Document Detail


Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling.
MedLine Citation:
PMID:  19761875     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Vascular endothelial growth factors (VEGFs) constitute a family of six polypeptides, VEGF-A, -B, -C, -D, -E and PlGF, that regulate blood and lymphatic vessel development. VEGFs specifically bind to three type V receptor tyrosine kinases (RTKs), VEGFR-1, -2 and -3, and to coreceptors such as neuropilins and heparan sulfate proteoglycans (HSPG). VEGFRs are activated upon ligand-induced dimerization mediated by the extracellular domain (ECD). A study using receptor constructs carrying artificial dimerization-promoting transmembrane domains (TMDs) showed that receptor dimerization is necessary, but not sufficient, for receptor activation and demonstrates that distinct orientation of receptor monomers is required to instigate transmembrane signaling. Angiogenic signaling by VEGF receptors also depends on cooperation with specific coreceptors such as neuropilins and HSPG. A number of VEGF isoforms differ in binding to coreceptors, and ligand-specific signal output is apparently the result of the specific coreceptor complex assembled by a particular VEGF isoform. Here we discuss the structural features of VEGF family ligands and their receptors in relation to their distinct signal output and angiogenic potential.
Authors:
Felix S Gr?newald; Andrea E Prota; Alexandra Giese; Kurt Ballmer-Hofer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2009-09-15
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1804     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-02-15     Completed Date:  2010-04-06     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  567-80     Citation Subset:  IM    
Copyright Information:
Copyright 2009 Elsevier B.V. All rights reserved.
Affiliation:
Paul Scherrer Institut, Biomolecular Research, 5232 Villigen PSI, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Animals
Heparan Sulfate Proteoglycans / chemistry,  metabolism
Humans
Neovascularization, Physiologic / physiology*
Neuropilins / chemistry,  metabolism
Protein Isoforms / chemistry,  metabolism
Protein Multimerization / physiology*
Protein Structure, Tertiary / physiology
Receptors, Vascular Endothelial Growth Factor / chemistry*,  metabolism*
Signal Transduction / physiology*
Structure-Activity Relationship
Vascular Endothelial Growth Factors / chemistry*,  metabolism*
Chemical
Reg. No./Substance:
0/Heparan Sulfate Proteoglycans; 0/Neuropilins; 0/Protein Isoforms; 0/Vascular Endothelial Growth Factors; EC 2.7.10.1/Receptors, Vascular Endothelial Growth Factor

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