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• W2068561314 abstract "Matrix metalloproteinases (MMPs) and integrins have been implicated in a variety of processes involved in tumor progression. To evaluate the individual roles of integrin αvβ3 and membrane-type 1 matrix metalloproteinase (MT1-MMP), as well as the effects of their joint expression on tumor cell functions, MCF7 breast carcinoma cells were transfected stably with either the MT1-MMP, the β3 integrin subunit or both MT1-MMP and β3 cDNAs. MT1-MMP expression is accompanied by the functional activation of integrin αvβ3, thereby increasing vitronectin-mediated adhesion and migration of MCF7 cells transfected with MT1-MMP and integrin αvβ3. MT1-MMP-dependent functional activation of αvβ3 correlates with modification(s) of the β3 subunit, including its higher electrophoretic mobility and affected the LM609-binding site. MCF7 cells jointly expressing MT1-MMP and αvβ3 were the most efficient in adhesion to the recombinant C-terminal domain of MMP-2 as well as in generating soluble and cell surface associated mature MMP-2 enzyme. These findings suggest a mechanism of selective docking of MMP-2 at tumor cell surfaces, specifically at the sites that include MT1-MMP and activated integrin αvβ3. These mechanisms may provide a link between spatial regulation of focal proteolysis by the cell surface associated MMPs and the regulation of integrin-mediated motility of tumor cells. Int. J. Cancer 86:15–23, 2000. © 2000 Wiley-Liss, Inc." @default.
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• W2068561314 date "2000-04-01" @default.
• W2068561314 modified "2023-10-17" @default.
• W2068561314 title "Functional activation of integrin ?v?3 in tumor cells expressing membrane-type 1 matrix metalloproteinase" @default.
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• W2068561314 doi "https://doi.org/10.1002/(sici)1097-0215(20000401)86:1<15::aid-ijc3>3.0.co;2-b" @default.
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