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VEGF receptors

fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascular permeability factor receptor)
Symbol FLT1
Alt. Symbols FLT
Entrez 2321
HUGO 3763
OMIM 165070
RefSeq NM_002019
UniProt P17948
Other data
EC number
Locus Chr. 13 q12
kinase insert domain receptor (a type III receptor tyrosine kinase)
Symbol KDR
Alt. Symbols FLK1, VEGFR, VEGFR2, CD309
Entrez 3791
HUGO 6307
OMIM 191306
RefSeq NM_002253
UniProt P35968
Other data
EC number
Locus Chr. 4 q11-q12
fms-related tyrosine kinase 4
Symbol FLT4
Alt. Symbols VEGFR3, PCL
Entrez 2324
HUGO 3767
OMIM 136352
RefSeq NM_002020
UniProt P35916
Other data
EC number
Locus Chr. 5 q34-q35

Receptors for Vascular Endothelial Growth Factor: VEGF.

VEGF biology

Vascular endothelial growth factor (VEGF) is an important signaling protein involved in both vasculogenesis (the formation of the embryonic circulatory system) and angiogenesis (the growth of blood vessels from pre-existing vasculature). As its name implies, VEGF activity is restricted mainly to cells of the vascular endothelium, although it does have effects on a limited number of other cell types (e.g. stimulation monocyte/macrophage migration). In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF also enhances microvascular permeability and is sometimes referred to as vascular permeability factor.

VEGF splice variants are released from cells as glycosylated disulfide-bonded homodimers. Structurally VEGF belongs to the PDGF family of cystine-knot growth factors. Subsequently, several closely-related proteins were discovered (Placenta growth factor (PlGF), VEGF-B, VEGF-C and VEGF-D) which together comprise the VEGF sub-family of growth factors. VEGF is sometimes referred to as VEGF-A to differentiate it from these related growth factors. A number of VEGF-related proteins have also been discovered encoded by viruses (VEGF-E) and in the venom of some snakes (VEGF-F).

Receptor biology

All members of the VEGF family stimulate cellular responses by binding to tyrosine kinase receptors (the VEGFRs) on the cell surface, causing them to dimerize and become activated through transphosphorylation. The VEGF receptors have an extracellular portion consisting of 7 immunoglobulin-like domains, a single transmembrane spanning region and an intracellular portion containing a split tyrosine-kinase domain. VEGF-A binds to VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1). VEGFR-2 appears to mediate almost all of the known cellular responses to VEGF. The function of VEGFR-1 is less well defined, although it is thought to modulate VEGFR-2 signaling. Another function of VEGFR-1 may be to act as a dummy/decoy receptor, sequestering VEGF from VEGFR-2 binding (this appears to be particularly important during vasculogenesis in the embryo). A third receptor has been discovered (VEGFR-3), however, VEGF-A is not a ligand for this receptor. VEGFR-3 mediates lymphangiogenesis in response to VEGF-C and VEGF-D.

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "VEGF_receptors". A list of authors is available in Wikipedia.
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