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Protein MMP8 PDB 1a85.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesMMP8, CLG1, HNC, MMP-8, PMNL-CL, matrix metallopeptidase 8
External IDsOMIM: 120355 MGI: 1202395 HomoloGene: 22482 GeneCards: MMP8
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for MMP8
Genomic location for MMP8
Band11q22.2Start102,711,796 bp[1]
End102,727,050 bp[1]
RNA expression pattern
PBB GE MMP8 207329 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



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

Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving enzyme which is present in the connective tissue of most mammals.[5] In humans, the MMP-8 protein is encoded by the MMP8 gene.[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.


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. 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]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118113 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005800 - Ensembl, 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. ^ a b "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. PMID 2164002.
  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. PMID 1646048.[permanent dead link]
  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: 38. doi:10.1186/s13058-015-0545-8. PMC 4380014. PMID 25848906.
  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). doi:10.1074/jbc.M113.464230. PMC 3675567. PMID 23632023.

Further reading[edit]

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: M10.002