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Am J Physiol Endocrinol Metab (March 16, 2004). doi:10.1152/ajpendo.00487.2003
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Submitted on October 29, 2003
Accepted on March 9, 2004

Possible Involvement of the {alpha}1 Isoform of 5'AMP-Activated Protein Kinase in Oxidative-Stress-Stimulated Glucose Transport in Skeletal Muscle

Taro Toyoda1, Tatsuya Hayashi2*, Licht Miyamoto2, Shin Yonemitsu2, Masako Nakano2, Satsuki Tanaka2, Ken Ebihara2, Hiroaki Masuzaki2, Kiminori Hosoda2, Gen Inoue2, Akira Otaka3, Kenji Sato4, Tohru Fushiki1, and Kazuwa Nakao2

1 Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan
2 Department of Medicine and Clinical Science, Kyoto University Graduate School of Medicine, Kyoto, Japan
3 Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan
4 Department of Food Sciences and Nutritional Health, Kyoto Prefectural University, Kyoto, Japan

* To whom correspondence should be addressed. E-mail: tatsuya{at}kuhp.kyoto-u.ac.jp.

Recent studies have suggested that 5'AMP-activated protein kinase (AMPK) is activated in response to metabolic stresses, such as contraction, hypoxia, and the inhibition of oxidative phosphorylation, which leads to insulin-independent glucose transport in skeletal muscle. In the present study, we hypothesized that acute oxidative stress increases the rate of glucose transport via an AMPK-mediated mechanism. When rat epitrochlearis muscles were isolated and incubated in vitro in Krebs buffer containing the oxidative agent H2O2, AMPK{alpha}1 activity increased in a time- and dose-dependent manner, whereas AMPK{alpha}2 activity remained unchanged. The activation of AMPK{alpha}1 was associated with phosphorylation of AMPK Thr172, suggesting that an upstream kinase is involved in the activation process. H2O2-induced AMPK{alpha}1 activation was blocked in the presence of the antioxidant N-acetyl-L-cysteine (NAC), and H2O2 significantly increased the ratio of glutathione to oxidized glutathione (GSSG:GSH), a sensitive marker of oxidative stress. H2O2 did not cause an increase in the conventional parameters of AMPK activation, such as AMP and AMP:ATP. H2O2 increased 3-O-methyl-D-glucose transport, and this increase was partially, but significantly, blocked in the presence of NAC. Results were similar when the muscles were incubated in a superoxide-generating system using hypoxanthine and xanthine oxidase. Taken together, our data suggest that acute oxidative stress activates AMPK{alpha}1 in skeletal muscle via an AMP-independent mechanism, and leads to an increase in the rate of glucose transport, at least in part via an AMPK{alpha}1-mediated mechanism.




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