| pubmed-article:15662029 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15662029 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:15662029 | lifeskim:mentions | umls-concept:C0001675 | lld:lifeskim |
| pubmed-article:15662029 | lifeskim:mentions | umls-concept:C0302600 | lld:lifeskim |
| pubmed-article:15662029 | lifeskim:mentions | umls-concept:C1801960 | lld:lifeskim |
| pubmed-article:15662029 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:15662029 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15662029 | pubmed:dateCreated | 2005-2-18 | lld:pubmed |
| pubmed-article:15662029 | pubmed:abstractText | Vascular endothelial-cadherin (VE-cadherin) plays a key role in angiogenesis and in vascular permeability. The regulation of its biological activity may be a central mechanism in normal or pathological angiogenesis. VE-cadherin has been shown to be phosphorylated on tyrosine in vitro under various conditions, including stimulation by VEGF. In the present study, we addressed the question of the existence of a tyrosine phosphorylated form of VE-cadherin in vivo, in correlation with the quiescent versus angiogenic state of adult tissues. Phosphorylated VE-cadherin was detected in mouse lung, uterus, and ovary but not in other tissues unless mice were injected with peroxovanadate to block protein phosphatases. Remarkably, VE-cadherin tyrosine phosphorylation was dramatically increased in uterus and ovary, and not in other organs, during PMSG/hCG-induced angiogenesis. In parallel, we observed an increased association of VE-cadherin with Flk1 (VEGF receptor 2) during hormonal angiogenesis. Additionally, Src kinase was constitutively associated with VE-cadherin in both quiescent and angiogenic tissues and increased phosphorylation of VE-cadherin-associated Src was detected in uterus and ovary after hormonal treatment. Src-VE-cadherin association was detected in cultured endothelial cells, independent of VE-cadherin phosphorylation state and Src activation level. In this model, Src inhibition impaired VEGF-induced VE-cadherin phosphorylation, indicating that VE-cadherin phosphorylation was dependent on Src activation. We conclude that VE-cadherin is a substrate for tyrosine kinases in vivo and that its phosphorylation, together with that of associated Src, is increased by angiogenic stimulation. Physical association between Flk1, Src, and VE-cadherin may thus provide an efficient mechanism for amplification and perpetuation of VEGF-stimulated angiogenic processes. | lld:pubmed |
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| pubmed-article:15662029 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15662029 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15662029 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15662029 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15662029 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15662029 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15662029 | pubmed:issn | 1524-4571 | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:Gulino-Debrac... | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:CandFrancineF | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:VilgrainIsabe... | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:LambengNathal... | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:RamponChristi... | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:HuberPhilippe... | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:WallezYannY | lld:pubmed |
| pubmed-article:15662029 | pubmed:author | pubmed-author:ChristéGeorge... | lld:pubmed |
| pubmed-article:15662029 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15662029 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:15662029 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:15662029 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15662029 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15662029 | pubmed:pagination | 384-91 | lld:pubmed |
| pubmed-article:15662029 | pubmed:dateRevised | 2011-10-31 | lld:pubmed |
