Neutrophil collagenase (IPR028709)

Short name: MMP8

Overlapping homologous superfamilies


Family relationships


Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that degrade most components of the extracellular matrix (ECM) and process a number of bioactive molecules. Collagenases are MMPs that share the ability to cleave the native helix of fibrillar collagens at a single peptide bond. Collagenase-1 (MMP1 or interstitial collagenase) and collagenase-2 (MMP8 or neutrophil collagenase) initiate the breakdown of the extracellular matrix by degrading native interstitial collagen types I, II, and III. They cleave the helical collagen molecule at a single Gly-Ile/Leu bond in each alpha-chain of the molecule. The cleavage generates fragments that spontaneously lose their helical conformation, denature to gelatin, and become soluble. The gelatin is then susceptible to attack by gelatinases and other proteases [PMID: 8898355].

Neutrophil collagenase (MMP8) may play a role in the degradation of collagen fibres during postpartum uterine involution [PMID: 9727011].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.