Role of lysyl oxidase in myocardial fibrosis. From basic science to clinical aspects
López B, González A, Hermida N, Valencia F, de Teresa E, Diez J.
1C entre for Applied Medical Research, University of Navarra.
Magazine: American Journal of Physiology
Date: May 14, 2010Cardiology
Due to its dynamic nature, the composition and structure of the myocardial collagen network can be reversibly modified to adapt to transient cardiac injuries. In response to persistent injury however, irreversible, maladaptive changes of the network occur leading to fibrosis mostly characterized by the excessive interstitial and perivascular deposition of collagen types I and III fibers.
It is now becoming apparent that myocardial fibrosis directly contributes to adverse myocardial remodeling and the resulting alterations of left ventricular (LV) anatomy and function present in the major types of cardiac diseases. The enzyme lysyl oxidase (LOX) is a cupper-dependent extracellular enzyme that catalyzes lysine-derived cross-links in collagen and elastin. LOX-mediated cross-linking of collagen types I and III fibrils leads to the formation of stiff collagen types I and III fibers and their subsequent tissue deposition.
Evidence from experimental and clinical studies shows that the excess of LOX is associated with increased collagen cross-linking and stiffness. It is thus conceivable that LOX up-regulation and/or overactivity could underlie myocardial fibrosis and altered LV mechanics and contribute to the compromise of LV function in cardiac diseases.
This review will consider the molecular aspects related to the regulation and actions of LOX, namely in the context of collagen synthesis. In addition, it will address the information related to the role of myocardial LOX in heart failure and the potential benefits of controlling its expression and function.
CITATION Am J Physiol Heart Circ Physiol. 2010 Jul;299(1):H1-9
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