RGD-dependent integrin

RGD-dependent integrins are a major subclass of the integrin family of cell surface receptors that specifically recognize the Arg-Gly-Asp (RGD) motif present in key extracellular matrix proteins such as fibronectin, vitronectin, osteopontin, and von Willebrand factor. Structurally, they are heterodimeric transmembrane receptors composed of one α and one β subunit—especially those containing αv or α5/8/IIb paired with β1/β3/β5/β6/β8—which mediate cell adhesion, migration, proliferation, survival, and intracellular signaling. They play a central functional role in physiological processes like tissue remodeling, wound healing, and angiogenesis, as well as in pathological conditions such as cancer progression, metastasis, and thrombosis. RGD-dependent integrins are prominent therapeutic targets, particularly in oncology and cardiovascular disease, with several drugs and peptide mimetics developed to inhibit their function. The inhibition of these integrins disrupts adhesive cell-ECM interactions, blocks neovascularization, and induces apoptosis in certain contexts. Monitoring integrin expression serves as a biomarker in some cancers, but clinical application of therapeutics is limited by bleeding risks and potential off-target effects.[1][3][5][6] Note: "RGD-dependent integrin" is a grouping of several specific integrin heterodimers rather than a single protein; it refers chiefly to αvβ3, αvβ5, α5β1, αvβ1, αvβ6, αvβ8, α8β1, and αIIbβ3[3][6]. For research or therapeutic applications, a more precise target (such as a specific integrin heterodimer) may be required.

Other names

integrins (RGD-binding subtype)RGD-binding integrinArg-Gly-Asp-binding integrinRGD motif integrinintegrin αvβ3integrin αvβ5integrin α5β1other specific αv or α5/8/IIb/β1/β3/β5/β6/β8 dimers that bind RGD motif

Inhibition of integrin-ligand binding (competitive antagonism); Disruption of cell adhesion and migration; Induction of cell apoptosis (detachment-induced, or anoikis); Blockade of angiogenesis