Biology:MMP25

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 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

• "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
• "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. doi:10.1074/jbc.271.29.17119. PMID 8663332. 
• "A transcriptional Map of the FMF region.". Genomics 50 (2): 147–60. 1998. doi:10.1006/geno.1998.5313. PMID 9653642. 
• "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. doi:10.1016/S0014-5793(00)01919-0. PMID 11034316. 
• "Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25).". FEBS Lett. 491 (1–2): 137–42. 2001. doi:10.1016/S0014-5793(01)02150-0. PMID 11226436. 
• "Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils.". J. Biol. Chem. 276 (24): 21960–8. 2001. doi:10.1074/jbc.M007997200. PMID 11282999. 
• "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. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "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. doi:10.1074/jbc.M210455200. PMID 12493773. 
• "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. doi:10.1074/jbc.M301509200. PMID 12860995. 
• "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. PMID 14583471. 
• "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. doi:10.1002/ajmg.a.20426. PMID 14755462. 
• "Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6.". Exp. Cell Res. 296 (2): 145–50. 2004. doi:10.1016/j.yexcr.2004.02.008. PMID 15149845. 
• "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. doi:10.1074/jbc.M701737200. PMID 17513868. 

External links

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