Integrin alpha-V-containing heterodimers (Alpha-v integrins)

Integrin alpha-V-containing heterodimers, also known as alpha-v (αv) integrins, are a subgroup of the integrin family of cell surface receptors that share the αv subunit (ITGAV) paired with one of five beta subunits: β1, β3, β5, β6, or β8 [NIH, 1.3.1]. These heterodimers primarily recognize the Arginine-Glycine-Aspartic acid (RGD) tripeptide motif in extracellular matrix (ECM) proteins such as vitronectin, fibronectin, and osteopontin [NIH, 1.2.4]. They play critical roles in mediating cell-ECM adhesion, migration, and bidirectional signaling (outside-in and inside-out), which are essential for processes like angiogenesis, wound healing, and tissue remodeling [NIH, 1.4.3]. In disease states, αv integrins are frequently upregulated and contribute to tumor progression, metastasis, and pathological fibrosis, particularly through the activation of latent TGF-β, a process primarily mediated by αvβ6 and αvβ8 [NIH, 1.1.4, 1.2.1]. Therapeutic strategies targeting these receptors include monoclonal antibodies like abituzumab and small-molecule inhibitors like bexotegrast, designed to block ligand binding or TGF-β activation, with applications in oncology and fibrotic diseases [NIH, 1.1.1, 1.1.4].

Other names

αv integrinsAlpha-v integrinsITGAV-containing heterodimersVitronectin receptors (subset)

Competitive inhibition of the RGD-binding site on the integrin extracellular domain, preventing interaction with extracellular matrix ligands and inhibiting downstream signaling pathways such as FAK/Src; specific inhibition of αvβ6 and αvβ8 also prevents the mechanical activation of latent TGF-beta [NIH, 1.2.4, 1.3.1].