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• W1978467605 abstract "The integrins are a family of cell surface receptors which mediate cellular adhesion and signalling events. Our goal was to evaluate integrin function and signalling pathways in ovarian cancer cells. Ovarian cancer cell lines, NIH:OVCAR-3 and NIH:OVCAR-5, exhibited distinct extracellular matrix (ECM) binding preferences which were mediated primarily through β1 integrin interactions. Western blot analysis was used to identify changes in cellular phosphotyrosine, focal adhesion kinase (FAK) and mitogen activated protein (MAP) kinase. Tyrosine phosphorylation of integrin-associated phosphoproteins was not enhanced in either cell type in response to adhesion onto ECM components or receptor crosslinking. FAK expression was greater in NIH:OVCAR-5 cells while MAP kinase activity was higher in NIH:OVCAR-3 cells. The data suggest that these two ovarian cancer cell lines exhibit specific ECM binding preferences and distinct differences in phosphotyrosine, focal adhesion and MAP kinase expression profiles." @default.
• W1978467605 created "2016-06-24" @default.
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• W1978467605 date "1998-01-01" @default.
• W1978467605 modified "2023-10-14" @default.
• W1978467605 title "Integrin-Mediated Adhesion and Signalling in Ovarian Cancer Cells" @default.
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• W1978467605 doi "https://doi.org/10.1016/s0898-6568(97)00074-0" @default.
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