The role of VEGF receptors in angiogenesis; complex partnerships
Identifieur interne : 001D41 ( Pmc/Curation ); précédent : 001D40; suivant : 001D42The role of VEGF receptors in angiogenesis; complex partnerships
Auteurs : S. Cébe-Suarez [Suisse] ; A. Zehnder-Fj Llman [Suisse] ; K. Ballmer-Hofer [Suisse]Source :
- Cellular and Molecular Life Sciences [ 1420-682X ] ; 2006.
Abstract
Vascular endothelial growth factors (VEGFs) regulate blood and lymphatic vessel development and homeostasis but also have profound effects on neural cells. VEGFs are predominantly produced by endothelial, hematopoietic and stromal cells in response to hypoxia and upon stimulation with growth factors such as transforming growth factors, interleukins or platelet-derived growth factor. VEGFs bind to three variants of type III receptor tyrosine kinases, VEGF receptor 1, 2 and 3. Each VEGF isoform binds to a particular subset of these receptors giving rise to the formation of receptor homo- and heterodimers that activate discrete signaling pathways. Signal specificity of VEGF receptors is further modulated upon recruitment of coreceptors, such as neuropilins, heparan sulfate, integrins or cadherins. Here we summarize the knowledge accumulated since the discovery of these proteins more than 20 years ago with the emphasis on the signaling pathways activated by VEGF receptors in endothelial cells during cell migration, growth and differentiation.
Url:
DOI: 10.1007/s00018-005-5426-3
PubMed: 16465447
PubMed Central: 2773843
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<front><div type="abstract" xml:lang="en"><title>Abstract.</title>
<p>Vascular endothelial growth factors (VEGFs) regulate blood and lymphatic vessel development and homeostasis but also have profound effects on neural cells. VEGFs are predominantly produced by endothelial, hematopoietic and stromal cells in response to hypoxia and upon stimulation with growth factors such as transforming growth factors, interleukins or platelet-derived growth factor. VEGFs bind to three variants of type III receptor tyrosine kinases, VEGF receptor 1, 2 and 3. Each VEGF isoform binds to a particular subset of these receptors giving rise to the formation of receptor homo- and heterodimers that activate discrete signaling pathways. Signal specificity of VEGF receptors is further modulated upon recruitment of coreceptors, such as neuropilins, heparan sulfate, integrins or cadherins. Here we summarize the knowledge accumulated since the discovery of these proteins more than 20 years ago with the emphasis on the signaling pathways activated by VEGF receptors in endothelial cells during cell migration, growth and differentiation.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Cell Mol Life Sci</journal-id>
<journal-title>Cellular and Molecular Life Sciences </journal-title>
<issn pub-type="ppub">1420-682X</issn>
<issn pub-type="epub">1420-9071</issn>
<publisher><publisher-name>Birkhäuser-Verlag</publisher-name>
<publisher-loc>Basel</publisher-loc>
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</journal-meta>
<article-meta><article-id pub-id-type="pmid">16465447</article-id>
<article-id pub-id-type="pmc">2773843</article-id>
<article-id pub-id-type="publisher-id">5426</article-id>
<article-id pub-id-type="doi">10.1007/s00018-005-5426-3</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Review</subject>
</subj-group>
</article-categories>
<title-group><article-title>The role of VEGF receptors in angiogenesis; complex partnerships</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name name-style="western"><surname>Cébe-Suarez</surname>
<given-names>S.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name name-style="western"><surname>Zehnder-Fjällman</surname>
<given-names>A.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name name-style="western"><surname>Ballmer-Hofer</surname>
<given-names>K.</given-names>
</name>
<address><email>kurt.ballmer@psi.ch</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1">Biomolecular Research, Molecular Cell Biology, Paul Scherrer Institut, 5232 Villigen, Switzerland</aff>
</contrib-group>
<pub-date pub-type="epub"><day>7</day>
<month>2</month>
<year>2006</year>
</pub-date>
<pub-date pub-type="ppub"><month>3</month>
<year>2006</year>
</pub-date>
<volume>63</volume>
<issue>5</issue>
<fpage>601</fpage>
<lpage>615</lpage>
<permissions><copyright-statement>© Birkhäuser Verlag, Basel 2006</copyright-statement>
</permissions>
<abstract xml:lang="EN"><title>Abstract.</title>
<p>Vascular endothelial growth factors (VEGFs) regulate blood and lymphatic vessel development and homeostasis but also have profound effects on neural cells. VEGFs are predominantly produced by endothelial, hematopoietic and stromal cells in response to hypoxia and upon stimulation with growth factors such as transforming growth factors, interleukins or platelet-derived growth factor. VEGFs bind to three variants of type III receptor tyrosine kinases, VEGF receptor 1, 2 and 3. Each VEGF isoform binds to a particular subset of these receptors giving rise to the formation of receptor homo- and heterodimers that activate discrete signaling pathways. Signal specificity of VEGF receptors is further modulated upon recruitment of coreceptors, such as neuropilins, heparan sulfate, integrins or cadherins. Here we summarize the knowledge accumulated since the discovery of these proteins more than 20 years ago with the emphasis on the signaling pathways activated by VEGF receptors in endothelial cells during cell migration, growth and differentiation.</p>
</abstract>
<kwd-group><title>Key words.</title>
<kwd>Angiogenesis</kwd>
<kwd>vascular endothelial growth factor</kwd>
<kwd>VEGF</kwd>
<kwd>neuropilin</kwd>
<kwd>signaling</kwd>
<kwd>endothelial cell</kwd>
<kwd>integrin</kwd>
<kwd>tyrosine kinase receptor</kwd>
</kwd-group>
<custom-meta-wrap><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© Birkhäuser Verlag, Basel 2006</meta-value>
</custom-meta>
</custom-meta-wrap>
</article-meta>
</front>
</pmc>
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