| Overexpression of alpha(v)beta6 integrin in serous epithelial ovarian cancer regulates extracellular matrix degradation via the plasminogen activation cascade. | |
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MedLine Citation:
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PMID: 11872628 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Recent evidence suggests that integrins are involved in the multi-step process of tumour metastasis. The biological relevance of alpha(v) integrins and associated beta-subunits in ovarian cancer metastasis was examined by analysing the expression of these cell surface receptors in nine ovarian cancer cell lines and also in the primary human ovarian surface epithelial cell line (HOSE). beta1, beta3 and beta5 subunits were present in all ten ovarian cell lines. beta6 subunit was present at varying levels in eight out of nine cancer cell lines but was absent in the HOSE cell line. Immunohistochemical staining showed that beta6 was present in both non-invasive (borderline) and high-grade ovarian cancer tissues but was absent in benign and normal ovarian tissue. High alpha(v)beta6 integrin expressing ovarian cancer cell lines had high cell surface expression of uPA and uPAR. Ovarian cancer cell lines expressing high to moderate level of alpha(v)beta6 integrin demonstrated ligand-independent enhanced levels of high molecular weight (HMW)-uPA and pro-matrix metalloproteinase 2 and 9 (pro-MMP-2 and pro-MMP-9) expression in the tumour-conditioned medium. High and moderate expression of alpha(v)beta6 integrin correlated with increased plasminogen-dependent degradation of extracellular matrix which could be inhibited by inhibitors of plasmin, uPA and MMPs or by monoclonal antibody against uPA, MMP-9 or alpha(v)beta6 integrin. These results suggest that endogenous de novo expression of alpha(v)beta6 integrin in ovarian cancer cells may contribute to their invasive potential, and that alpha(v)beta6 expression may play a role in ovarian cancer progression and metastasis. |
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Authors:
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N Ahmed; F Pansino; Riley Clyde; P Murthi; M A Quinn; G E Rice; M V Agrez; S Mok; M S Baker |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Carcinogenesis Volume: 23 ISSN: 0143-3334 ISO Abbreviation: Carcinogenesis Publication Date: 2002 Feb |
Date Detail:
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Created Date: 2002-03-01 Completed Date: 2002-04-04 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8008055 Medline TA: Carcinogenesis Country: England |
Other Details:
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Languages: eng Pagination: 237-44 Citation Subset: IM |
Affiliation:
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Gynaecological Cancer Research Centre, Royal Women's Hospital, Melbourne, Australia. nuzhata@unimelb.edu.au |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Antigens, Neoplasm* Blotting, Western Cell Separation Collagenases / biosynthesis Culture Media, Conditioned / pharmacology Enzyme Precursors / biosynthesis Extracellular Matrix / metabolism* Female Flow Cytometry Gelatinases / biosynthesis Humans Immunoglobulin G / metabolism Immunohistochemistry Integrins / biosynthesis* Ligands Matrix Metalloproteinase 9 Metalloendopeptidases / biosynthesis Neoplasm Invasiveness Neoplasm Metastasis Neoplasms, Glandular and Epithelial / metabolism* Ovarian Neoplasms / metabolism* Plasminogen / metabolism* Plasminogen Activators / metabolism* Protein Structure, Tertiary Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Antigens, Neoplasm; 0/Culture Media, Conditioned; 0/Enzyme Precursors; 0/Immunoglobulin G; 0/Integrins; 0/Ligands; 0/integrin alphavbeta6; 9001-91-6/Plasminogen; EC 3.4.21.-/Plasminogen Activators; EC 3.4.24.-/Collagenases; EC 3.4.24.-/Gelatinases; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.-/pro-matrix metalloproteinase 9; EC 3.4.24.-/progelatinase; EC 3.4.24.35/Matrix Metalloproteinase 9 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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