The Korean Journal of Physiology and Pharmacology

  • 제16권3호
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  • Pages.199-204
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  • 2012
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  • 1226-4512(pISSN)
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  • 2093-3827(eISSN)
대한약리학회 (The Korean Society of Pharmacology)
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Tat-Mediated p66shc Transduction Decreased Phosphorylation of Endothelial Nitric Oxide Synthase in Endothelial Cells

  • Lee, Sang-Ki (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Lee, Ji-Young (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Joo, Hee-Kyoung (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Cho, Eun-Jung (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Kim, Cuk-Seong (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Lee, Sang-Do (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Park, Jin-Bong (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University) ;
  • Jeon, Byeong-Hwa (Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University)
  • 투고 : 2012.03.26
  • 심사 : 2012.05.12
  • 발행 : 2012.06.30
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초록

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-${\alpha}$-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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참고문헌

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