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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-8-18
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pubmed:abstractText |
Vascular endothelial growth factor (VEGF) stimulates endothelial cell (EC) migration. The protein kinase Akt activates the endothelial NO synthase (eNOS) by phosphorylation of Ser-1177. Therefore, we investigated the contribution of Akt-mediated eNOS phosphorylation to VEGF-induced EC migration. Inhibition of NO synthase or overexpression of a dominant negative Akt abrogated VEGF-induced cell migration. In contrast, overexpression of constitutively active Akt was sufficient to induce cell migration. Moreover, transfection of an Akt site phospho-mimetic eNOS (S1177D) potently stimulated EC migration, whereas a non-phosphorylatable mutant (S1177A) inhibited VEGF-induced EC migration. Our data indicate that eNOS activation via phosphorylation of Ser-1177 by Akt is necessary and sufficient for VEGF-mediated EC migration.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
477
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
258-62
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10908731-Cell Line,
pubmed-meshheading:10908731-Endothelial Growth Factors,
pubmed-meshheading:10908731-Endothelium, Vascular,
pubmed-meshheading:10908731-Humans,
pubmed-meshheading:10908731-Lymphokines,
pubmed-meshheading:10908731-Nitric Oxide Synthase,
pubmed-meshheading:10908731-Nitric Oxide Synthase Type III,
pubmed-meshheading:10908731-Phosphorylation,
pubmed-meshheading:10908731-Serine,
pubmed-meshheading:10908731-Transfection,
pubmed-meshheading:10908731-Vascular Endothelial Growth Factor A,
pubmed-meshheading:10908731-Vascular Endothelial Growth Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Phosphorylation of the endothelial nitric oxide synthase at ser-1177 is required for VEGF-induced endothelial cell migration.
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pubmed:affiliation |
Molecular Cardiology, Department of Internal Medicine IV, University of Frankfurt, Theodor-Stern-Kai 7, 60590, Frankfurt, Germany. dimmeler@em.uni-frankfurt.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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