Matrix Metalloproteinase functions in tissue remodeling linked with several physiological or pathological processes like morphogenesis, tissue repair, cirrhosis, metastasis, angiogenesis and arthritis. An excess of Matrix Metalloproteinase degrade the structuralproteins of the aortic wall, thus deregulation of these enzymes characterized acute and chronic cardiovascular diseases. It is also competent in degrading all kinds of extracellular matrix proteins yet can process a number of bioactive molecules.
Matrix Metalloproteinase are members of family astacins, adamalysins and serralysins that are zinc dependent endopeptidase. Have three common domain structures such as pro-peptide domain,catalytic domain and haemopexin-like C-terminal domain that are associated to the catalytic domain via flexible hinge region.
Matrix Metalloproteinase are known to mixed up in the cleavage of cell surface receptors, liberate apoptotic ligands and chemokine inactivation as well as functions in cell behaviors like cell proliferation, adhesion, differentiation, migration and host defense. Have diverse substrate specificity and are programmed by different genes that are notable from other endopeptidases due to its dependence on metal ion as co-factors and its capability to degrade extracellular matrix and its specific evolutionary DNA sequence.
Gene name: MMP14
Protein name: Matrix metalloproteinase-14