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Am J Physiol Endocrinol Metab (June 27, 2006). doi:10.1152/ajpendo.00204.2006
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Submitted on April 27, 2006
Accepted on June 15, 2006

Role of Akt2 in Contraction-Stimulated Cell Signaling and Glucose Uptake in Skeletal Muscle

Kei Sakamoto1, David E Arnolds1, Nobuharu Fujii1, Henning F Kramer1, Michael F Hirshman1, and Laurie J. Goodyear2*

1 Boston, Massachusetts, United States; Joslin Diabetes Center, Metabolism Section, Harvard Medical School, One Joslin Place, Boston, Massachusetts, 02215, United States
2 Joslin Diabetes Center, Metabolism Section, Harvard Medical School, Boston, Massachusetts, United States

* To whom correspondence should be addressed. E-mail: laurie.goodyear{at}joslin.harvard.edu.

The serine/threonine kinase Akt/PKB plays diverse roles in cells, and genetic studies have indicated distinct roles for the three Akt isoforms expressed in mammalian cells and tissues. Akt2 is a key signaling intermediate for insulin-stimulated glucose uptake and glycogen synthesis in skeletal muscle. Akt2 has also been shown to be activated by exercise and muscle contraction in both rodents and humans. In this study, we used Akt2 knockout mice to explore the role of Akt2 in exercise-stimulated glucose uptake and glycogen synthesis, as well as intracellular signaling pathways that regulate glycogen metabolism in skeletal muscle. We found that Akt2 deficiency does not affect basal or exercise-stimulated glucose uptake or intracellular glycogen content in the soleus muscle. In addition, lack of Akt2 did not result in alterations in basal Akt Thr 308 or basal and contraction-stimulated GSK-3{alpha} Ser9 phosphorylation, glycogen synthase phosphorylation, or glycogen synthase activity. In contrast, in-situ contraction failed to elicit normal increases in Akt T-loop Thr308 phosphorylation and GSK-3{alpha} Ser21 phosphorylation in tibialis anterior muscles from Akt2 deficient animals. Our data establishes a key role for Akt2 in the regulation of GSK-3{alpha}Ser21 phosphorylation with contraction, and adds genetic evidence to support the separation of the intracellular pathways regulated by insulin and exercise that converge on glucose uptake and glycogen synthesis in skeletal muscle.




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