Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 조인호 | * |
dc.contributor.author | 박정현 | * |
dc.date.accessioned | 2016-08-28T12:08:51Z | - |
dc.date.available | 2016-08-28T12:08:51Z | - |
dc.date.issued | 2012 | * |
dc.identifier.issn | 0006-291X | * |
dc.identifier.other | OAK-8399 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/222307 | - |
dc.description.abstract | The c-Jun N-terminal kinases (JNKs) belonging to the mitogen-activated protein kinase (MAPK) superfamily play important roles in foam-cell formation, hypercholesterolemia-mediated endothelial dysfunction, and the development of obesity. Although decreased nitric oxide (NO) production via decreased phosphorylation of endothelial NO synthase at serine 1179 (eNOS-Ser 1179) was reported to be partly involved in JNK2-derived endothelial dysfunction, JNK2 seems likely to be indirectly involved in this signaling pathway. Here, using bovine aortic endothelial cells, we examined whether JNK2 directly phosphorylated eNOS-Ser 116, a putative substrate site for the MAPK superfamily, and this phosphorylation resulted in decreased NO release. JNK inhibitor SP60012 increased NO release in a time- and dose-dependent manner, which was accompanied by increased eNOS-Ser 116 phosphorylation. Purified JNK2 directly phosphorylated eNOS-Ser 116 in vitro. Ectopic expression of dominant negative JNK2 repressed eNOS-Ser 116 phosphorylation and increased NO production. Coimmunoprecipitation and confocal microscopy studies revealed a colocalization of eNOS and JNK2. However, all these observed effects were not manifested when JNK1 probes were used. Overall, this study indicates that JNK2 is a physiological kinase responsible for eNOS-Ser 116 phosphorylation and regulates NO production. © 2011 Elsevier Inc. | * |
dc.language | English | * |
dc.title | C-Jun N-terminal kinase 2 phosphorylates endothelial nitric oxide synthase at serine 116 and regulates nitric oxide production | * |
dc.type | Article | * |
dc.relation.issue | 1 | * |
dc.relation.volume | 417 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 340 | * |
dc.relation.lastpage | 345 | * |
dc.relation.journaltitle | Biochemical and Biophysical Research Communications | * |
dc.identifier.doi | 10.1016/j.bbrc.2011.11.112 | * |
dc.identifier.wosid | WOS:000299491600058 | * |
dc.identifier.scopusid | 2-s2.0-84855772893 | * |
dc.author.google | Park J.-H. | * |
dc.author.google | Park M. | * |
dc.author.google | Byun C.J. | * |
dc.author.google | Jo I. | * |
dc.contributor.scopusid | 조인호(26643129000;56663841900) | * |
dc.contributor.scopusid | 박정현(56937220800;57157650200;57157679600) | * |
dc.date.modifydate | 20240123112949 | * |