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redox regulation of the amp-activated protein kinase氧化还原活化蛋白激酶的调节
Redox Regulation of the AMP-Activated Protein Kinase
1,2 1 1 2 1
Yingying Han , Qilong Wang , Ping Song , Yi Zhu , Ming-Hui Zou *
1 Department of Biochemistry and Department of Medicine, University of Oklahoma Health Science Center, Oklahoma City, Oklahoma, United States of America,
2 Department of Physiology and Pathophysiology, Peking University Health Science Center, Beijing, China
Abstract
Redox state is a critical determinant of cell function, and any major imbalances can cause severe damage or death.
Objectives: The aim of this study is to determine if AMP-activated protein kinase (AMPK), a cellular energy sensor, is
activated by oxidants generated by Berberine in endothelial cells (EC).
Methods: Bovine aortic endothelial cells (BAEC) were exposed to Berberine. AMPK activity and reactive oxygen species were
monitored after the incubation.
Results: In BAEC, Berberine caused a dose- and time-dependent increase in the phosphorylation of AMPK at Thr172 and
acetyl CoA carboxylase (ACC) at Ser79, a well characterized downstream target of AMPK. Concomitantly, Berberine increased
peroxynitrite, a potent oxidant formed by simultaneous generation of superoxide and nitric oxide. Pre-incubation of BAEC
with anti-oxidants markedly attenuated Berberine-enhanced phosphorylation of both AMPK and ACC. Consistently,
adenoviral expression of superoxide dismutase and pretreatment of L-NG-Nitroarginine methyl ester (L-NAME; a non-
selective NOS inhibitor) blunted Berberine-induced phosphorylation of AMPK. Furthermore, mitochondria-targeted tempol
(mito-tempol) pretreatment or expression of uncoupling protein attenuated AMPK activation caused by Berber
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