Matrix metalloproteinases in myocardial ischemia-reperfusion injury in Progress.docVIP

 PAGE \* MERGEFORMAT 18 Matrix metalloproteinases in myocardial ischemia-reperfusion injury in Progress [Keywords:] matrix metalloproteinases, myocardium, ischemia reperfusion injury Recent studies indicate that matrix metalloproteinase (matrix metalloproteinases, MMPs) involved in platelet aggregation, myocardial ischemia reperfusion injury and other acute process. In a variety of cardiovascular diseases such as atherosclerosis, myocardial infarction, heart failure, ventricular remodeling, arterial neointimal formation after injury to play an important role. appropriate inhibition of MMPs may become drug targets for the treatment of cardiovascular disease. MMPs this paper the structure, function and biochemistry as well as in ischemia-reperfusion injury are summarized below. 1 MMPs three-dimensional structure (1) 5 side by a pleated sheet, three rings of helices and connecting the main chain. In general, protease region is the catalytic role played by one of zinc, a structure (I) of zinc and three calcium ions. Bottom material breach by the IV chain connection, helix and -helix formed after the extended ring region. three histidine active site zinc coordination. Central region, including the conservative “spin Met”, which is the catalytic role of zinc from the surrounding support structure from the foundation. 2 MMPs function and biochemical Since 1962, Gross and Lapiere found the first since the MMPs collagenase, has found that about 66 kinds of MMPs (including 25 kinds of human MMPs). Based on their structure and substrate can be divided into six major categories: collagen enzyme, matrilysin, matrix soluble factor, gelatinase, membrane-type MMPs (MT MMP, matrix metalloproteinase other MMPs. MMPs are structurally related peptides with zinc enzyme family. MMP in the normal degradation of the extracellular matrix play an important role in these physiological processes, including: tissue, tissue repair, angiogenesis, and so on. In addi