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]
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]
^ abcGRCh38: Ensembl release 89: ENSG00000137673 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000018623 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Knox JD, Boreham DR, Walker JA, Morrison DP, Matrisian LM, Nagle RB, Bowden GT (Jan 1997). "Mapping of the metalloproteinase gene matrilysin (MMP7) to human chromosome 11q21→q22". Cytogenet Cell Genet. 72 (2–3): 179–82. doi:10.1159/000134181. PMID 8978768.
^Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273. PMID 2844164.
^Woessner JF, Taplin CJ (November 1988). "Purification and properties of a small latent matrix metalloproteinase of the rat uterus". The Journal of Biological Chemistry. 263 (32): 16918–25. doi:10.1016/S0021-9258(18)37479-9. PMID 3182822.
^Quantin B, Murphy G, Breathnach R (June 1989). "Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members". Biochemistry. 28 (13): 5327–34. doi:10.1021/bi00439a004. PMID 2550050.
^Miyazaki K, Hattori Y, Umenishi F, Yasumitsu H, Umeda M (December 1990). "Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line". Cancer Research. 50 (24): 7758–64. PMID 2253219.
^Woessner JF, Taplin CJ (November 1988). "Purification and properties of a small latent matrix metalloproteinase of the rat uterus". J. Biol. Chem. 263 (32): 16918–25. doi:10.1016/S0021-9258(18)37479-9. PMID 3182822.
^ abParks WC, Mecham RP (1988). "Matrix Metalloproteinases". 263. San Diego: Academic. {{cite journal}}: Cite journal requires |journal= (help)
^Yokoyama Y, Grünebach F, Schmidt SM, Heine A, Häntschel M, Stevanovic S, Rammensee HG, Brossart P (2008). "Matrilysin (MMP-7) is a novel broadly expressed tumor antigen recognized by antigen-specific T cells". Clin. Cancer Res. 14 (17): 5503–11. doi:10.1158/1078-0432.CCR-07-4041. PMID 18765542. S2CID 8202181.
uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme (EC 3.4.24.23) has also been known as matrin, putative (or...
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