MMP8

Also known as CLG1, HNC, MMP-8, PMNL-CL, matrix metallopeptidase 8

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. In humans, the MMP-8 protein is encoded by the MMP8 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. 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.

Gene data

MMP8

Name: matrix metallopeptidase 8
Type: protein-coding
Position: 102,711,796–102,727,050 (−)
Aliases: CLG1, HNC, MMP-8, PMNL-CL
Ensembl: ENSG00000118113
RefSeq RNA: NM_001304441.2, NM_001304442.2, NM_002424.3, XM_011542834.3, XM_011542835.3
RefSeq protein: NP_001291370.1, NP_001291371.1, NP_002415.1, XP_011541136.1, XP_011541137.1

This gene encodes a member of the matrix metalloproteinase (MMP) family of proteins. These proteins are involved in the breakdown of extracellular matrix in embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Proteolysis at different sites on this protein results in multiple active forms of the enzyme with distinct N-termini. This protein functions in the degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015].