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Experimental Physiology 93.3 pp 426-433
DOI: 10.1113/expphysiol.2007.040477
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Alterations in in vitro function and protein oxidation of rat sarcoplasmic reticulum Ca2+-ATPase during recovery from high-intensity exercise

Satoshi Matsunaga1, Takaaki Mishima2, Takashi Yamada3, Shuichiro Inashima4 and Masanobu Wada5

1 Research Center for Urban Health and Sports, Osaka City University, 3–3-138 Sugimoto, Sumiyoshi, Osaka 558–8585, Japan 2 Pre School Education Department, Hachinohe Junior College, 13–384 Mihono, Hachinohe, Aomori 031–0844, Japan 3 Department of Physiology and Pharmacology, Karolinska Institutet, SE-171 77 Stockholm, Sweden 4 Research Center of Health, Physical Fitness and Sports, Nagoya University, Furo, Chikusa, Nagoya, Aichi 464–8601, Japan 5 Graduate School of Integrated Arts and Sciences, Hiroshima University, 1–7-1 Kagamiyama, Higashi-hiroshima, Hiroshima 739–8521, Japan

The hypothesis tested in this study was that the extent to which sarcoplasmic reticulum (SR) Ca2+-ATPase is oxidized would correlate with a decline in its activity. For this purpose, changes in the SR Ca2+-sequestering ability and the contents of carbonyl and sulfhydryl groups during recovery after exercise were examined in the superficial portions of vastus lateralis muscles from rats subjected to 5 min running at an intensity corresponding to maximal oxygen uptake (50 m min–1, 10% gradient). A single bout of exercise elicited a 22.4% reduction (P < 0.05) in SR Ca2+-ATPase activity. The decreased activity progressively reverted to normal levels during recovery after exercise, reaching normal levels after 60 min of recovery. This change was paralleled by a depressed SR Ca2+-uptake rate, and the proportional alteration in these two variables resulted in no change in the ratio of Ca2+-uptake rate to Ca2+-ATPase activity. The contents of SR Ca2+-ATPase protein and sulfhydryl groups in microsomes were unchanged after exercise and during recovery periods. In contrast, the content of carbonyl groups in SR Ca2+-ATPase behaved in an opposite manner to that of SR Ca2+-ATPase activity. An approximately 80% augmentation (P < 0.05) in the carbonyl group content occurred immediately after exercise. The elevated carbonyl content decreased towards normal levels during 60 min of recovery. These results are strongly suggestive that oxidation of SR Ca2+-ATPase is responsible, at least in part, for a decay in the SR Ca2+-pumping function produced by high-intensity exercise and imply that oxidized proteins may be repaired during recovery from exercise.

(Received 29 August 2007; accepted after revision 18 December 2007; first published online 21 December 2007)
Corresponding author S. Matsunaga: Research Center for Urban Health and Sports, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi, Osaka 558-8585, Japan. Email: matunaga{at}sports.osaka-cu.ac.jp







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