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1. Seethala RR, LiVolsi VA, Zhang PJ, Pasha TL, Baloch ZW: Comparison of p63 and p73 expression in benign and malignant salivary gland lesions. Head Neck; 2005 Aug;27(8):696-702
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Comparison of p63 and p73 expression in benign and malignant salivary gland lesions.
  • In this study, we examined the expression of p63 and p73 in 50 various benign salivary gland lesions and 45 malignant salivary gland tumors.
  • METHODS: The 95 salivary gland tumors were selected from the archives of the Department of Pathology and Laboratory Medicine at the Hospital of the University of Pennsylvania.
  • RESULTS: In benign lesions, p63 and p73 nuclear reactivity was seen in 46 (92%) of 50 and 47 (94%) of 50 cases, respectively.
  • CONCLUSIONS: Hence, p63 and p73 expression is retained in both benign and malignant salivary gland tumors with basaloid or myoepithelial differentiation.
  • [MeSH-major] DNA-Binding Proteins / biosynthesis. Myoepithelioma / pathology. Nuclear Proteins / biosynthesis. Phosphoproteins / biosynthesis. Salivary Gland Neoplasms / pathology. Trans-Activators / biosynthesis
  • [MeSH-minor] Biomarkers, Tumor. Gene Expression Regulation, Neoplastic. Genes, Tumor Suppressor. Humans. Immunohistochemistry. Transcription Factors. Tumor Suppressor Proteins

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  • [Copyright] Copyright 2005 Wiley Periodicals, Inc.
  • (PMID = 16021638.001).
  • [ISSN] 1043-3074
  • [Journal-full-title] Head & neck
  • [ISO-abbreviation] Head Neck
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Biomarkers, Tumor; 0 / DNA-Binding Proteins; 0 / Nuclear Proteins; 0 / Phosphoproteins; 0 / TP63 protein, human; 0 / Trans-Activators; 0 / Transcription Factors; 0 / Tumor Suppressor Proteins; 0 / tumor suppressor protein p73
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2. Gama-de-Souza LN, Cyreno-Oliveira E, Freitas VM, Melo ES, Vilas-Boas VF, Moriscot AS, Jaeger RG: Adhesion and protease activity in cell lines from human salivary gland tumors are regulated by the laminin-derived peptide AG73, syndecan-1 and beta1 integrin. Matrix Biol; 2008 Jun;27(5):402-19
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  • We studied the induction of protease activity by the laminin alpha1-derived peptide AG73 in cells from adenoid cystic carcinoma (CAC2) and myoepithelioma (M1), respectively a malignant and a benign salivary gland tumors.
  • Laminin alpha1 chain and MMP9 were immunolocalized in adenoid cystic carcinoma and myoepithelioma in vivo and in vitro.
  • [MeSH-minor] Blotting, Western. Calcium / metabolism. Carcinoma, Adenoid Cystic / genetics. Carcinoma, Adenoid Cystic / metabolism. Carcinoma, Adenoid Cystic / pathology. Cell Adhesion / drug effects. Cell Line, Tumor. Chelating Agents / pharmacology. Dipeptides / pharmacology. Extracellular Matrix / drug effects. Extracellular Matrix / metabolism. Heparin / pharmacology. Humans. Immunohistochemistry. Matrix Metalloproteinase 2 / genetics. Matrix Metalloproteinase 2 / metabolism. Matrix Metalloproteinase 9 / genetics. Matrix Metalloproteinase 9 / metabolism. Matrix Metalloproteinase Inhibitors. Myoepithelioma / genetics. Myoepithelioma / metabolism. Myoepithelioma / pathology. RNA, Small Interfering / genetics. Reverse Transcriptase Polymerase Chain Reaction. Signal Transduction / physiology

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  • (PMID = 18378436.001).
  • [ISSN] 0945-053X
  • [Journal-full-title] Matrix biology : journal of the International Society for Matrix Biology
  • [ISO-abbreviation] Matrix Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / AG 73; 0 / Antigens, CD29; 0 / Chelating Agents; 0 / Dipeptides; 0 / Laminin; 0 / Matrix Metalloproteinase Inhibitors; 0 / N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide; 0 / Peptide Fragments; 0 / RNA, Small Interfering; 0 / SDC1 protein, human; 0 / Syndecan-1; 151186-83-3 / laminin A; 9005-49-6 / Heparin; EC 3.4.24.- / Matrix Metalloproteinases; EC 3.4.24.24 / MMP2 protein, human; EC 3.4.24.24 / Matrix Metalloproteinase 2; EC 3.4.24.35 / Matrix Metalloproteinase 9; SY7Q814VUP / Calcium
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3. Vuhahula EA: Salivary gland tumors in Uganda: clinical pathological study. Afr Health Sci; 2004 Apr;4(1):15-23
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • SETTING: Makerere University, Faculty of Medicine, Department of Pathology.
  • METHODS: All epithelial tumors from major and minor salivary glands accessioned from 1979 to 1988 were analyzed in respect to sex and age of patients, anatomical location of the tumor and histological type.
  • There were a total of 125 (46.6%) malignant tumors and 143 (53.4%) benign tumors.
  • The mean age of patients with malignant lesions (43.1 years; SD=16.75; median=44.00 years) was 9.6 years older than those with benign tumors (mean=33.5 years; SD=16.0; median=30.00 years).
  • Pleomorphic adenoma was the most common benign tumor (74.8%), followed by myoepithelioma (9.8%).
  • i) females are more affected than males, ii) there is a low proportion of tumors from the parotid gland and high proportion of tumors from the submandibular and minor salivary glands, iii) the parotid and minor salivary gland tumors have more probability of being malignant than those tumors from the submandibular gland iv) the newly categorized pathological entities are common and v) Whartin's tumor is extremely rare in black African population.

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  • (PMID = 15126188.001).
  • [ISSN] 1729-0503
  • [Journal-full-title] African health sciences
  • [ISO-abbreviation] Afr Health Sci
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Uganda
  • [Other-IDs] NLM/ PMC2141656
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