Is VEGF a hormone?

Is VEGF a hormone?

The induction of vascular endothelial growth factor (VEGF) expression by 17beta-estradiol (E(2)) in many target cells, including epithelial cells, fibroblasts and smooth muscle cells, suggests a role for this hormone in the modulation of angiogenesis and vascular permeability.

Is VEGF a dimer?

VEGF is a member of the cysteine knot family of growth factors and is secreted as a dimer in which the monomers are linked together by two intersubunit disulfide bridges [6,7] (Figure 1A).

What is the role of VEGF?

Vascular endothelial growth factor (VEGF) is a potent and specific angiogenic factor. Originally identified for its ability to induce vascular permeability and stimulate endothelial cell growth, VEGF is now known to be a key requirement for tumor growth.

What type of receptor does VEGF have?

VEGF receptors are classified as type V RTKs whose extracellular domains consists of seven immunoglobulin-like (Ig-like) domains. VEGF receptors are activated upon ligand-mediated dimerization.

What is the structure of the VEGF monomer?

The overall structure of the VEGF monomer is similar to that of other cystine knot proteins,,,. It consists of a central antiparallel four-stranded β sheet with the characteristic cystine knot at one end (Figure 1).

How is the crystal structure of VEGF determined?

Results: We have determined the crystal structure of the receptor-binding domain of VEGF at 1.93 Å resolution in a triclinic space group containing eight monomers in the asymmetric unit.

How does the vascular endothelial growth factor A ( VEGFA ) work?

As embryonic tissue utilizes more oxygen than it receives from diffusion, it becomes hypoxic. These cells will secrete the signaling molecule vascular endothelial factor A (VEGFA) which will recruit the angioblasts expressing its partnering receptor to the site of future angiogenesis.

What is the crystal structure of VEGF receptor binding domain?

The crystal structure of the receptor-binding domain of VEGF shows that it is a member of the cystine knot growth factor superfamily. A comprehensive mutagenesis analysis has revealed that the residues important for KDR binding map in two patches on the same face of the molecule, spanning across the dimer interface.