MMP25

Protein-coding gene in the species Homo sapiens
MMP25
Identifiers
AliasesMMP25, MMP-25, MMP20, MMP20A, MMPL1, MT-MMP 6, MT-MMP6, MT6-MMP, MT6MMP, MTMMP6, matrix metallopeptidase 25
External IDsOMIM: 608482 MGI: 2443938 HomoloGene: 23375 GeneCards: MMP25
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[1]
Chromosome 17 (mouse)
Genomic location for MMP25
Genomic location for MMP25
Band17|17 A3.3Start23,847,285 bp[1]
End23,864,251 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • spleen

  • vena cava

  • olfactory bulb

  • sperm

  • periodontal fiber

  • appendix

  • body of tongue

  • cervix epithelium

  • bone marrow
Top expressed in
  • bone marrow

  • trigeminal ganglion

  • morula

  • thymus

  • neural tube

  • jejunum

  • ileum

  • mesencephalon

  • lip

  • colon
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
SpeciesHumanMouse
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/aChr 17: 23.85 – 23.86 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/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 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.[6]

References

  1. ^ a b c 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. ^ a b "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. 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. 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


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