MMP25

MMP25
Identifiers
Aliases	MMP25 , MMP-25, MMP20, MMP20A, MMPL1, MT-MMP 6, MT-MMP6, MT6-MMP, MT6MMP, MTMMP6, matrix metallopeptidase 25
External IDs	OMIM: 608482; MGI: 2443938; HomoloGene: 23375; GeneCards: MMP25; OMA:MMP25 - orthologs
Gene location (Mouse) Chr. Chromosome 17 (mouse) [1] Band 17|17 A3.3 Start 23,847,285 bp [1] End 23,864,251 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in blood spleen vena cava olfactory bulb sperm periodontal fiber appendix body of tongue cervix epithelium bone marrow Top expressed in granulocyte epiblast bone marrow trigeminal ganglion embryo embryo morula tail of embryo thymus neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component integral component of membrane extracellular region anchored component of membrane membrane plasma membrane specific granule membrane extracellular matrix extracellular space Biological process inflammatory response hard palate development proteolysis neutrophil degranulation extracellular matrix organization collagen catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 64386 240047 Ensembl n/a ENSMUSG00000023903 UniProt Q9NPA2 Q3U435 RefSeq (mRNA) NM_004142 NM_022468 NM_022718 NM_001033339 NM_001320258 RefSeq (protein) NP_071913 NP_001028511 NP_001307187 Location (UCSC) n/a Chr 17: 23.85 – 23.86 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene. ^{[4] [5] [6]}

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. ^[6]

References

1. GRCm38: Ensembl release 89: ENSMUSG00000023903 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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.
5. 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.
6. "Entrez Gene: MMP25 matrix metallopeptidase 25".

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi: 10.1074/jbc.274.31.21491 . 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. doi: 10.1074/jbc.271.29.17119 . PMID   8663332.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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. S2CID   38529833.
• 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 . PMC   1978545 . PMID   17513868.

External links

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