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- W120624935 abstract "Proteases of the serine, cysteine, aspartic, and metallo classes are capable of degrading extracellular matrix and basement membrane components thus contributing to the invasive and metastatic properties of tumor cells. The localization of proteases to tumor cell surfaces may be important for their ability to invade and may also be a way to regulate protease expression and activity. Proteases found to be associated with the tumor cell surface and which are also correlated with tumor invasion and metastasis include: urokinase plasminogen activator, cathep-sin B, and matrix metalloproteinase-2. Cell surface receptors have been identified for urokinase plasminogen activator and matrix metalloproteinase-2. Although regulation of protease expression and activity can occur at several levels, the interaction of proteases with cell surface receptors may be most crucial to protease function. Increased expression of proteases, cell surface receptors, and endogenous inhibitors have been observed in many cancers." @default.
- W120624935 created "2016-06-24" @default.
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- W120624935 date "1999-01-01" @default.
- W120624935 modified "2023-09-26" @default.
- W120624935 title "Cell-surface proteases in cancer" @default.
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- W120624935 doi "https://doi.org/10.1007/978-3-0348-8737-3_8" @default.
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