Vascular endothelial growth factor receptor 1; Vascular endothelial growth factor receptor 2; Vascular endothelial growth factor receptor 3 (VEGFR-1; VEGFR-2; VEGFR-3)

Vascular endothelial growth factor receptors (VEGFR-1, VEGFR-2, and VEGFR-3) are receptor tyrosine kinases that mediate the effects of various VEGF family ligands in the regulation of angiogenesis, vasculogenesis, and lymphangiogenesis. They are single-pass transmembrane glycoproteins characterized by an extracellular region with seven immunoglobulin-like domains and an intracellular split kinase domain. These receptors play major roles in both healthy and pathological processes including embryonic development, tissue repair, tumor formation, cancer metastasis, and lymphatic function[1][2][3][4][5][6][7]. They are highly validated targets for anti-angiogenic and anti-lymphangiogenic therapy in cancer and other diseases, and several approved drugs inhibit their signaling clinically. Drugs targeting these receptors primarily inhibit their tyrosine kinase activity or interfere with ligand-receptor interactions, leading to reduced pathological blood and lymph vessel growth[5][6][7]. Safety concerns are linked to their role in physiological vascular maintenance, leading to effects such as hypertension and impaired wound healing when chronically inhibited[5][6].

Other names

VEGFR-1: FMS-like tyrosine kinase 1 (Flt-1)VEGFR-2: Kinase insert domain receptor (KDR) / Fetal liver kinase-1 (Flk-1)VEGFR-3: Fms-related tyrosine kinase 4 (Flt-4)

Inhibition of receptor tyrosine kinase activity, blocking downstream angiogenic signalling Prevention of ligand binding (e.g., by monoclonal antibodies) Ligand sequestration (decoy activity, especially VEGFR-1)