Integrin alpha-V (ITGAV) (ITGAV)

Integrin alpha-V (ITGAV), also known as CD51, is a critical cell surface receptor that functions as the alpha subunit for five distinct integrin heterodimers (alpha-V beta-1, alpha-V beta-3, alpha-V beta-5, alpha-V beta-6, and alpha-V beta-8) [5, 11]. These receptors mediate cell-extracellular matrix (ECM) and cell-cell interactions by binding to ligands containing the Arg-Gly-Asp (RGD) motif, such as vitronectin, fibronectin, and osteopontin [3, 12]. In the context of oncology, alpha-V integrins are significantly overexpressed on both tumor cells and the activated endothelial cells of the tumor neovasculature, while remaining largely absent from resting endothelium [1, 8]. This differential expression makes them attractive therapeutic targets for inhibiting tumor growth, angiogenesis, and metastasis [2, 4]. Drugs targeting alpha-V integrins, including monoclonal antibodies like abituzumab and cyclic peptides like cilengitide, aim to block ligand binding and disrupt outside-in signaling pathways that promote cell survival and migration [6, 14]. Despite their strong biological rationale and success in preclinical models, many alpha-V-targeted therapies have faced challenges in clinical trials, often due to the redundancy of angiogenic signaling and the complex regulatory roles of these receptors in the tumor microenvironment [13, 16]. Current research continues to explore alpha-V integrins as biomarkers for patient selection and as anchors for the targeted delivery of cytotoxic agents or imaging probes [1, 16].

Other names

CD51Vitronectin receptor subunit alphaMSK8VNRAVTNR

Inhibition of integrin-ligand binding (RGD motif), suppression of outside-in signaling pathways (e.g., FAK, Src, MAP kinase), disruption of tumor angiogenesis, and induction of endothelial cell apoptosis (anoikis) [1, 8, 14].