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.
- ^ a b c GRCh38: Ensembl release 89: ENSG00000118113 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005800 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: MMP8 matrix metallopeptidase 8 (neutrophil collagenase)".
- ^ 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. PMID 2164002.
- ^ 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. PMID 1646048.