Integrin, RGD-binding subtype (RGD-binding integrin)

RGD-binding integrins are a subclass of the integrin receptor family defined by their ability to specifically recognize and bind to proteins containing the Arg-Gly-Asp (RGD) tripeptide motif, found in many extracellular matrix components such as fibronectin, vitronectin, and fibrinogen[1][2][7]. These integrins are heterodimeric transmembrane glycoproteins, each composed of an α and a β subunit, with a crucial role in mediating cell adhesion, migration, signal transduction, and survival signals[5][7]. Subtype members include integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, α8β1, and αIIbβ3; they govern diverse physiological processes and are implicated in pathological contexts such as cancer, thrombosis, fibrosis, and inflammation[6][7]. RGD-binding integrins are validated therapeutic targets, with clinically approved inhibitors like Eptifibatide (for αIIbβ3 in acute coronary syndromes) and experimental drugs such as Cilengitide (for αvβ3/αvβ5 in oncology)[1][6][7]. Their essential function in cell-extracellular matrix interactions also makes them critical research tools and imaging targets[1][7].

Other names

RGD-binding integrinArg-Gly-Asp-binding integrinRGD-dependent integrinαv-class integrin (when referring to certain αv subunit containing integrins, but more precisely refers to a subset)Specific heterodimers (see below) include: integrin αvβ3, αvβ5, αvβ6, αvβ8, α5β1, α8β1, αIIbβ3

Inhibition of ligand binding (competing with endogenous RGD motif for integrin binding, blocking ECM attachment); Inhibition of platelet aggregation (specific for αIIbβ3 antagonists); Inhibition of angiogenesis and tumor cell migration (by preventing integrin-ECM interactions); Modulation of cell signaling (via altered cytoskeletal and signal transduction responses to ligand binding/blockade)