MMP25

Matrix metallopeptidase 25
Identifiers
Symbols	MMP25 ; MMP20; MMPL1; MT-MMP6; MT6-MMP
External IDs	Template:OMIM5 Template:MGI HomoloGene: 23375
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MMP25 207289 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Matrix metallopeptidase 25, also known as MMP25, is a human gene.

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.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
• 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. PMID 8663332.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bernot A, Heilig R, Clepet C; et al. (1998). "A transcriptional Map of the FMF region". Genomics. 50 (2): 147–60. PMID 9653642.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pei D (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.
• Velasco G, Cal S, Merlos-Suárez A; et al. (2000). "Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 11034316.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 11226436.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• 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. PMID 17513868.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)