| pubmed-article:15601837 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C1801960 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0001455 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:15601837 | lifeskim:mentions | umls-concept:C0173022 | lld:lifeskim |
| pubmed-article:15601837 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15601837 | pubmed:dateCreated | 2004-12-16 | lld:pubmed |
| pubmed-article:15601837 | pubmed:abstractText | Cyclic AMP (cAMP) is a well-known intracellular signaling molecule improving barrier function in vascular endothelial cells. Here, we delineate a novel cAMP-triggered signal that regulates the barrier function. We found that cAMP-elevating reagents, prostacyclin and forskolin, decreased cell permeability and enhanced vascular endothelial (VE) cadherin-dependent cell adhesion. Although the decreased permeability and the increased VE-cadherin-mediated adhesion by prostacyclin and forskolin were insensitive to a specific inhibitor for cAMP-dependent protein kinase, these effects were mimicked by 8-(4-chlorophenylthio)-2'-O-methyladenosine-3', 5'-cyclic monophosphate, a specific activator for Epac, which is a novel cAMP-dependent guanine nucleotide exchange factor for Rap1. Thus, we investigated the effect of Rap1 on permeability and the VE-cadherin-mediated cell adhesion by expressing either constitutive active Rap1 or Rap1GAPII. Activation of Rap1 resulted in a decrease in permeability and enhancement of VE-cadherin-dependent cell adhesion, whereas inactivation of Rap1 had the counter effect. Furthermore, prostacyclin and forskolin induced cortical actin rearrangement in a Rap1-dependent manner. In conclusion, cAMP-Epac-Rap1 signaling promotes decreased cell permeability by enhancing VE-cadherin-mediated adhesion lined by the rearranged cortical actin. | lld:pubmed |
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| pubmed-article:15601837 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15601837 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15601837 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15601837 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15601837 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15601837 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:KangawaKenjiK | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:FukuharaShige... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:SaitoYoshihik... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:MochizukiNaok... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:TakakuraNobuy... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:SanoHidetoH | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:YamagishiAkik... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:SakuraiAtsuko... | lld:pubmed |
| pubmed-article:15601837 | pubmed:author | pubmed-author:SomekawaSatos... | lld:pubmed |
| pubmed-article:15601837 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15601837 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:15601837 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15601837 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15601837 | pubmed:pagination | 136-46 | lld:pubmed |
| pubmed-article:15601837 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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