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- W996786548 abstract "This chapter focuses on the structure and functions of matrix metalloproteinase-2 (MMP2) or gelatinase A that is active in cleaving denatured collagens, native type V collagen, elastin, and other matrix proteins and also carries out specific cleavages of native type IV collagen chains. The major role of gelatinase A appears to be in basement membrane turnover. This activity means that gelatinase A plays a key role in metastasis and tumor invasion. Analysis of the primary structure of gelatinase A shows that it is a modular molecule containing a prodomain, catalytic domain, collagen-like hinge, and hemopexin-like domain. Gelatinase A can be activated by membrane-type I MMP and probably involves the formation of a complex among MT1-MMP, tissue inhibitor of metalloproteinase-2 (TIMP2), and progelatinase A by MT2-MMP. The chapter discusses the gene structure and isolation of MMP2." @default.
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- W996786548 date "1998-01-01" @default.
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- W996786548 title "MMP2 gelatinase A, 72 kDa type IV collagenase, 72kDa gelatinase, TBE-1, CLG4A" @default.
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- W996786548 doi "https://doi.org/10.1016/b978-012068911-8.50150-0" @default.
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