MMP 2 Substrate, fluorogenic

Matrix metalloproteinases (MMP) are a family of zinc-dependent endopeptidases that degrade matrix proteins. MMPs include collagenases, gelatinases, matrilysins, enamelysins, metalloelastases, stromelysins and other structural protein and receptor lysins. The activity of these enzymes is selectively inhibited or measured by appropriately labeled peptides. MCA-Pro-Leu-Ala-Nva-DNP-Dap-Ala-Arg-NH2; DNP-Pro-Leu-Gly-Met-Trp-Ser-Arg (DNP-PLGMWSR), Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 (DNP-PLGLWA-D-R-NH2), Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH (DNP-PQGIAGQ-D-R-OH) and MOCAc [(7-methoxy coumarin-4-yl) acetyl]-RPKPYANvaWMK(Dnp[2,4-dinitrophenyl])-NH(2) are substrates for matrix metalloproteinase 2.

Matrix metalloproteinases (MMPs) are responsible for degrading membrane proteins, such as basal lamina proteins of cerebral blood vessels. Proteolysis of intracellular substrates by MMPs is associated with the innate immune system and apoptosis. They are also involved in disease conditions such as oncogenesis, cardiac, neurological and autoimmune disorders. MMPs are also associated with pathogenesis related to protein conformational changes. Elevated expression of a number of MMPs is observed in myocardial infarction and heart failure.

Matrix metalloproteinases (MMPs) are localized to the nucleus, mitochondria, vesicles and cytoplasm. MMP family comprises of 25 members, of which 24 are present in mammals. MMPs are encoded as inactive enzymes and are localized to cell membranes. All MMP members possess pro domain (80 amino acids) and catalytic domains.