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C-Jun N-terminal kinase 2 phosphorylates endothelial nitric oxide synthase at serine 116 and regulates nitric oxide production

Title
C-Jun N-terminal kinase 2 phosphorylates endothelial nitric oxide synthase at serine 116 and regulates nitric oxide production
Authors
Park J.-H.Park M.Byun C.J.Jo I.
Ewha Authors
조인호박정현
SCOPUS Author ID
조인호scopus
Issue Date
2012
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 417, no. 1, pp. 340 - 345
Indexed
SCI; SCIE; SCOPUS WOS scopus
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.
DOI
10.1016/j.bbrc.2011.11.112
Appears in Collections:
의과대학 > 의학과 > Journal papers
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