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• W1747578412 abstract "Publisher Summary This chapter describes the Ras regulation of urokinase-type plasminogen activator. Degradation of the extracellular matrix (ECM) is essential in many physiological and pathological processes, including involution of the prostate, cytotrophoblast implantation; wound healing, and tumor cell invasion, all of which require extensive extracellular matrix proteolysis. Many different types of ECM-degrading enzymes are implicated in these processes, including matrix metalloproteinases, cysteine proteases (cathepsins B, L, and H), caspases, aspartyl proteases (cathepsin D), and serine proteases. Together, these proteolytic functions facilitate the migration of tumor cells through the extracellular matrix and basement membrane barriers. High urokinase expression is correlated with a poor prognosis for patients suffering from a variety of different types of cancer including breast, ovary, lung, and gastrointestinal cancer. In short, constitutively active Ras has is shown to induce the expression of urokinase, urokinase receptor, and other invasion-related genes. Considering the synthesis of farnesyltransferase inhibitors that counter Ras activity, it is attractive to speculate that Ras inhibition could be an effective adjuvant strategy for preventing invasion and metastasis of tumors characterized by molecular aberrations involving the Ras pathway." @default.
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• W1747578412 date "2001-01-01" @default.
• W1747578412 modified "2023-09-23" @default.
• W1747578412 title "Ras Regulation of urokinase-type plasminogen activator" @default.
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• W1747578412 doi "https://doi.org/10.1016/s0076-6879(01)33049-5" @default.
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