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MMP8

From Wikipedia, the free encyclopedia
MMP8
Available structures
PDBOrtholog search:PDBeRCSB
Identifiers
AliasesMMP8,CLG1, HNC, MMP-8, PMNL-CL, matrix metallopeptidase 8
External IDsOMIM:120355;MGI:1202395;HomoloGene:22482;GeneCards:MMP8;OMA:MMP8 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001304441
NM_001304442
NM_002424

NM_008611

RefSeq (protein)

NP_001291370
NP_001291371
NP_002415

NP_032637

Location (UCSC)Chr 11: 102.71 – 102.73 MbChr 9: 7.56 – 7.57 Mb
PubMedsearch[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Neutrophil collagenase,also known asmatrix metalloproteinase-8(MMP-8) or PMNL collagenase (MNL-CL), is acollagencleavingenzymewhich is present in the connective tissue of most mammals.[5]In humans, the MMP-8proteinis encoded by theMMP8gene.[6][7] The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[5]Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage.

Function

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Proteins of thematrix metalloproteinase(MMP) family are involved in the breakdown ofextracellular matrixin normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The primary function of MMP-8 is the degradation of type I, II and III collagens. In cancer, loss of MMP-8 in the murine MMTV-PyMT breast cancer model has been associated with increased tumor growth and metastatic burden, as well as enhanced tumor vascularity and altered immune cell infiltration.[8]Furthermore, analysis of MMP-8 in breast cancer cell lines revealed a causal connection between MMP-8 activity and IL6 and IL8 production, suggesting a role for MMP-8 in the regulation of the innate immune system.[9]

References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000118113Ensembl,May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000005800Ensembl,May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ab"Entrez Gene: MMP8 matrix metallopeptidase 8 (neutrophil collagenase)".
  6. ^Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL (July 1990)."Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases".J. Biol. Chem.265(20): 11421–4.doi:10.1016/S0021-9258(19)38413-3.PMID2164002.
  7. ^Devarajan P, Mookhtiar K, Van Wart H, Berliner N (June 1991)."Structure and expression of the cDNA encoding human neutrophil collagenase".Blood.77(12): 2731–8.doi:10.1182/blood.V77.12.2731.2731.PMID1646048.
  8. ^Decock, Julie; Hendrickx, Wouter; Thirkettle, Sally; Gutiérrez-Fernández, Ana; Robinson, Stephen D; Edwards, Dylan R (2015)."Pleiotropic functions of the tumor- and metastasis-suppressing matrix metalloproteinase-8 in mammary cancer in MMTV-PyMT transgenic mice".Breast Cancer Res.17(1): 38.doi:10.1186/s13058-015-0545-8.PMC4380014.PMID25848906.
  9. ^Thirkettle, Sally; Decock, Julie; Arnold, Hugh; Pennington, Caroline J; Jaworski, Diane M; Edwards, Dylan R (2013)."Matrix metalloproteinase 8 (collagenase 2) induces the expression of interleukins 6 and 8 in breast cancer cells".J Biol Chem.288(23): 16282–16294.doi:10.1074/jbc.M113.464230.PMC3675567.PMID23632023.

Further reading

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  • TheMEROPSonline database for peptidases and their inhibitors:M10.002