Integrin alpha-V (CD51, Vitronectin receptor subunit alpha; UniProt P06756) and Integrin beta-3 (CD61, GPIIIa, Platelet membrane glycoprotein IIIa; UniProt P05106) are encoded by the ITGAV (MSK8, VNRA; Gene ID 3685) and ITGB3 (GP3A; Gene ID 3690) gene, respectively, in human. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and a beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence, known to be present in the extracellular matrix components fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. The involvement of integrins in vascular proliferation, adhesion, and wound repair has been well documented. The adhesion receptor, integrin alphaVbeta3, appears to be selectively expressed on growing blood vessels and has been identified as a marker of angiogenic vascular tissue. Due to its involvement in angiogenesis, integrin alphaVbeta3 is among of the most studied integrin receptors.