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Published online March 16, 2007
Diabetes 56:1608-1614, 2007
DOI: 10.2337/db06-1398
© 2007 by the American Diabetes Association
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Resistance Exercise and Insulin Regulate AS160 and Interaction With 14-3-3 in Human Skeletal Muscle

Kirsten F. Howlett1, Kei Sakamoto2, Andrew Garnham1, David Cameron-Smith1, and Mark Hargreaves3

1 School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria, Australia
2 Medical Research Council (MRC) Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dundee, Scotland, United Kingdom
3 Department of Physiology, The University of Melbourne, Parkville, Australia

Address correspondence and reprint requests to Kirsten Howlett, School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria, 3125, Australia. E-mail: kirsten.howlett{at}deakin.edu.au

Abbreviations: ACC, acetyl Co–carboxylase; AMPK, AMP-activated protein kinase; AS160, Akt substrate of 160 kDa; DIG, digoxigenin; FFA, free fatty acid; GAP, GTPase-activating protein; GSV, GLUT4 storage vesicle; IRS-1, insulin receptor substrate-1; TBST, Tris-buffered saline with Tween; TNF-{alpha}, tumor necrosis factor-{alpha}

A single bout of aerobic exercise can enhance insulin action, but whether a similar effect occurs after resistance exercise is unknown. Hyperinsulinemic-euglycemic clamps were performed on eight male subjects at rest and after a single bout and three repeated bouts of resistance exercise over 7 days. Skeletal muscle biopsies were taken before and after the clamp and immediately after a single exercise bout. Whole-body insulin action measured by glucose infusion rate decreased (P < 0.05) after a single exercise bout, whereas in response to repeated bouts of resistance exercise, the glucose infusion rate was similar to the rest trial. In skeletal muscle, Akt substrate of 160 kDa (AS160) phosphorylation, an Akt substrate implicated in the regulation of GLUT4 translocation, and its interaction with 14-3-3 was decreased (P < 0.05) only after a single exercise bout. Insulin increased (P < 0.05) phosphorylation of AS160 and its interaction with 14-3-3, but the insulin response was not influenced by resistance exercise. Phosphorylation of insulin receptor substrate-1 and Akt were similar to changes in AS160 phosphorylation after exercise and/or insulin. In conclusion, a single bout of resistance exercise impairs whole-body insulin action. Regulation of AS160 and interaction with 14-3-3 in skeletal muscle are influenced by resistance exercise and insulin but do not fully explain the effect of resistance exercise on whole-body insulin action.


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