Vascular endothelial growth factor receptor 2; Integrin (VEGFR2 (also KDR/Flk-1); Integrin (multiple subunits, e.g., αvβ3, α4β1))

Vascular endothelial growth factor receptor 2 (VEGFR2) is a receptor tyrosine kinase predominantly expressed on endothelial cells, where it mediates the main pro-angiogenic effects of VEGF, including endothelial proliferation, migration, and vascular permeability[6]. Integrins are a large family of cell surface heterodimeric adhesion receptors (e.g., αvββ3, α4β1) that mediate cell adhesion to the extracellular matrix and also regulate migration, survival, and signal transduction[4][8]. A well-established molecular cross-talk exists between VEGFR2 and specific integrins (notably αvβ3 and α4β1) in both normal and pathological angiogenesis and certain cancers: integrins promote and stabilize VEGFR2 signaling, and conversely, VEGFR2 activation modulates integrin function and surface localization[1][2][3][7]. Both are validated therapeutic targets, often co-expressed in tumors or diseased tissues, with several inhibitors of VEGFR2 and integrin modulators approved or in development for cancer, ophthalmology, and inflammatory diseases[5]. Note: "VEGFR2 and Integrins" is not a single canonical molecular entity, but a shorthand for two interactive but separate target classes. For structured data, it is advisable to capture "Vascular endothelial growth factor receptor 2" and each integrin heterodimer (e.g., "Integrin αvβ3," "Integrin α4β1") as distinct targets.

Other names

KDR (kinase insert domain receptor)Flk-1αvβ3 integrinα4β1 integrinvitronectin receptorVLA-4

VEGFR2: Inhibition of receptor tyrosine kinase activity blocks VEGF-driven angiogenesis and vascular permeability. Integrins: Antagonists block ligand binding or downstream signaling, disrupting cell adhesion, migration, and survival signals.