| pubmed-article:20061392 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C0294209 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C1801960 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C2361980 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C1624612 | lld:lifeskim |
| pubmed-article:20061392 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:20061392 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:20061392 | pubmed:dateCreated | 2010-3-8 | lld:pubmed |
| pubmed-article:20061392 | pubmed:abstractText | In this study, we obtained evidence indicating that annexin 1 is a new target of the p38/MAPKAP kinase-2 pathway and that it regulates endothelial cell migration in response to vascular endothelial growth factor (VEGF). These conclusions are supported by a series of substantiating experiments. First, by two-dimensional gel electrophoresis and mass spectrometry, we identified annexin 1 as a protein whose phosphorylation is induced by VEGF and is impaired by inhibiting p38. Second, using in vitro kinase assays and in vivo phosphorylation assays, we found that VEGF-mediated activation of LIM kinase 1 downstream of the p38 pathway triggers the phosphorylation of annexin 1. Third, VEGF-induced cell migration and tube formation in Matrigel are inhibited following small interfering RNA-mediated knockdown of annexin 1. Fourth, both processes are rescued in cells expressing an annexin 1 construct insensitive to the small interfering RNA knockdown. Finally, the VEGF/annexin 1-mediated cell migration is impaired by inhibiting p38. We therefore conclude that phosphorylation of annexin 1 regulates the angiogenic effect that is associated with the activation of the p38/LIM kinase 1 axis by VEGF. | lld:pubmed |
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| pubmed-article:20061392 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20061392 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20061392 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20061392 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20061392 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20061392 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20061392 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:HuotJacquesJ | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:RousseauSimon... | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:HouleFrançois... | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:PoirierAndrée... | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:CôtéMaxime... | lld:pubmed |
| pubmed-article:20061392 | pubmed:author | pubmed-author:LavoieJessie... | lld:pubmed |
| pubmed-article:20061392 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20061392 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:20061392 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20061392 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20061392 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20061392 | pubmed:pagination | 8013-21 | lld:pubmed |
| pubmed-article:20061392 | pubmed:dateRevised | 2011-7-26 | lld:pubmed |
| pubmed-article:20061392 | pubmed:meshHeading | pubmed-meshheading:20061392... | lld:pubmed |
| pubmed-article:20061392 | pubmed:meshHeading | pubmed-meshheading:20061392... | lld:pubmed |
| pubmed-article:20061392 | pubmed:meshHeading | pubmed-meshheading:20061392... | lld:pubmed |
