Journal of Applied Physiology AJP: Renal Physiology
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J Appl Physiol 102: 1624-1631, 2007. First published December 21, 2006; doi:10.1152/japplphysiol.00821.2006
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Increased insulin-stimulated Akt pSer473 and cytosolic SHP2 protein abundance in human skeletal muscle following acute exercise and short-term training

Glenn D. Wadley,1,2 Nicky Konstantopoulos,3,4 Lance Macaulay,3 Kirsten F. Howlett,1 Andrew Garnham,1 Mark Hargreaves,2 and David Cameron-Smith1

1School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria; 2Department of Physiology, The University of Melbourne, Parkville, Victoria; 3Commonwealth Scientific and Industrial Research Organisation Molecular and Health Technologies, Parkville, Victoria; and 4Metabolic Research Unit, Deakin University, Geelong, Victoria, Australia

Submitted 26 July 2006 ; accepted in final form 16 December 2006

The purpose of the present study was to determine in human skeletal muscle whether a single exercise bout and 7 days of consecutive endurance (cycling) training 1) increased insulin-stimulated Akt pSer473 and 2) altered the abundance of the protein tyrosine phosphatases (PTPases), PTP1B and SHP2. In healthy, untrained men (n = 8; 24 ± 1 yr), glucose infusion rate during a hyperinsulinemic euglycemic clamp, when compared with untrained values, was not improved 24 h following a single 60-min bout of endurance cycling but was significantly increased (~30%; P < 0.05) 24 h following completion of 7 days of exercise training. Insulin-stimulated Akt pSer473 was ~50% higher (P < 0.05) 24 h following the acute bout of exercise, with this effect remaining after 7 days of training (P < 0.05). Insulin-stimulated insulin receptor and insulin receptor substrate-1 tyrosine phosphorylation were not altered 24 h after acute exercise and short-term training. Insulin did not acutely regulate the localization of the PTPases, PTP1B or SHP2, although cytosolic protein abundance of SHP2 was increased (P < 0.05; main effect) 24 h following acute exercise and short-term training. In conclusion, insulin-sensitive Akt pSer473 and cytosolic SHP2 protein abundance are higher after acute exercise and short-term training, and this effect appears largely due to the residual effects of the last bout of prior exercise. The significance of exercise-induced alterations in cytosolic SHP2 and insulin-stimulated Akt pSer473 on the improvement in insulin sensitivity requires further elucidation.

contraction; insulin-signaling; protein phosphatases



Address for reprint requests and other correspondence: G. Wadley, Dept. of Physiology, The Univ. of Melbourne, Parkville, 3010, Australia (e-mail: gdwadley{at}unimelb.edu.au)




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