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Am J Physiol Regul Integr Comp Physiol 294: R1319-R1328, 2008. First published January 23, 2008; doi:10.1152/ajpregu.00631.2007
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ENVIRONMENTAL, EXERCISE AND RESPIRATORY PHYSIOLOGY

Adaptive responses to creatine loading and exercise in fast-twitch rat skeletal muscle

Maria Gallo,1 Ian MacLean,1 Neil Tyreman,2,3 Karen J. B. Martins,1 Daniel Syrotuik,1 Tessa Gordon,2,3 and Charles T. Putman1,3

1Exercise Biochemistry Laboratory, Faculty of Physical Education and Recreation, and 2Division of Physical Medicine and Rehabilitation and 3Centre for Neuroscience, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

Submitted 31 August 2007 ; accepted in final form 22 January 2008

We investigated the effects of chronic creatine loading and voluntary running (Run) on muscle fiber types, proteins that regulate intracellular Ca2+, and the metabolic profile in rat plantaris muscle to ascertain the bases for our previous observations that creatine loading results in a higher proportion of myosin heavy chain (MHC) IIb, without corresponding changes in contractile properties. Forty Sprague-Dawley rats were assigned to one of four groups: creatine-fed sedentary, creatine-fed run-trained, control-fed sedentary, and control-fed run-trained animals. Proportion and cross-sectional area increased 10% and 15% in type IIb fibers and the proportion of type IIa fibers decreased 11% in the creatine-fed run-trained compared with the control-fed run-trained group (P < 0.03). No differences were observed in fast Ca2+-ATPase isoform SERCA1 content (P > 0.49). Creatine feeding alone induced a 41% increase (P < 0.03) in slow Ca2+-ATPase (SERCA2) content, which was further elevated by 33% with running (P < 0.02). Run training alone reduced parvalbumin content by 50% (P < 0.05). By comparison, parvalbumin content was dramatically decreased by 75% (P < 0.01) by creatine feeding alone but was not further reduced by run training. These adaptive changes indicate that elevating the capacity for high-energy phosphate shuttling, through creatine loading, alleviates the need for intracellular Ca2+ buffering by parvalbumin and increases the efficiency of Ca2+ uptake by SERCAs. Citrate synthase and 3-hydroxyacyl-CoA dehydrogenase activities were elevated by run training (P < 0.003) but not by run training + creatine feeding. This indicates that creatine loading during run training supports a faster muscle phenotype that is adequately supported by the existing glycolytic potential, without changes in the capacity for terminal substrate oxidation.

fiber type transitions; myosin heavy chain; Ca2+-ATPase; SERCA; parvalbumin



Address for reprint requests and other correspondence: C. T. Putman, E-417 Van Vliet Centre, Univ. of Alberta, Edmonton, AB, Canada T6G 2H9 (e-mail: tputman{at}ualberta.ca)




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