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- W4250129386 abstract "Unstimulated human fibrosarcoma cells (HT1080) constitutively secrete matrix metalloproteinase 2 (MMP 2) as a proenzyme requiring proteolytic cleavage by membrane type-1 MMP (MT1 MMP) for activation. Physiological and pharmacological stimuli induce clustering of MT1 MMP/tissue inhibitor of MMP 2 “receptors”, promoting binding and activation of MMP 2. We now report that cholesterol depleted HT1080 cells accumulated MT1 MMP on the cell surface and activated MMP 2. A specific inhibitor of mitogen activated protein kinase kinase 1/2 inhibited both MMP 2 activation and extracellular signal-related kinase phosphorylation induced by cholesterol depletion. Our data indicate that the cholesterol content of unstimulated cells is critical for secretion of MMP 2 as an inactive zymogen and control of pericellular proteolysis." @default.
- W4250129386 created "2022-05-12" @default.
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- W4250129386 date "2004-05-01" @default.
- W4250129386 modified "2023-09-26" @default.
- W4250129386 title "Cellular cholesterol regulates MT1 MMP dependent activation of MMP 2 via MEK-1 in HT1080 fibrosarcoma cells" @default.
- W4250129386 doi "https://doi.org/10.1016/s0014-5793(04)00443-0" @default.
- W4250129386 hasPublicationYear "2004" @default.
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