RGD-binding integrin

RGD-binding integrins on cardiac myocytes are a specialized group of heterodimeric transmembrane receptors that recognize the Arg-Gly-Asp (RGD) amino acid sequence found in various extracellular matrix (ECM) proteins, such as fibronectin, vitronectin, and osteopontin. In the heart, the primary RGD-binding integrins expressed on myocytes include alpha-5 beta-1, alpha-v beta-3, and alpha-v beta-5. These receptors are localized at critical structural sites like costameres and intercalated discs, where they function as mechanotransducers that convert physical forces into biochemical signals to regulate cardiomyocyte survival, contractility, and growth. Under pathological conditions such as myocardial infarction, pressure overload, or diabetic cardiomyopathy, the expression and activity of these integrins are significantly upregulated. This overactivation contributes to maladaptive cardiac remodeling, excessive fibrosis, and cardiomyocyte apoptosis. Consequently, RGD-binding integrins have emerged as therapeutic targets for RGD-mimetic drugs and as homing sites for targeted nanomedicines designed to deliver cardioprotective agents directly to the injured myocardium. Furthermore, RGD-based radiopharmaceuticals are increasingly used in molecular imaging to non-invasively monitor cardiac repair and the progression of heart failure.

Other names

Arginine-glycine-aspartic acid-binding integrinVitronectin receptorFibronectin receptorRGD-recognizing integrin

Integrin antagonism and competitive inhibition of extracellular matrix binding