Document Detail


Alterations in in vitro function and protein oxidation of rat sarcoplasmic reticulum Ca2+-ATPase during recovery from high-intensity exercise.
MedLine Citation:
PMID:  18156168     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The hypothesis tested in this study was that the extent to which sarcoplasmic reticulum (SR) Ca(2+)-ATPase is oxidized would correlate with a decline in its activity. For this purpose, changes in the SR Ca(2+)-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 Ca(2+)-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 Ca(2+)-uptake rate, and the proportional alteration in these two variables resulted in no change in the ratio of Ca(2+)-uptake rate to Ca(2+)-ATPase activity. The contents of SR Ca(2+)-ATPase protein and sulfhydryl groups in microsomes were unchanged after exercise and during recovery periods. In contrast, the content of carbonyl groups in SR Ca(2+)-ATPase behaved in an opposite manner to that of SR Ca(2+)-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 Ca(2+)-ATPase is responsible, at least in part, for a decay in the SR Ca(2+)-pumping function produced by high-intensity exercise and imply that oxidized proteins may be repaired during recovery from exercise.
Authors:
Satoshi Matsunaga; Takaaki Mishima; Takashi Yamada; Shuichiro Inashima; Masanobu Wada
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-12-21
Journal Detail:
Title:  Experimental physiology     Volume:  93     ISSN:  0958-0670     ISO Abbreviation:  Exp. Physiol.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-02-26     Completed Date:  2008-06-24     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9002940     Medline TA:  Exp Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  426-33     Citation Subset:  IM    
Affiliation:
Research Center for Urban Health and Sports, Osaka City University, Sugimoto, Sumiyoshi, Osaka, Japan. matunaga@sports.osaka-cu.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Adenosine Diphosphate / metabolism
Adenosine Triphosphate / metabolism
Animals
Calcium / metabolism
Cytoplasm / metabolism
Down-Regulation
Male
Microsomes
Muscle Fibers, Fast-Twitch / enzymology,  metabolism*
Oxidation-Reduction
Oxygen Consumption
Physical Exertion / physiology*
Protein Carbonylation
Quadriceps Muscle / enzymology,  metabolism*
Rats
Rats, Wistar
Recovery of Function
Sarcoplasmic Reticulum / enzymology,  metabolism*
Sarcoplasmic Reticulum Calcium-Transporting ATPases / metabolism*
Sulfhydryl Compounds / metabolism
Time Factors
Chemical
Reg. No./Substance:
0/Sulfhydryl Compounds; 56-65-5/Adenosine Triphosphate; 58-64-0/Adenosine Diphosphate; 7440-70-2/Calcium; EC 3.6.3.8/Sarcoplasmic Reticulum Calcium-Transporting ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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