A synthetic peptide corresponding to the hinge of human MMP-9.
Alternative Synonym:
CLG4B,GELB,macrophage gelatinase,MANDP2,matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase),matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase),matrix metalloproteinase-9,MMP-9,type V collagenase.
Matrix metalloproteinases (MMPs) belong to a family of proteinases that target many extracellular matrix proteins including additional proteinases, growth factors, cell surface receptors and adhesion molecules. MMPs contain common domain structures that include a signal sequence, a propeptide, a catalytic domain, and a hemopexin-like (Hpx) domain. The MMP activity requires proteolytic cleavage of MMPs in order to geneRate activie MMPs by release of the inhibitory propeptide domain from the whole molecules. MMP-2, MMP-3, MMP-7, MMP-9 and MMP-13 have been characterized as important factors for normal tissue remodeling during embryo development and wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis. MMP activities are correlated with cancer metastatic process.MMP-2 and MMP-9, gelatinases, degrade basement membrane collagen.