG59S / Congo Red; EC 2.7.- / Phosphotransferases; EC 2.7.11.22 / Cdk5 protein, mouse; EC 2.7.11.22 / Cyclin-Dependent Kinase 5
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83. Gonzalez-Velasquez FJ, Kotarek JA, Moss MA: Soluble aggregates of the amyloid-beta protein selectively stimulate permeability in human brain microvascular endothelial monolayers. J Neurochem; 2008 Oct;107(2):466-77
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  • [Title] Soluble aggregates of the amyloid-beta protein selectively stimulate permeability in human brain microvascular endothelial monolayers.
  • Cerebral amyloid angiopathy associated with Alzheimer's disease is characterized by cerebrovascular deposition of the amyloid-beta protein (Abeta).
  • These results support previous findings demonstrating that small soluble Abeta(1-40) aggregates are also primarily responsible for endothelial activation, suggesting that these same species may elicit other changes in the cerebrovasculature associated with cerebral amyloid angiopathy and Alzheimer's disease.

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  • (PMID = 18702666.001).
  • [ISSN] 1471-4159
  • [Journal-full-title] Journal of neurochemistry
  • [ISO-abbreviation] J. Neurochem.
  • [Language] ENG
  • [Grant] United States / NCRR NIH HHS / RR / P20 RR016461; United States / NCRR NIH HHS / RR / P20 RR016461-07; United States / NCRR NIH HHS / RR / P20 RR-016461
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Membrane Proteins; 0 / Peptide Fragments; 0 / Phosphoproteins; 0 / TJP1 protein, human; 0 / Tumor Necrosis Factor-alpha; 0 / Zonula Occludens-1 Protein; 0 / amyloid beta-protein (1-40)
  • [Other-IDs] NLM/ NIHMS70504; NLM/ PMC4406342
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84. Ohyagi Y, Miyoshi K, Ma L, Motomura K, Kira J: [Inhibition of neuronal death by promoting degradation of intracellular amyloid beta-protein]. Nihon Shinkei Seishin Yakurigaku Zasshi; 2007 Apr;27(2):57-62
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  • [Title] [Inhibition of neuronal death by promoting degradation of intracellular amyloid beta-protein].
  • Inhibition of aggregation of amyloid p-protein (AP) and promotion of extracellular AM removal are known as potent therapeutic tools for Alzheimer's disease (AD).
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Apoptosis. Neurons / cytology
  • [MeSH-minor] Apomorphine / pharmacology. Humans. Proteasome Endopeptidase Complex / metabolism. Tumor Suppressor Protein p53 / metabolism

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  • (PMID = 17515111.001).
  • [ISSN] 1340-2544
  • [Journal-full-title] Nihon shinkei seishin yakurigaku zasshi = Japanese journal of psychopharmacology
  • [ISO-abbreviation] Nihon Shinkei Seishin Yakurigaku Zasshi
  • [Language] jpn
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] Japan
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Tumor Suppressor Protein p53; EC 3.4.25.1 / Proteasome Endopeptidase Complex; N21FAR7B4S / Apomorphine
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85. Nehar S, Mishra M, Heese K: Identification and characterisation of the novel amyloid-beta peptide-induced protein p17. FEBS Lett; 2009 Oct 6;583(19):3247-53
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  • [Title] Identification and characterisation of the novel amyloid-beta peptide-induced protein p17.
  • Amyloid-beta peptide (Abeta) achieves neurodegeneration through unknown mechanisms.
  • It impedes survival factors and enhances amyloid precursor protein expression thus suggesting its involvement in the Abeta-mediated pro-apoptotic pathways in AD.
  • [MeSH-major] Alzheimer Disease / metabolism. Alzheimer Disease / pathology. Amyloid beta-Peptides / metabolism. Apoptosis. Apoptosis Regulatory Proteins / metabolism. Peptide Fragments / metabolism
  • [MeSH-minor] Amino Acid Sequence. Animals. Cell Line, Tumor. Disease Models, Animal. Humans. Mice. Molecular Sequence Data. Rats. Tissue Distribution


86. Wang ZF, Li HL, Li XC, Zhang Q, Tian Q, Wang Q, Xu H, Wang JZ: Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture. J Neurochem; 2006 Aug;98(4):1167-75
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  • [Title] Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture.
  • Alzheimer's disease is characterized by beta-amyloid (Abeta) overproduction and tau hyperphosphorylation.
  • Here, we used mouse neuroblastoma N2a stably expressing wild-type amyloid precursor protein (APPwt) or the Swedish mutant APP (APPswe) to determine the alterations of phosphorylated tau and the related protein kinases.
  • We found that phosphorylation of tau at paired helical filament (PHF)-1, pSer396 and pThr231 epitopes was significantly increased in cells transfected with APPwt and APPswe, which produced higher levels of Abeta than cells transfected with vector or amyloid precursor-like protein 1.
  • [MeSH-major] Amyloid beta-Protein Precursor / biosynthesis. tau Proteins / metabolism
  • [MeSH-minor] Animals. Blotting, Western. Brain Neoplasms / metabolism. Cell Survival / physiology. Culture Media. Cyclin-Dependent Kinase 5 / metabolism. Enzyme Activation / physiology. Enzyme Inhibitors / pharmacology. Glycogen Synthase Kinase 3 / antagonists & inhibitors. Glycogen Synthase Kinase 3 / metabolism. Mice. Mutation / physiology. Neuroblastoma / metabolism. Phosphorylation. Protein Kinase C / antagonists & inhibitors. Protein Kinase C / metabolism. Transfection. Tumor Cells, Cultured

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  • (PMID = 16762022.001).
  • [ISSN] 0022-3042
  • [Journal-full-title] Journal of neurochemistry
  • [ISO-abbreviation] J. Neurochem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor; 0 / Culture Media; 0 / Enzyme Inhibitors; 0 / tau Proteins; EC 2.7.11.13 / Protein Kinase C; EC 2.7.11.22 / Cyclin-Dependent Kinase 5; EC 2.7.11.26 / Glycogen Synthase Kinase 3
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87. Même W, Calvo CF, Froger N, Ezan P, Amigou E, Koulakoff A, Giaume C: Proinflammatory cytokines released from microglia inhibit gap junctions in astrocytes: potentiation by beta-amyloid. FASEB J; 2006 Mar;20(3):494-6

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Proinflammatory cytokines released from microglia inhibit gap junctions in astrocytes: potentiation by beta-amyloid.
  • Interleukin-1beta (IL-1beta) and tumor necrosis factor-alpha (TNF-alpha) were identified as being the main factors responsible for this conditioned medium-mediated activity.
  • Interestingly, an inflammatory response characterized by MG activation and reactive astrocytes occurs in Alzheimer's disease, at sites of beta-amyloid (Abeta) deposits.
  • [MeSH-major] Amyloid beta-Peptides / pharmacology. Astrocytes / drug effects. Gap Junctions / drug effects. Interleukin-1 / pharmacology. Microglia / secretion. Peptide Fragments / pharmacology. Tumor Necrosis Factor-alpha / pharmacology

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  • (PMID = 16423877.001).
  • [ISSN] 1530-6860
  • [Journal-full-title] FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • [ISO-abbreviation] FASEB J.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Connexin 43; 0 / Culture Media, Conditioned; 0 / Il1rn protein, mouse; 0 / Interleukin 1 Receptor Antagonist Protein; 0 / Interleukin-1; 0 / Lipopolysaccharides; 0 / Peptide Fragments; 0 / Sialoglycoproteins; 0 / Tumor Necrosis Factor-alpha; 0 / amyloid beta-protein (25-35); 0 / amyloid beta-protein (35-25)
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88. Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, Wouters F, Hell SW, Simons M: Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci; 2008 Mar 12;28(11):2874-82
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  • [Title] Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons.
  • Endocytosis is required for the amyloidogenic processing of the amyloid precursor protein (APP) and thus to initiate the release of the neurotoxic beta-amyloid peptide (Abeta), the major component of extracellular plaques found in the brains of Alzheimer's disease patients.
  • [MeSH-major] Amyloid beta-Protein Precursor / metabolism. Endocytosis / physiology. Membrane Proteins / metabolism. Neurons / metabolism
  • [MeSH-minor] Amyloid beta-Peptides / genetics. Amyloid beta-Peptides / metabolism. Animals. Cell Line, Tumor. Cells, Cultured. Humans. Mice. Mice, Transgenic

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  • (PMID = 18337418.001).
  • [ISSN] 1529-2401
  • [Journal-full-title] The Journal of neuroscience : the official journal of the Society for Neuroscience
  • [ISO-abbreviation] J. Neurosci.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Amyloid beta-Protein Precursor; 0 / Membrane Proteins; 0 / flotillins
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89. Cecchi C, Pensalfini A, Liguri G, Baglioni S, Fiorillo C, Guadagna S, Zampagni M, Formigli L, Nosi D, Stefani M: Differentiation increases the resistance of neuronal cells to amyloid toxicity. Neurochem Res; 2008 Dec;33(12):2516-31
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  • [Title] Differentiation increases the resistance of neuronal cells to amyloid toxicity.
  • A substantial lack of information is recognized on the features underlying the variable susceptibility to amyloid aggregate toxicity of cells with different phenotypes.
  • In the present study we investigated whether differentiation affects cell susceptibility to amyloid injury using a human neurotypic SH-SY5Y cell differentiation model.
  • [MeSH-major] Amyloid / physiology. Cell Differentiation. Neurons / cytology
  • [MeSH-minor] Apoptosis. Calcium / metabolism. Calcium-Transporting ATPases / metabolism. Cell Line, Tumor. Cholesterol / metabolism. Humans. Membrane Lipids / metabolism. Microscopy, Confocal. Oxidation-Reduction. Reactive Oxygen Species / metabolism

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  • (PMID = 18307032.001).
  • [ISSN] 1573-6903
  • [Journal-full-title] Neurochemical research
  • [ISO-abbreviation] Neurochem. Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid; 0 / Membrane Lipids; 0 / Reactive Oxygen Species; 97C5T2UQ7J / Cholesterol; EC 3.6.3.8 / Calcium-Transporting ATPases; SY7Q814VUP / Calcium
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90. Xu S, Zhong M, Zhang L, Wang Y, Zhou Z, Hao Y, Zhang W, Yang X, Wei A, Pei L, Yu Z: Overexpression of Tfam protects mitochondria against beta-amyloid-induced oxidative damage in SH-SY5Y cells. FEBS J; 2009 Jul;276(14):3800-9
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  • [Title] Overexpression of Tfam protects mitochondria against beta-amyloid-induced oxidative damage in SH-SY5Y cells.
  • There is strong evidence that beta-amyloid (Abeta) causes oxidative stress and induces mitochondrial dysfunction in the pathogenesis of Alzheimer's disease.
  • To study the protective roles of Tfam against amyloid neurotoxicity, we established SH-SY5Y cell lines stably overexpressing Tfam and exposed them to 10 microm Abeta1-42 for 24 h.
  • [MeSH-major] Amyloid beta-Peptides / metabolism. DNA, Mitochondrial / genetics. DNA-Binding Proteins / metabolism. Mitochondria / genetics. Mitochondrial Proteins / metabolism. Oxidative Stress. Peptide Fragments / metabolism. Transcription Factors / metabolism
  • [MeSH-minor] Adenosine Triphosphate / metabolism. Cell Line, Tumor. Cell Survival / drug effects. DNA Damage. Electron Transport Complex IV / metabolism. Gene Dosage. Humans

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  • (PMID = 19496804.001).
  • [ISSN] 1742-4658
  • [Journal-full-title] The FEBS journal
  • [ISO-abbreviation] FEBS J.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / DNA, Mitochondrial; 0 / DNA-Binding Proteins; 0 / Mitochondrial Proteins; 0 / Peptide Fragments; 0 / TFAM protein, human; 0 / Transcription Factors; 0 / amyloid beta-protein (1-42); 8L70Q75FXE / Adenosine Triphosphate; EC 1.9.3.1 / Electron Transport Complex IV
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91. Takata K, Kitamura Y, Yanagisawa D, Morikawa S, Morita M, Inubushi T, Tsuchiya D, Chishiro S, Saeki M, Taniguchi T, Shimohama S, Tooyama I: Microglial transplantation increases amyloid-beta clearance in Alzheimer model rats. FEBS Lett; 2007 Feb 6;581(3):475-8
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  • [Title] Microglial transplantation increases amyloid-beta clearance in Alzheimer model rats.
  • Immunization with amyloid-beta (Abeta) peptides, a therapeutic approach in Alzheimer's disease (AD), reduces brain Abeta, and microglial Abeta phagocytosis has been proposed as an Abeta-lowering mechanism.
  • [MeSH-major] Alzheimer Disease / metabolism. Alzheimer Disease / surgery. Amyloid beta-Peptides / metabolism. Microglia / transplantation
  • [MeSH-minor] Animals. Brain Tissue Transplantation. Cell Movement. Disease Models, Animal. Hippocampus / metabolism. Hippocampus / pathology. Humans. Magnetic Resonance Imaging. Male. Phagocytosis. Rats. Rats, Wistar. Tumor Necrosis Factor-alpha / metabolism

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  • (PMID = 17240371.001).
  • [ISSN] 0014-5793
  • [Journal-full-title] FEBS letters
  • [ISO-abbreviation] FEBS Lett.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Tumor Necrosis Factor-alpha
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92. Meloni G, Sonois V, Delaine T, Guilloreau L, Gillet A, Teissié J, Faller P, Vasák M: Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity. Nat Chem Biol; 2008 Jun;4(6):366-72
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity.
  • Aberrant interactions of copper and zinc ions with the amyloid-beta peptide (Abeta) potentiate Alzheimer's disease (AD) by participating in the aggregation process of Abeta and in the generation of reactive oxygen species (ROS).
  • [MeSH-major] Amyloid beta-Peptides / antagonists & inhibitors. Amyloid beta-Peptides / toxicity. Copper / toxicity. Metallothionein / pharmacology. Organometallic Compounds / antagonists & inhibitors. Organometallic Compounds / toxicity. Peptide Fragments / antagonists & inhibitors. Peptide Fragments / toxicity
  • [MeSH-minor] Cell Survival / drug effects. Circular Dichroism. Humans. Neurons / cytology. Neurons / drug effects. Reactive Oxygen Species / antagonists & inhibitors. Reactive Oxygen Species / metabolism. Solubility. Tumor Cells, Cultured. Zinc / chemistry

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  • (PMID = 18454142.001).
  • [ISSN] 1552-4469
  • [Journal-full-title] Nature chemical biology
  • [ISO-abbreviation] Nat. Chem. Biol.
  • [Language] eng
  • [Databank-accession-numbers] PubChem-Substance/ 49684275/ 49684276/ 49684277/ 49684278/ 49684279/ 49684280/ 49684281/ 49684282/ 49684283
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Organometallic Compounds; 0 / Peptide Fragments; 0 / Reactive Oxygen Species; 0 / amyloid beta-protein (1-40); 789U1901C5 / Copper; 9038-94-2 / Metallothionein; J41CSQ7QDS / Zinc
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93. Zheng L, Roberg K, Jerhammar F, Marcusson J, Terman A: Oxidative stress induces intralysosomal accumulation of Alzheimer amyloid beta-protein in cultured neuroblastoma cells. Ann N Y Acad Sci; 2006 May;1067:248-51
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Oxidative stress induces intralysosomal accumulation of Alzheimer amyloid beta-protein in cultured neuroblastoma cells.
  • Oxidative stress is considered important for the pathogenesis of Alzheimer's disease (AD), which is characterized by the formation of extracellular senile plaques, mainly composed of amyloid beta-protein (Abeta).
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Lysosomes / metabolism. Neuroblastoma / metabolism. Oxidative Stress
  • [MeSH-minor] Cell Culture Techniques. Cell Line, Tumor. Humans. Lysosomal-Associated Membrane Protein 2. Lysosome-Associated Membrane Glycoproteins / metabolism. Lysosome-Associated Membrane Glycoproteins / ultrastructure. Tumor Cells, Cultured

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  • (PMID = 16803994.001).
  • [ISSN] 0077-8923
  • [Journal-full-title] Annals of the New York Academy of Sciences
  • [ISO-abbreviation] Ann. N. Y. Acad. Sci.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / LAMP2 protein, human; 0 / Lysosomal-Associated Membrane Protein 2; 0 / Lysosome-Associated Membrane Glycoproteins
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94. Gevorkian G, Gonzalez-Noriega A, Acero G, Ordoñez J, Michalak C, Munguia ME, Govezensky T, Cribbs DH, Manoutcharian K: Amyloid-beta peptide binds to microtubule-associated protein 1B (MAP1B). Neurochem Int; 2008 May;52(6):1030-6
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Amyloid-beta peptide binds to microtubule-associated protein 1B (MAP1B).
  • Extracellular and intraneuronal formation of amyloid-beta aggregates have been demonstrated to be involved in the pathogenesis of Alzheimer's disease.
  • However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood.
  • Previous studies suggest that binding of amyloid-beta to a number of targets have deleterious effects on cellular functions.
  • In the present study we have shown for the first time that amyloid-beta 1-42 bound to a peptide comprising the microtubule binding domain of the heavy chain of microtubule-associated protein 1B by the screening of a human brain cDNA library expressed on M13 phage.

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  • (PMID = 18079022.001).
  • [ISSN] 0197-0186
  • [Journal-full-title] Neurochemistry international
  • [ISO-abbreviation] Neurochem. Int.
  • [Language] ENG
  • [Grant] United States / NINDS NIH HHS / NS / NS-050895; United States / NIA NIH HHS / AG / R21 AG023534; United States / NIA NIH HHS / AG / AG023534-02; United States / NIA NIH HHS / AG / AG 023534; United States / NINDS NIH HHS / NS / R01 NS050895; United States / NIA NIH HHS / AG / R21 AG023534-01; United States / NIA NIH HHS / AG / R01 AG020241; United States / NIA NIH HHS / AG / AG-20241; United States / NIA NIH HHS / AG / AG023534-01; United States / NIA NIH HHS / AG / R21 AG023534-02
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / MAP1B protein, human; 0 / Microtubule-Associated Proteins; 0 / Peptide Fragments; 0 / Peptides; 0 / amyloid beta-protein (1-42)
  • [Other-IDs] NLM/ NIHMS46961; NLM/ PMC2390996
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95. Tanahashi H, Yoshioka K: RNA interference silencing of DRAL affects processing of amyloid precursor protein. Neurosci Lett; 2008 Jul 18;439(3):293-7

  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] RNA interference silencing of DRAL affects processing of amyloid precursor protein.
  • In this study, we investigated whether DRAL modifies the metabolism of the amyloid precursor protein (APP).
  • We found that the knockdown was accompanied by a decrease in the amount of secreted alpha-secretase-cleaved APP and the membrane-bound C-terminal fragment C83 and an increase in the amount of secreted beta-amyloid peptide (Abeta) from the cells.
  • [MeSH-major] Amyloid beta-Protein Precursor / metabolism. Homeodomain Proteins / metabolism. Muscle Proteins / metabolism. Transcription Factors / metabolism
  • [MeSH-minor] ADAM Proteins / metabolism. Amyloid Precursor Protein Secretases / metabolism. Animals. Cell Line, Transformed. Cercopithecus aethiops. Cricetinae. Humans. LIM-Homeodomain Proteins. Membrane Proteins / metabolism. Phorbol Esters / pharmacology. Prostanoic Acids / metabolism. RNA, Small Interfering / metabolism. Transfection

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  • (PMID = 18534756.001).
  • [ISSN] 0304-3940
  • [Journal-full-title] Neuroscience letters
  • [ISO-abbreviation] Neurosci. Lett.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Ireland
  • [Chemical-registry-number] 0 / Amyloid beta-Protein Precursor; 0 / FHL2 protein, human; 0 / Homeodomain Proteins; 0 / LIM-Homeodomain Proteins; 0 / Membrane Proteins; 0 / Muscle Proteins; 0 / Phorbol Esters; 0 / Prostanoic Acids; 0 / RNA, Small Interfering; 0 / Transcription Factors; 20839-06-9 / phorbol-12-myristate; EC 3.4.- / Amyloid Precursor Protein Secretases; EC 3.4.24.- / ADAM Proteins; EC 3.4.24.- / tumor necrosis factor-alpha convertase; EC 3.4.24.81 / ADAM10 protein, human; W4459A2P0J / rosaprostol
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96. Laws SM, Perneczky R, Wagenpfeil S, Müller U, Förstl H, Martins RN, Kurz A, Riemenschneider M: TNF polymorphisms in Alzheimer disease and functional implications on CSF beta-amyloid levels. Hum Mutat; 2005 Jul;26(1):29-35
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  • [Title] TNF polymorphisms in Alzheimer disease and functional implications on CSF beta-amyloid levels.
  • Recently a polymorphism in the proinflammatory cytokine tumor necrosis factor (TNF), in association with apolipoprotein E (APOE), was reported to increase AD risk.
  • In a subset of 90 individuals we also investigated whether these SNPs exerted any functional effects on cerebrospinal fluid (CSF) beta-amyloid (Abeta) levels.
  • [MeSH-major] Alzheimer Disease / cerebrospinal fluid. Alzheimer Disease / genetics. Amyloid beta-Peptides / cerebrospinal fluid. Polymorphism, Single Nucleotide / genetics. Tumor Necrosis Factor-alpha / genetics


97. Costantini C, Della-Bianca V, Formaggio E, Chiamulera C, Montresor A, Rossi F: The expression of p75 neurotrophin receptor protects against the neurotoxicity of soluble oligomers of beta-amyloid. Exp Cell Res; 2005 Nov 15;311(1):126-34
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  • [Title] The expression of p75 neurotrophin receptor protects against the neurotoxicity of soluble oligomers of beta-amyloid.
  • In this paper, evidence is provided that p75 neurotrophin receptor (p75NTR) exerts an opposite role on the cytotoxic function of beta-amyloid (Abeta) depending on the different state of the peptide, fibrillar or oligomeric soluble form.
  • Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines. J. Exp. Med.
  • [MeSH-major] Amyloid beta-Peptides / toxicity. Neuroblastoma / drug therapy. Peptide Fragments / toxicity. Receptor, Nerve Growth Factor / metabolism
  • [MeSH-minor] Caspases / metabolism. Cell Death / drug effects. Cell Proliferation / drug effects. Cytoprotection. Dimerization. Humans. Mutation. Phosphatidylinositol 3-Kinases / metabolism. Tumor Cells, Cultured

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  • (PMID = 16223482.001).
  • [ISSN] 0014-4827
  • [Journal-full-title] Experimental cell research
  • [ISO-abbreviation] Exp. Cell Res.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Peptide Fragments; 0 / Receptor, Nerve Growth Factor; 0 / amyloid beta-protein (1-42); EC 2.7.1.- / Phosphatidylinositol 3-Kinases; EC 3.4.22.- / Caspases
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98. Guix FX, Ill-Raga G, Bravo R, Nakaya T, de Fabritiis G, Coma M, Miscione GP, Villà-Freixa J, Suzuki T, Fernàndez-Busquets X, Valverde MA, de Strooper B, Muñoz FJ: Amyloid-dependent triosephosphate isomerase nitrotyrosination induces glycation and tau fibrillation. Brain; 2009 May;132(Pt 5):1335-45
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  • [Title] Amyloid-dependent triosephosphate isomerase nitrotyrosination induces glycation and tau fibrillation.
  • Alzheimer's disease neuropathology is characterized by neuronal death, amyloid beta-peptide deposits and neurofibrillary tangles composed of paired helical filaments of tau protein.
  • Although crucial for our understanding of the pathogenesis of Alzheimer's disease, the molecular mechanisms linking amyloid beta-peptide and paired helical filaments remain unknown.
  • Here, we show that amyloid beta-peptide-induced nitro-oxidative damage promotes the nitrotyrosination of the glycolytic enzyme triosephosphate isomerase in human neuroblastoma cells.
  • Consequently, nitro-triosephosphate isomerase was found to be present in brain slides from double transgenic mice overexpressing human amyloid precursor protein and presenilin 1, and in Alzheimer's disease patients.
  • This finding correlates with the widespread glycation immunostaining in Alzheimer's disease cortex and hippocampus from double transgenic mice overexpressing amyloid precursor protein and presenilin 1.
  • Our results link oxidative stress, the main etiopathogenic mechanism in sporadic Alzheimer's disease, via the production of peroxynitrite and nitrotyrosination of triosephosphate isomerase, to amyloid beta-peptide-induced toxicity and tau pathology.
  • [MeSH-major] Alzheimer Disease / metabolism. Amyloid beta-Peptides / metabolism. Frontal Lobe / metabolism. Models, Molecular. Triose-Phosphate Isomerase / metabolism. Tyrosine / analogs & derivatives
  • [MeSH-minor] Animals. Blotting, Western. Case-Control Studies. Cell Line. Cell Line, Tumor. Humans. Immunohistochemistry. Mice. Mice, Transgenic. Microscopy, Atomic Force. Microscopy, Confocal. Microscopy, Electron. Neuroblastoma. Neurofibrillary Tangles / metabolism. Oxidative Stress. Peroxynitrous Acid / analysis. Peroxynitrous Acid / metabolism. Phosphorylation. tau Proteins / analysis. tau Proteins / metabolism

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  • (PMID = 19251756.001).
  • [ISSN] 1460-2156
  • [Journal-full-title] Brain : a journal of neurology
  • [ISO-abbreviation] Brain
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / tau Proteins; 14691-52-2 / Peroxynitrous Acid; 3604-79-3 / 3-nitrotyrosine; 42HK56048U / Tyrosine; EC 5.3.1.1 / Triose-Phosphate Isomerase
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99. Berson A, Knobloch M, Hanan M, Diamant S, Sharoni M, Schuppli D, Geyer BC, Ravid R, Mor TS, Nitsch RM, Soreq H: Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology. Brain; 2008 Jan;131(Pt 1):109-19
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  • [Title] Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology.
  • Alzheimer's disease has long been known to involve cholinergic deficits, but the linkage between cholinergic gene expression and the Alzheimer's disease amyloid pathology has remained incompletely understood.
  • One known link involves synaptic acetylcholinesterase (AChE-S), shown to accelerate amyloid fibrils formation.
  • Here, we report that the 'Readthrough' AChE-R splice variant, which differs from AChE-S in its 26 C-terminal residues, inversely exerts neuroprotective effects from amyloid beta (Abeta) induced toxicity.
  • [MeSH-major] Acetylcholinesterase / pharmacology. Alzheimer Disease / metabolism. Amyloid beta-Peptides / biosynthesis
  • [MeSH-minor] Adult. Aged. Aged, 80 and over. Alternative Splicing. Animals. Astrocytes / pathology. Brain / metabolism. Brain / pathology. Dendrites / pathology. Dose-Response Relationship, Drug. Female. Gene Expression Regulation, Enzymologic. Hippocampus / enzymology. Humans. Male. Mice. Mice, Transgenic. Middle Aged. RNA, Messenger / genetics. Recombinant Proteins / pharmacology. Tumor Cells, Cultured

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  • (PMID = 18056160.001).
  • [ISSN] 1460-2156
  • [Journal-full-title] Brain : a journal of neurology
  • [ISO-abbreviation] Brain
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / RNA, Messenger; 0 / Recombinant Proteins; EC 3.1.1.7 / Acetylcholinesterase
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100. Grillo-Bosch D, Carulla N, Cruz M, Sánchez L, Pujol-Pina R, Madurga S, Rabanal F, Giralt E: Retro-enantio N-methylated peptides as beta-amyloid aggregation inhibitors. ChemMedChem; 2009 Sep;4(9):1488-94
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  • [Title] Retro-enantio N-methylated peptides as beta-amyloid aggregation inhibitors.
  • An emerging and attractive target for the treatment of Alzheimer's disease is to inhibit the aggregation of beta-amyloid protein (Abeta).
  • [MeSH-major] Amyloid beta-Peptides / antagonists & inhibitors. Neuroprotective Agents / chemistry. Oligopeptides / chemistry. Peptide Fragments / antagonists & inhibitors. Peptides / chemistry
  • [MeSH-minor] Alzheimer Disease / drug therapy. Amino Acid Sequence. Cell Line, Tumor. Drug Design. Humans. Stereoisomerism

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  • (PMID = 19591190.001).
  • [ISSN] 1860-7187
  • [Journal-full-title] ChemMedChem
  • [ISO-abbreviation] ChemMedChem
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Amyloid beta-Peptides; 0 / Neuroprotective Agents; 0 / Oligopeptides; 0 / Peptide Fragments; 0 / Peptides; 0 / amyloid beta-protein (1-42); 0 / inD peptide; 0 / inL peptide; 0 / inrD peptide
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