Tat-Mediated p66shc Transduction Decreased Phosphorylation of Endothelial Nitric Oxide Synthase in Endothelial Cells.
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-α-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.
Infection Signaling Network Research Center, Research Institute of Medical Sciences, Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-131, Korea.
Sang Ki
SK
Lee
Ji Young
JY
Lee
Hee Kyoung
HK
Joo
Eun Jung
EJ
Cho
Cuk Seong
CS
Kim
Sang Do
SD
Lee
Jin Bong
JB
Park
Byeong Hwa
BH
Jeon