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

Author:

Gallo Maria,MacLean Ian,Tyreman Neil,Martins Karen J. B.,Syrotuik Daniel,Gordon Tessa,Putman Charles T.

Abstract

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.

Publisher

American Physiological Society

Subject

Physiology (medical),Physiology

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