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This study was conducted to determine whether dietary chicken-breast extract (CBEX), a rich source of histidine-containing dipeptides, could modify exercise-induced changes in sarcoplasmic reticulum (SR) function. After 5 weeks of dietary CBEX, SR Ca2+-handling ability was examined in the vastus lateralis muscles of rats subjected to high-intensity running for 2.5 min. Dietary CBEX caused an approximately 15% and 45% increase (p<.01) in muscle carnosine and anserine concentrations, respectively. In resting muscles, depressions in SR Ca2+-ATPase activity were evoked by dietary CBEX without concomitant changes in SR Ca2+ uptake and release rates. The data confirm that high-intensity exercise depresses SR Ca2+ handling. In spite of the same run time, SR Ca2+ handling was reduced to a lesser degree in muscles of CBEX-containing-chow-fed rats than in standard-chow-fed rats (p<.05). These results suggest that dietary CBEX might attenuate deteriorations in SR Ca2+-handling ability that occur with high-intensity exercise.

Time-dependent changes in sarcoplasmic reticulum (SR) Ca2+-handling and Na+-K+-ATPase activity, as assessed in vitro, were investigated in the superficial (GS) and deep regions (GD) of rat gastrocnemius muscles undergoing short-term (up to 30 min) electrical stimulation. There was a rapid and progressive loss of force output during the first 5 min of stimulation. For GS, significant depressions (P < 0.05) in SR Ca2+-uptake rate and Ca2+-ATPase activity were observed during only the first 1 min. No further reductions occurred with stimulation time. SR Ca2+-release rate was significantly (P < 0.05) decreased at 3 min. For GD, significant reductions (P < 0.05) in Ca2+-uptake rate, Ca2+-release rate and Ca2+-ATPase activity were manifested after 3, 5, and 5 min, respectively. A decay in Na+-K+-ATPase activity was found only in 1-min stimulated GD and 30-min stimulated GS. After 30 min, the depressed functions reverted to resting levels in GD but not in GS. The alterations in any variables examined were not parallel with changes in force output. These results suggest that, at least under the conditions used in this study, in vivo disruptions in cation regulation mediated by vigorous contractile activity would be attributable primarily to events other than structural alterations to the respective proteins.

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.

To evaluate the effects of high-intensity training and/or a single bout of exercise on in vitro function of the sarcoplasmic reticulum (SR), the rats were subjected to 8 weeks of interval running program (final training: 2.5-min running x 4 sets per day, 50 m/min at 10% incline). Following training, SR function, i.e., Ca2+-ATPase activity and Ca2+-uptake and release rates, was examined in homogenates of the superficial region of the vastus lateralis muscle from rats subjected to a single bout of treadmill running (50 m/min at 10% incline) for 2.5 min or to exhaustion. Training brought about a 12.4% increase (P < 0.05) in SR Ca2+-uptake rate in rested muscles. This change was not accompanied by alterations in Ca2+-ATPase activity, Ca2+-release rate, Ca2+ dependence of enzyme and protein contents of Ca2+-ATPase and ryanodine receptor. A single bout of high-intensity exercise to exhaustion evoked significant reductions (P < 0.05) in SR function, irrespective of whether or not the animals were trained. For 2.5-min run and exhausted rats, no differences existed between SR functions of untrained and trained muscles. These data suggest that high-intensity training may be capable of enhancing SR Ca2+-sequestering ability, and may not protect against decreasing SR function with high-intensity exercise.

Ca(2+)-ATPase and Ca(2+)-pumping activities by the sarcoplasmic reticulum (SR) and the amounts of sulphydryl and carbonyl groups contained in the SR protein were examined in the superficial portion of the gastrocnemius and vastus lateralis muscles of the rat after high-intensity treadmill runs to exhaustion (average time to exhaustion: 363 s). Exercise at the estimated maximal O(2) uptake rate led to 16% and 34% reductions in SR Ca(2+)-ATPase activity ( P<0.01) and Ca(2+) uptake rate ( P<0.01), respectively. The carbonyl group content in SR Ca(2+)-ATPase, assessed by immunoblotting analysis, was increased by 127% after exercise ( P<0.05), while the sulphydryl group content in the purified SR fraction was unchanged. Consistent with the unchanged sulphydryl group content, treatment of homogenates with dithiothreitol, the disulphide reducing reagent, failed to restore the decreased catalytic activity of SR Ca(2+)-ATPase in exercised muscles. These findings show clearly that high-intensity, exhaustive exercise causes oxidation of SR Ca(2+)-ATPase protein and suggest that oxidation of amino acids, other than cysteine, in the SR Ca(2+)-ATPase may be responsible, at least in part, for exercise-induced inactivation of this enzyme.

Following 10 weeks of endurance training and in age-matched sedentary rats, sarcoplasmic reticulum (SR) Ca(2+)-uptake, Ca(2+)-release, and Ca(2+)-stimulated adenosinetriphosphatase (ATPase) activity were examined in homogenates of the plantaris and soleus muscles from rats subjected to moderate-intensity treadmill running to exhaustion. In order to examine the effects of acute exercise and/or training on SR Ca(2+)-handling capacity, comparisons between exhausted and non-exercised rats and between trained and untrained rats were performed. Our data confirm that Ca(2+)-sequestration by the SR from fast-twitch muscles is depressed after training. Immediately after exhaustive running, decreases in SR function occurred in both muscles, but were more pronounced in the soleus. In the plantaris, reductions in SR Ca(2+)-uptake rate and Ca(2+)-ATPase activity were observed in untrained rats only, while in the soleus they were adversely affected irrespective of training status. Although the average run time to exhaustion varied markedly between untrained and trained animals (untrained: 253.0 min; trained: 559.4 min), no differences existed with regard to the magnitude of decreases in SR function in the soleus after exercise. The mean rate of decline in SR Ca(2+)-handling capacity during acute exercise, as estimated from the run time and the extent of the decline, was more than twofold higher in untrained than in trained soleus. From the present study, it is unclear whether there exists a causal relationship between muscular fatigue and SR function because the run time to exhaustion was not significantly correlated with any of parameters indicative of SR Ca(2+)-handling capacity, but suggested that endurance training may be capable of delaying a progression of the deterioration in SR function that occurs during exercise.

This study was conducted to determine whether dietary chicken-breast extract (CBEX), a rich source of histidine-containing dipeptides, could modify exercise-induced changes in sarcoplasmic reticulum (SR) function. After 5 weeks of dietary CBEX, SR Ca2+-handling ability was examined in the vastus lateralis muscles of rats subjected to high-intensity running for 2.5 min. Dietary CBEX caused an approximately 15% and 45% increase (p < .01) in muscle carnosine and anserine concentrations, respectively. In resting muscles, depressions in SR Ca2+-ATPase activity were evoked by dietary CBEX without concomitant changes in SR Ca2+ uptake and release rates. The data confirm that high-intensity exercise depresses SR Ca2+ handling. In spite of the same run time, SR Ca2+ handling was reduced to a lesser degree in muscles of CBEX-containing-chow-fed rats than in standard-chow-fed rats (p < .05). These results suggest that dietary CBEX might attenuate deteriorations in SR Ca2+-handling ability that occur with high-intensity exercise. [ABSTRACT FROM AUTHOR]

Time-dependent changes in sarcoplasmic reticulum (SR) Ca2+-handling and Na+-K+-ATPase activity, as assessed in vitro, were investigated in the superficial (GS) and deep regions (GD) of rat gastrocnemius muscles undergoing short-term (up to 30 min) electrical stimulation. There was a rapid and progressive loss of force output during the first 5 min of stimulation. For GS, significant depressions ( P < 0.05) in SR Ca2+-uptake rate and Ca2+-ATPase activity were observed during only the first 1 min. No further reductions occurred with stimulation time. SR Ca2+-release rate was significantly ( P < 0.05) decreased at 3 min. For GD, significant reductions ( P < 0.05) in Ca2+-uptake rate, Ca2+-release rate and Ca2+-ATPase activity were manifested after 3, 5, and 5 min, respectively. A decay in Na+-K+-ATPase activity was found only in 1-min stimulated GD and 30-min stimulated GS. After 30 min, the depressed functions reverted to resting levels in GD but not in GS. The alterations in any variables examined were not parallel with changes in force output. These results suggest that, at least under the conditions used in this study, in vivo disruptions in cation regulation mediated by vigorous contractile activity would be attributable primarily to events other than structural alterations to the respective proteins. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

Ca2+-ATPase and Ca2+-pumping activities by the sarcoplasmic reticulum (SR) and the amounts of sulphydryl and carbonyl groups contained in the SR protein were examined in the superficial portion of the gastrocnemius and vastus lateralis muscles of the rat after high-intensity treadmill runs to exhaustion (average time to exhaustion: 363 s). Exercise at the estimated maximal O2 uptake rate led to 16% and 34% reductions in SR Ca2+-ATPase activity (P<0.01) and Ca2+ uptake rate (P<0.01), respectively. The carbonyl group content in SR Ca2+-ATPase, assessed by immunoblotting analysis, was increased by 127% after exercise (P<0.05), while the sulphydryl group content in the purified SR fraction was unchanged. Consistent with the unchanged sulphydryl group content, treatment of homogenates with dithiothreitol, the disulphide reducing reagent, failed to restore the decreased catalytic activity of SR Ca2+-ATPase in exercised muscles. These findings show clearly that high-intensity, exhaustive exercise causes oxidation of SR Ca2+-ATPase protein and suggest that oxidation of amino acids, other than cysteine, in the SR Ca2+-ATPase may be responsible, at least in part, for exercise-induced inactivation of this enzyme. [ABSTRACT FROM AUTHOR]