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

The Platelet-derived growth factor receptor (PDGFR) family consists of two primary isoforms, PDGFR-alpha (PDGFRA) and PDGFR-beta (PDGFRB), which are members of the Type III receptor tyrosine kinase (RTK) family [1]. These receptors are essential regulators of mesenchymal cell biology, influencing cell proliferation, migration, and survival during both embryonic development and adult tissue repair [2]. Upon binding to their cognate PDGF ligands, the receptors undergo dimerization and autophosphorylation, activating downstream signaling cascades such as the PI3K/AKT, MAPK/ERK, and PLC-gamma pathways [3]. Dysregulation of PDGFR signaling—through activating mutations, gene fusions, or overexpression—is a primary driver in various malignancies, including gastrointestinal stromal tumors (GIST) and certain leukemias, as well as fibrotic diseases like idiopathic pulmonary fibrosis [4]. Consequently, the PDGFR family is a major target for small-molecule tyrosine kinase inhibitors (TKIs) like imatinib and sunitinib, which compete for the ATP-binding site to halt oncogenic signaling [5]. Clinical management often involves monitoring specific genetic alterations, such as PDGFRA mutations, to predict drug sensitivity and overcome therapeutic resistance [1][4]. Sources: [1] UniProt (P16234, P09619) [2] StatPearls: Tyrosine Kinase Inhibitors (2023) [3] PubMed: PDGFR signaling in cancer and fibrosis (PMC4523515) [4] National Cancer Institute (NCI) Drug Dictionary [5] DrugBank Online: PDGFR inhibitors

Other names

CD140Platelet-derived growth factor receptor alpha (PDGFRA)Platelet-derived growth factor receptor beta (PDGFRB)Type III receptor tyrosine kinasePDGF receptor

Competitive inhibition of the ATP-binding site within the intracellular tyrosine kinase domain; Monoclonal antibody-mediated blockade of ligand binding and receptor dimerization.