| Description | Vascular endothelial growth factor (VEGF) is a potent and specific endothelial cell mitogen that regulates blood and lymphatic vessel development and homeostasis [ , ]. EGFs are predominantly produced by endothelial, hematopoietic, and stromal cells in response to hypoxia and upon stimulation by growth factors such as transforming growth factor beta (TGFbeta), interleukins, or platelet-derived growth factors []. VEGFs specifically interact with one or several receptor tyrosine kinases, VEGF receptors, and with distinct co-receptors such as neuropilins or heparan sulphate glycosaminoglycans. The VEGF receptor family consists of three members, VEGFR1 (FLT1), VEGFR2 (KDR/FLK1) and VEGFR3 (FLT4) []. Among these receptors, VEGFR1 binds strongest to VEGF, VEGF2 binds more weakly, and VEGFR3 shows essentially no binding, although it does bind to other members of the VEGF family. VEGF receptors have a characteristic structure, with 7 Ig-like domains in the extracellular domain and a cytoplasmic tyrosine kinase domain with a long kinase insert region. VEGF receptors are activated upon ligand-mediated dimerisation.This entry represents VEGFR2 proteins. The tyrosine kinase domain of VEGFR2 tranduces signals for endothelial cells with a greater efficacy than VEGFR1. VEGFR2 expression in adult endothelial cells appears to account for most of the mitogenic and chemotactic effects of VEGF [ ]. At the post-receptor level, activation of endothelial cells by VEGF leads to the autophosphorylation of VEGFR2 and the subsequent tyrosine phosphorylation of numerous downstream targets. | Name | Vascular endothelial growth factor receptor 2 (VEGFR2) |
| Short Name | VEGFR2_rcpt | Type | Family |
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