MMP25 explained

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 which 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.^[4]

Further reading

• Nagase H, Woessner JF . Matrix metalloproteinases. . J. Biol. Chem. . 274 . 31 . 21491–4 . 1999 . 10419448 . 10.1074/jbc.274.31.21491 . free .
• Will H, Atkinson SJ, Butler GS, etal . 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 . 1996 . 8663332 . 10.1074/jbc.271.29.17119 . free .
• Bernot A, Heilig R, Clepet C, etal . A transcriptional Map of the FMF region. . Genomics . 50 . 2 . 147–60 . 1998 . 9653642 . 10.1006/geno.1998.5313 .
• Kojima S, Itoh Y, Matsumoto S, etal . 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 . 2000 . 11034316 . 10.1016/S0014-5793(00)01919-0 . 37430406 . free .
• English WR, Velasco G, Stracke JO, etal . Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25). . FEBS Lett. . 491 . 1–2 . 137–42 . 2001 . 11226436 . 10.1016/S0014-5793(01)02150-0 . 34368200 . free .
• Kang T, Yi J, Guo A, etal . Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils. . J. Biol. Chem. . 276 . 24 . 21960–8 . 2001 . 11282999 . 10.1074/jbc.M007997200 . free .
• Strausberg RL, Feingold EA, Grouse LH, etal . 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 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Shin BK, Wang H, Yim AM, etal . 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 . 2003 . 12493773 . 10.1074/jbc.M210455200 . free .
• Matsuda A, Itoh Y, Koshikawa N, etal . 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 . 2003 . 12860995 . 10.1074/jbc.M301509200 . free .
• Nie J, Pei D . 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 . 2003 . 14583471 .
• Blanton SH, Bertin T, Serna ME, etal . 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 . 2004 . 14755462 . 10.1002/ajmg.a.20426 . 38529833 .
• Nie J, Pei D . Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6. . Exp. Cell Res. . 296 . 2 . 145–50 . 2004 . 15149845 . 10.1016/j.yexcr.2004.02.008 .
• Sun Q, Weber CR, Sohail A, etal . 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 . 2007 . 17513868 . 10.1074/jbc.M701737200 . 1978545 . free .

External links

• The MEROPS online database for peptidases and their inhibitors: M10.024

Notes and References

1. Pei D . Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage . Cell Res . 9 . 4 . 291–303 . Feb 2000 . 10628838 . 10.1038/sj.cr.7290028 . free .
2. Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C . Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors . Cancer Res . 60 . 4 . 877–82 . Mar 2000 . 10706098 .
3. Web site: Entrez Gene: MMP25 matrix metallopeptidase 25.
4. Web site: Entrez Gene: MMP25 matrix metallopeptidase 25.