MMP25
Template:Short description An Error has occurred retrieving Wikidata item for infobox Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene.[1][2][3]
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily, attached to the plasma membrane via a glycosylphosphatidyl inositol anchor. In response to bacterial infection or inflammation, the encoded protein is thought to inactivate alpha-1 proteinase inhibitor, a major tissue protectant against proteolytic enzymes released by activated neutrophils, facilitating the transendothelial migration of neutrophils to inflammatory sites. The encoded protein may also play a role in tumor invasion and metastasis through activation of MMP2. The gene has previously been referred to as MMP20 but has been renamed MMP25.[3]
References
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- ^ Page Module:Citation/CS1/styles.css has no content.Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
- ^ Page Module:Citation/CS1/styles.css has no content.Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: MMP25 matrix metallopeptidase 25".
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
- Page Module:Citation/CS1/styles.css has no content.Will H, Atkinson SJ, Butler GS, et al. (1996). "The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3". J. Biol. Chem. 271 (29): 17119–23. doi:10.1074/jbc.271.29.17119. PMID 8663332.
- Page Module:Citation/CS1/styles.css has no content.Bernot A, Heilig R, Clepet C, et al. (1998). "A transcriptional Map of the FMF region". Genomics. 50 (2): 147–60. doi:10.1006/geno.1998.5313. PMID 9653642.
- Page Module:Citation/CS1/styles.css has no content.Kojima S, Itoh Y, Matsumoto S, et al. (2000). "Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP". FEBS Lett. 480 (2–3): 142–6. Bibcode:2000FEBSL.480..142K. doi:10.1016/S0014-5793(00)01919-0. PMID 11034316. S2CID 37430406.
- Page Module:Citation/CS1/styles.css has no content.English WR, Velasco G, Stracke JO, et al. (2001). "Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25)". FEBS Lett. 491 (1–2): 137–42. Bibcode:2001FEBSL.491..137E. doi:10.1016/S0014-5793(01)02150-0. PMID 11226436. S2CID 34368200.
- Page Module:Citation/CS1/styles.css has no content.Kang T, Yi J, Guo A, et al. (2001). "Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils". J. Biol. Chem. 276 (24): 21960–8. doi:10.1074/jbc.M007997200. PMID 11282999.
- Page Module:Citation/CS1/styles.css has no content.Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Page Module:Citation/CS1/styles.css has no content.Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
- Page Module:Citation/CS1/styles.css has no content.Matsuda A, Itoh Y, Koshikawa N, et al. (2003). "Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils". J. Biol. Chem. 278 (38): 36350–7. doi:10.1074/jbc.M301509200. PMID 12860995.
- Page Module:Citation/CS1/styles.css has no content.Nie J, Pei D (2003). "Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond". Cancer Res. 63 (20): 6758–62. PMID 14583471.
- Page Module:Citation/CS1/styles.css has no content.Blanton SH, Bertin T, Serna ME, et al. (2004). "Association of chromosomal regions 3p21.2, 10p13, and 16p13.3 with nonsyndromic cleft lip and palate". Am. J. Med. Genet. A. 125 (1): 23–7. doi:10.1002/ajmg.a.20426. PMID 14755462. S2CID 38529833.
- Page Module:Citation/CS1/styles.css has no content.Nie J, Pei D (2004). "Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6". Exp. Cell Res. 296 (2): 145–50. doi:10.1016/j.yexcr.2004.02.008. PMID 15149845.
- Page Module:Citation/CS1/styles.css has no content.Sun Q, Weber CR, Sohail A, et al. (2007). "MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties". J. Biol. Chem. 282 (30): 21998–2010. doi:10.1074/jbc.M701737200. PMC 1978545. PMID 17513868.
External links
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