Integrin receptor (RGD-binding)

The so-called "RGD integrin receptor" is not a single molecular entity but refers collectively to a subset of the *integrin* family that specifically recognize and bind the tripeptide motif arginine-glycine-aspartic acid (*RGD*) found in many extracellular matrix proteins such as fibronectin, vitronectin, fibrinogen, and osteopontin. There are eight known human/mammalian *RGD-binding* or *RGD-recognizing* integrins—most notably including αvβ3, α5β1, and αIIbβ3—which mediate diverse biological processes including cell adhesion to the extracellular matrix, signal transduction regulating proliferation or apoptosis, angiogenesis during tumor growth or wound healing, thrombosis via platelet aggregation (αIIbβ3), and tissue remodeling. These receptors are important therapeutic targets for cancer therapy (e.g., antiangiogenic agents like cilengitide), cardiovascular disease/thrombosis prevention (e.g., eptifibatide), diagnostic imaging agents using radiolabeled cyclic-RGD peptides for PET scans in oncology settings, among others. However, "RGD integrin receptor" is not a precise canonical name; it should be replaced by specifying which individual member(s) of this subset are meant—such as "Integrin alpha-v beta 3" (*αvβ3*) or "Integrin alpha-IIb beta 3" (*αIIbβ3*)—since each has distinct tissue distribution and function. **Note:** The term “RGD integrin receptor” is imprecise; it describes a functional group rather than an individual target molecule. For structured data purposes you should use specific names like “Integrin alpha-v beta 3” when possible.

Other names

RGD-binding integrinRGD-recognizing integrinRGD integrinIntegrins (subset recognizing RGD)αvβ3 integrin (example)α5β1 integrin (example)αIIbβ3 integrin (example)

– Inhibition of ligand binding to the extracellular matrix via competitive antagonism at the RGD recognition site on specific integrins, leading to inhibition of cell adhesion, migration, angiogenesis, or platelet aggregation