Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene.[5] The enzyme (EC 3.4.24.23) has also been known as matrin, putative (or punctuated) metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP).[6][7][8][9] Human MMP-7 has a molecular weight around 30 kDa.[10]
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Matrilysin was discovered by Sellers and Woessner in the uterus of the rat in 1988.[11] The complementary DNA (cDNA) of human MMP7 was isolated in 1988 by Muller et al.[12] MMP7 is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. The primary role of cleaved/activated MMP7 is to break down extracellular matrix by degrading macromolecules including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan.[12][13]