Platelet-derived growth factor receptor (PDGFR) (PDGFR)

Platelet-derived growth factor receptor (PDGFR) is a cell-surface receptor tyrosine kinase that plays a pivotal role in regulating cell growth, proliferation, and migration. It exists as two distinct subunits, alpha (PDGFRA) and beta (PDGFRB), which form homo- or heterodimeric complexes upon binding to their ligands, such as the PDGF-BB homodimer and the PDGF-AB heterodimer. PDGF-BB is a universal ligand that activates all three receptor dimer combinations (alpha-alpha, alpha-beta, and beta-beta), while PDGF-AB primarily activates the alpha-alpha and alpha-beta forms. These receptors are essential for normal physiological processes, including embryonic development and wound healing, but their overactivation is linked to various pathologies, including glioblastoma, gastrointestinal stromal tumors (GIST), and fibrotic diseases. Therapeutic intervention involves small-molecule inhibitors like imatinib and sunitinib that block the intracellular kinase activity, as well as monoclonal antibodies like olaratumab that target the extracellular domain. Conversely, recombinant PDGF-BB (becaplermin) is utilized as a therapeutic agonist to promote the healing of chronic wounds, such as diabetic foot ulcers.

Other names

PDGF receptorCD140PDGFRAPDGFRBPlatelet-derived growth factor receptor alphaPlatelet-derived growth factor receptor betaPDGF-BBPDGF-AB

Inhibition of receptor tyrosine kinase activity, competitive antagonism of ligand binding, and agonistic activation of the receptor signaling pathway.