Matrix Metalloproteinase-2

Matrix Metalloproteinase-2 (MMP-2), also known as 72kd type IV collagenase, is a ubiquitous metalloproteinase that is involved in diverse functions including remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. MMP-2 is also involved in degrading extracellular matrix proteins, and can act on several non-matrix proteins such as big endothelin-1 and beta-type CGRP, promoting vasoconstriction. It appears to have a role in myocardial cell death pathways and contributes to myocardial oxidative stress by regulating the activity of GSK3 beta. The C-terminal non-catalytic fragment of MMP-2 possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro. The pro-peptide is processed by MMP-14 (MT-MMP-1) and MMP-16 (MT-MMP-3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrin/beta3. Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast, and prostate.

Swiss-Prot Accession Number: P08253