The integrin family of cell adhesion receptors consists of at least 19 membrane-associated heterodimers, composed of an alpha and beta subunit that associate in a non-covalent manner. To date, 16 different alpha-subunits and 8 different beta-subunits have been identified. 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. Integrin alphaV is a type I membrane glycoptroein with no I (inserted) domain. The alphaV protein is post-translationally cleaved into a heavy and light chain, which is expressed on the cell surface as a disulfide linked polypeptide.