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dc.contributor.author조인호-
dc.contributor.author서정원-
dc.date.accessioned2016-08-28T12:08:45Z-
dc.date.available2016-08-28T12:08:45Z-
dc.date.issued2010-
dc.identifier.issn0194-911X-
dc.identifier.otherOAK-6227-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/220491-
dc.description.abstractNitric oxide (NO) production in endothelial cells (EC) is regulated by multisite phosphorylation of specific serine and threonine residues in endothelial NO synthase (eNOS). Among these, eNOS-Ser116 is phosphorylated in the basal state, and its phosphorylation contributes to basal NO production. Here, we investigated the mechanism by which eNOS-Ser116 is phosphorylated during the basal state using bovine aortic EC. Although a previous study suggested that protein kinase C was involved in eNOS-Ser116 phosphorylation, overexpression of various protein kinase C isoforms did not affect eNOS-Ser116 phosphorylation. An in silico analysis using a motif scan revealed that the eNOS-Ser116 residue might be a substrate for proline-directed protein kinases. Roscovitine, a specific inhibitor of cyclin-dependent kinase (CDK), 1, 2, and 5, but not an inhibitor of mitogen-activated protein kinase kinase or glycogen synthase kinase 3β, inhibited eNOS-Ser116 phosphorylation dose dependently. Furthermore, purified CDK1, 2, or 5 directly phosphorylated eNOS-Ser116 in vitro. Ectopic expression of the dominant-negative CDK5 but not dominant-negative CDK1 or dominant-negative CDK2 repressed eNOS-Ser116 phosphorylation and increased NO production. In addition, CDK5 activity was detected in bovine aortic EC, and coimmunoprecipitation and confocal microscopy studies revealed a colocalization of eNOS and CDK5. Cotransfection of CDK5 and p25, the specific CDK5 activator, increased eNOS-Ser116 phosphorylation and decreased NO production, but its parent molecule, p35, and p39, another activator, were not detected in bovine aortic EC, which suggests the existence of a novel CDK5 activator. Overall, this is the first study to find that CDK5 is a physiological kinase responsible for eNOS-Ser116 phosphorylation and regulation of NO production. © 2010 American Heart Association. All rights reserved.-
dc.languageEnglish-
dc.titleCyclin-dependent kinase 5 phosphorylates endothelial nitric oxide synthase at serine 116-
dc.typeArticle-
dc.relation.issue2-
dc.relation.volume55-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage345-
dc.relation.lastpage352-
dc.relation.journaltitleHypertension-
dc.identifier.doi10.1161/HYPERTENSIONAHA.109.140210-
dc.identifier.wosidWOS:000273802500028-
dc.identifier.scopusid2-s2.0-74949143633-
dc.author.googleCho D.-H.-
dc.author.googleSeo J.-
dc.author.googlePark J.-H.-
dc.author.googleJo C.-
dc.author.googleChoi Y.J.-
dc.author.googleSoh J.-W.-
dc.author.googleJo I.-
dc.contributor.scopusid조인호(26643129000)-
dc.date.modifydate20200911081002-
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의과대학 > 의학과 > Journal papers
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