Integrin alpha V
Integrin alpha V (CD51), encoded by ITGAV, is the most versatile RGD-binding alpha subunit, forming heterodimers with beta-1, beta-3, beta-5, beta-6 and beta-8 that collectively recognize vitronectin, fibronectin, fibrinogen, osteopontin and latent TGF-beta. The alpha V chain is synthesized as a single precursor that is proteolytically cleaved into disulfide-linked heavy and light chains. These receptors are central to angiogenesis, bone remodeling, wound repair and immune regulation, the latter through TGF-beta activation by the beta-6 and beta-8 partners. Alpha V integrins are upregulated in tumor neovasculature, which underpins both therapeutic antibodies and RGD-based imaging ligands such as radiolabeled peptides used for PET imaging of tumors.