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J. Biol. Chem., Vol. 278, Issue 30, 28312-28323, July 25, 2003
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¶ ¶ || **
¶¶
From the
Division of Molecular Genetics,
Institutes for Enzyme Research and Department of
Ophthalmology, Graduate School of Medicine, University of Tokushima, 3-18-15
Kuramoto, Tokushima City, Tokushima 770-8503, Japan, the
Institute of Molecular and Cellular
Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032,
Japan, and the ||Division of Signal Transduction,
Department of Medicine, Beth Israel Deaconess Medical Center, Boston,
Massachusetts 02215
Insulin plays a central role in the regulation of glucose homeostasis in part by stimulating glucose uptake and glycogen synthesis. The serine/threonine protein kinase Akt has been proposed to mediate insulin signaling in several processes. However, it is unclear whether Akt is involved in insulin-stimulated glucose uptake and which isoforms of Akt are responsible for each insulin action. We confirmed that expression of a constitutively active Akt, using an adenoviral expression vector, promoted translocation of glucose transporter 4 (GLUT4) to plasma membrane, 2-deoxyglucose (2-DG) uptake, and glycogen synthesis in both Chinese hamster ovary cells and 3T3-L1 adipocytes. Inhibition of Akt either by adenoviral expression of a dominant negative Akt or by the introduction of synthetic 21-mer short interference RNA against Akt markedly reduced insulin-stimulated GLUT4 translocation, 2-DG uptake, and glycogen synthesis. Experiments with isoform-specific short interference RNA revealed that Akt2, and Akt1 to a lesser extent, has an essential role in insulin-stimulated GLUT4 translocation and 2-DG uptake in both cell lines, whereas Akt1 and Akt2 contribute equally to insulin-stimulated glycogen synthesis. These data suggest a prerequisite role of Akt in insulin-stimulated glucose uptake and distinct functions among Akt isoforms.
Received for publication, February 27, 2003 , and in revised form, April 15, 2003.
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ These authors contributed equally to this work.
** Supported by the Uehara Memorial Foundation and Ministry of Education, Science, Technology, Sports, and Culture of Japan Grant 13680691.
Supported by National Institutes of Health Grant GM41890.
¶¶ Supported by a grant from the Ministry of Education, Science, Technology, Sports, and Culture of Japan. To whom correspondence should be addressed. Tel.: 81-88-633-7436; Fax: 81-88-633-7437; E-mail: ebina{at}ier.tokushima-u.ac.jp.
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