Matrix Metalloproteinase 2 and Type Ⅱ D.M in The Elderly

Abstract

Background:  Matrix metalloproteinases (MMPs) are a family of zinc-binding proteolytic enzymes that normally remodel the extracellular matrix such as collagen, gelatin, fibronectin, laminin, elastin, and proteoglycans and pathologically attack substrates as part of an inflammatory response. Increased activity of MMPs has been reported in numerous disease processes including tumor growth, arthritis and cardiovascular disease. Increased matrix degradation by MMPs within the atherosclerotic plaque has been implicated as one of the key factors that leads to plaque instability, and consequently to cardiovascular events. Deterioration of MMP regulation contributes to the development of arterial lesions, in part, by facilitating monocyte invasion. Gelatin zymography studies have shown that MMPs, especially MMP-2 (72-kDa gelatinase A) and MMP-9 (92-kDa gelatinase B), are involved in remodeling processes associated with atherogenesis. MMPs are synthesized in atheromatous plaques and are present at elevated levels in rupture-prone shoulder regions of arterial blood vessels. Increased MMP activity has also been correlated with cardiovascular pathologies. Since vascular complications such as acute coronary artery syndrome and peripheral arterial disease are significantly more common among diabetics. Chronic low-grade inflammation is a characteristic feature of T2DM. MMPs are involved in modulating the inflammatory response by regulating the migration and activation of immune cells, as well as the release of pro-inflammatory cytokines. Elevated levels of MMPs have been observed in the circulation and tissues of individuals with T2DM, suggesting their potential role in promoting inflammation and contributing to the pathogenesis of the disease