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j.1748-1716.2010.02169.x.pdf | 602.31 kB | Adobe PDF | 見る/開く |
タイトル: | Caffeine activates preferentially α1-isoform of 5'AMP-activated protein kinase in rat skeletal muscle. |
著者: | Egawa, T https://orcid.org/0000-0001-9363-1589 (unconfirmed) Hamada, T Ma, X Karaike, K Kameda, N Masuda, S Iwanaka, N Hayashi, T |
著者名の別形: | 江川, 達郎 林, 達也 |
キーワード: | acetyl-CoA carboxylase Ca(2+)/calmodulin-dependent protein kinase glucose transport glycogen phosphocreatine |
発行日: | 18-Jul-2010 |
出版者: | wiley |
誌名: | Acta physiologica |
巻: | 201 |
号: | 2 |
開始ページ: | 227 |
終了ページ: | 238 |
抄録: | [Aim]: Caffeine activates 5′AMP-activated protein kinase (AMPK), a signalling intermediary implicated in the regulation of glucose, lipid and energy metabolism in skeletal muscle. Skeletal muscle expresses two catalytic α subunits of AMPK, α1 and α2, but the isoform specificity of caffeine-induced AMPK activation is unclear. The aim of this study was to determine which α isoform is preferentially activated by caffeine in vitroand in vivo using rat skeletal muscle. [Methods]: Rat epitrochlearis muscle was isolated and incubated in vitro in the absence or presence of caffeine. In another experiment, the muscle was dissected after intravenous injection of caffeine. Isoform-specific AMPK activity, the phosphorylation status of AMPKα Thr172 and acetyl-CoA carboxylase (ACC) Ser79, the concentrations of ATP, phosphocreatine (PCr) and glycogen, and 3-O-methyl-D-glucose (3MG) transport activity were estimated. [Results]: Incubation of isolated epitrochlearis muscle with 1 mM of caffeine for 15 min increased AMPKα1 activity, but not AMPKα2 activity; concentrations of ATP, PCr and glycogen were not affected. Incubation with 3 mM of caffeine activated AMPKα2 and reduced PCr and glycogen concentrations. Incubation with 1 mM of caffeine increased the phosphorylation of AMPK and ACC and enhanced 3MG transport. Intravenous injection of caffeine (5 mg kg−1) predominantly activated AMPKα1 and increased 3MG transport without affecting energy status. [Conclusion]: Our results suggest that of the two α isoforms of AMPK, AMPKα1 is predominantly activated by caffeine via an energy-independent mechanism and that the activation of AMPKα1 increases glucose transport and ACC phosphorylation in skeletal muscle. |
著作権等: | This is the peer reviewed version of the following article: Egawa, T., Hamada, T., Ma, X., Karaike, K., Kameda, N., Masuda, S., Iwanaka, N. and Hayashi, T. (2011), Caffeine activates preferentially α1-isoform of 5′AMP-activated protein kinase in rat skeletal muscle. Acta Physiologica, 201: 227–238, which has been published in final form at http://dx.doi.org/10.1111/j.1748-1716.2010.02169.x This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/197223 |
DOI(出版社版): | 10.1111/j.1748-1716.2010.02169.x |
PubMed ID: | 21241457 |
出現コレクション: | 学術雑誌掲載論文等 |
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