MMP25

Matrix metallopeptidase 25, also known as MMP25, is a human gene.cite web | title = Entrez Gene: MMP25 matrix metallopeptidase 25| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64386| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: MMP25 matrix metallopeptidase 25| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64386| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=
*cite journal | author=Will H, Atkinson SJ, Butler GS, "et al." |title=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. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17119–23 |year= 1996 |pmid= 8663332 |doi=
*cite journal | author=Bernot A, Heilig R, Clepet C, "et al." |title=A transcriptional Map of the FMF region. |journal=Genomics |volume=50 |issue= 2 |pages= 147–60 |year= 1998 |pmid= 9653642 |doi=
*cite journal | author=Pei D |title=Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. |journal=Cell Res. |volume=9 |issue= 4 |pages= 291–303 |year= 2000 |pmid= 10628838 |doi= 10.1038/sj.cr.7290028
*cite journal | author=Velasco G, Cal S, Merlos-Suárez A, "et al." |title=Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors. |journal=Cancer Res. |volume=60 |issue= 4 |pages= 877–82 |year= 2000 |pmid= 10706098 |doi=
*cite journal | author=Kojima S, Itoh Y, Matsumoto S, "et al." |title=Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP. |journal=FEBS Lett. |volume=480 |issue= 2-3 |pages= 142–6 |year= 2000 |pmid= 11034316 |doi=
*cite journal | author=English WR, Velasco G, Stracke JO, "et al." |title=Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25). |journal=FEBS Lett. |volume=491 |issue= 1-2 |pages= 137–42 |year= 2001 |pmid= 11226436 |doi=
*cite journal | author=Kang T, Yi J, Guo A, "et al." |title=Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils. |journal=J. Biol. Chem. |volume=276 |issue= 24 |pages= 21960–8 |year= 2001 |pmid= 11282999 |doi= 10.1074/jbc.M007997200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Shin BK, Wang H, Yim AM, "et al." |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607–16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200
*cite journal | author=Matsuda A, Itoh Y, Koshikawa N, "et al." |title=Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils. |journal=J. Biol. Chem. |volume=278 |issue= 38 |pages= 36350–7 |year= 2003 |pmid= 12860995 |doi= 10.1074/jbc.M301509200
*cite journal | author=Nie J, Pei D |title=Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. |journal=Cancer Res. |volume=63 |issue= 20 |pages= 6758–62 |year= 2003 |pmid= 14583471 |doi=
*cite journal | author=Blanton SH, Bertin T, Serna ME, "et al." |title=Association of chromosomal regions 3p21.2, 10p13, and 16p13.3 with nonsyndromic cleft lip and palate. |journal=Am. J. Med. Genet. A |volume=125 |issue= 1 |pages= 23–7 |year= 2004 |pmid= 14755462 |doi= 10.1002/ajmg.a.20426
*cite journal | author=Nie J, Pei D |title=Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6. |journal=Exp. Cell Res. |volume=296 |issue= 2 |pages= 145–50 |year= 2004 |pmid= 15149845 |doi= 10.1016/j.yexcr.2004.02.008
*cite journal | author=Sun Q, Weber CR, Sohail A, "et al." |title=MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties. |journal=J. Biol. Chem. |volume=282 |issue= 30 |pages= 21998–2010 |year= 2007 |pmid= 17513868 |doi= 10.1074/jbc.M701737200

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