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背景
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Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-10 (stromelysin 2) degrades a broad range of substrates including gelatin, collagen types?III, IV and V, fibronectin, aggrecan, and pig cartilage proteoglycan. MMP-10 can activate other MMPs such as MMP-1 and MMP-8. MMP-10 is expressed in keratinocytes, T?cells, menstrual endometrium, and a few tumor samples. Structurally, MMP-10 may be divided into four distinct domains: a pro-domain which is cleaved upon activation, a catalytic domain containing the zinc binding site; a short linker region, and a carboxyl terminal hemopexin-like domain.
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