Platelet-derived growth factor receptor alpha and Platelet-derived growth factor receptor beta (PDGFRA, PDGFRB)

Platelet-derived growth factor receptors alpha (PDGFRA) and beta (PDGFRB) are closely related cell-surface receptor tyrosine kinases that bind members of the platelet-derived growth factor (PDGF) family[1][4][6]. Upon ligand binding, these receptors dimerize and become activated through transphosphorylation of tyrosine residues, initiating signal transduction cascades that regulate vital cellular processes including proliferation, migration, differentiation, and survival[1][2][3]. PDGFRA/PDGFRB are essential during embryonic development and tissue maintenance, particularly affecting connective tissue cells[4]. Aberrant activation—through mutations, gene fusions (e.g., ETV6-PDGFRB in leukemia), or overexpression—contributes to the pathogenesis of various cancers, fibroproliferative diseases, and cardiovascular disorders[2][3][4]. PDGFRA/PDGFRB are important therapeutic targets of several tyrosine kinase inhibitors used in oncology and hematology, but clinical use is associated with class-related safety concerns[2][4][6].

Other names

PDGFR-αPDGFR-βCD140a (alpha)CD140b (beta)PDGF receptor alphaPDGF receptor beta

Tyrosine kinase inhibition; Blockade of PDGF ligand binding or receptor dimerization; Inhibition of downstream signaling pathways (e.g., PI3K/AKT, Ras/MAPK, Src family kinases); Inhibition of receptor autophosphorylation