Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

1. These results suggest that PEP-1-SIRT2 promotes matrix metalloproteinases-induced dedifferentiation via ERK signaling in articular chondrocytes. PMID: 27697532
2. the total content and active forms of matrix metalloproteinases (MMPs)-1, -3, and -13 was measured to assess the potential role of the mechanical environment in regulation of matrix turnover by ligament fibroblasts. PMID: 23879595
3. chitosan-pDNA nanoparticles encoding shRNA targeting MMP-3 and -13 had great potential in silencing the dedifferentiation-related genes for regenerating prolonged and endurable cartilage. PMID: 23520014
4. Leptin can induce MMP-13 and have a synergistic induction effect on NO with TNF-alpha in rabbit articular chondrocytes in vitro. PMID: 19893248

Secreted, extracellular space, extracellular matrix. Secreted.

Peptidase M10A family

KEGG: ocu:100008685

STRING: 9986.ENSOCUP00000002145

UniGene: Ocu.2263