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KMID : 0811720120160030199
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Korean Journal of Physiology & Pharmacology
2012 Volume.16 No. 3 p.199 ~ p.204
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Tat-Mediated p66shc Transduction Decreased Phosphorylation of Endothelial Nitric Oxide Synthase in Endothelial Cells
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Lee Sang-Ki
Lee Ji-Young
Joo Hee-Kyoung
Cho Eun-Jung
Kim Cuk-Seong
Lee Sang-Do
Park Jin-Bong
Jeon Byeong-Hwa
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Abstract
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We evaluated the role of Tat-mediated p66shc transduction on the activation of endothelial nitric oxide synthase in cultured mouse endothelial cells. To construct the Tat-p66shc fusion protein, human full length p66shc cDNA was fused with the Tat-protein transduction domain. Transduction of TAT-p66shc showed a concentration- and time-dependent manner in endothelial cells. Tat-mediated p66shc transduction showed increased hydrogen peroxide and superoxide production, compared with Tat-p66shc (S/A), serine 36 residue mutant of p66shc. Tat-mediated p66shc transduction decreased endothelial nitric oxide synthase phosphorylation in endothelial cells. Furthermore, Tat-mediated p66shc transduction augmented TNF-?-induced p38 MAPK phosphorylation in endothelial cells. These results suggest that Tat-mediated p66shc transduction efficiently inhibited endothelial nitric oxide synthase phosphorylation in endothelial cells.
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KEYWORD
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p66shc, Tat-mediated transduction, Endothelial nitric oxide synthase, Superoxide, Endothelial cells
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