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J Appl Physiol 85: 1744-1752, 1998;
8750-7587/98 $5.00
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Vol. 85, Issue 5, 1744-1752, November 1998

Modulation of whole body protein metabolism, during and after exercise, by variation of dietary protein

J. L. Bowtell1, G. P. Leese1, K. Smith1, P. W. Watt1, A. Nevill2, O. Rooyackers3, A. J. M. Wagenmakers3, and M. J. Rennie1

1 Department of Anatomy and Physiology, Small's Wynd, University of Dundee, Dundee, DD1 4HN; 2 Research Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, United Kingdom; and 3 Department of Human Biology, Maastricht University, Maastricht, The Netherlands

The aim of this study was to investigate dietary protein-induced changes in whole body leucine turnover and oxidation and in skeletal muscle branched chain 2-oxo acid dehydrogenase (BCOADH) activity, at rest and during exercise. Postabsorptive subjects received a primed constant infusion of L-[1-13C,15N]leucine for 6 h, after previous consumption of a high- (HP; 1.8 g · kg-1 · day-1, n = 8) or a low-protein diet (LP; 0.7 g · kg-1 · day-1, n = 8) for 7 days. The subjects were studied at rest for 2 h, during 2-h exercise at 60% maximum oxygen consumption, then again for 2 h at rest. Exercise induced a doubling of both leucine oxidation from 20 µmol · kg-1 · h-1 and BCOADH percent activation from 7% in all subjects. Leucine oxidation was greater before (+46%) and during (+40%, P < 0.05) the first hour of exercise in subjects consuming the HP rather than the LP diet, but there was no additional change in muscle BCOADH activity. The results suggest that leucine oxidation was increased by previous ingestion of an HP diet, attributable to an increase in leucine availability rather than to a stimulation of the skeletal muscle BCOADH activity.

branched chain 2-oxo acid dehydrogenase; leucine oxidation; stable isotope


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