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J Appl Physiol 105: 1098-1105, 2008. First published July 24, 2008; doi:10.1152/japplphysiol.00847.2007
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Rapid exercise-induced changes in PGC-1{alpha} mRNA and protein in human skeletal muscle

Anila S. Mathai, Arend Bonen, Carley R. Benton, D. L. Robinson, and Terry E. Graham

Department of Human Health and Nutritional Sciences, University of Guelph, Guelph, Ontario, Canada

Submitted 7 August 2007 ; accepted in final form 15 July 2008

The mRNA of the nuclear coactivator peroxisome proliferator-activated receptor-{gamma} coactivator-1{alpha} (PGC-1{alpha}) increases during prolonged exercise and is influenced by carbohydrate availability. It is unknown if the increases in mRNA reflect the PGC-1{alpha} protein or if glycogen stores are an important regulator. Seven male subjects [23 ± 1.3 yr old, maximum oxygen uptake (VO2 max) 48.4 ± 0.8 ml·kg–1·min–1] exercised to exhaustion (~2 h) at 65% VO2 max followed by ingestion of either a high-carbohydrate (HC) or low-carbohydrate (LC) diet (7 or 2.9 g·kg–1·day–1, respectively) for 52 h of recovery. Glycogen remained depressed in LC (P < 0.05) while returning to resting levels by 24 h in HC. PGC-1{alpha} mRNA increased both at exhaustion (3-fold) and 2 h later (6.2-fold) (P < 0.05) but returned to rest levels by 24 h. PGC-1{alpha} protein increased (P < 0.05) 23% at exhaustion and remained elevated for at least 24 h (P < 0.05). While there was no direct treatment effect (HC vs. LC) for PGC-1{alpha} mRNA or protein, there was a linear relationship between the changes in glycogen and those in PGC-1{alpha} protein during exercise and recovery (r = –0.68, P < 0.05). In contrast, PGC-1β did not increase with exercise but rather decreased (P < 0.05) below rest level at 24 and 52 h, and the decrease was greater (P < 0.05) in LC. PGC-1{alpha} protein content increased in prolonged exercise and remained upregulated for 24 h, but this could not have been predicted by the changes in mRNA. The β-isoform declined rather than increasing, and this was greater when glycogen was not resynthesized to rest levels.

carbohydrate; gene expression; glucose; insulin; training signals; metabolism



Address for reprint requests and other correspondence: T. E. Graham, Dept. of Human Health and Nutritional Sciences, Univ. of Guelph, Guelph, ON, Canada N1G 2W1 (e-mail: terrygra{at}uoguelph.ca)







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