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Satoshi Matsunaga

Publications and source records attributed to Satoshi Matsunaga.

9 recordsLinked to original sources
PubMed2007

Effects of high-intensity training and acute exercise on in vitro function of rat sarcoplasmic reticulum.

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.

Animals↗
PubMed2006

Oxidation of myosin heavy chain and reduction in force production in hyperthyroid rat soleus.

We tested the hypothesis that a force reduction in hyperthyroid rat soleus muscle would be associated with oxidative modification in myosin heavy chain (MHC). Daily injection of thyroid hormone [3,5,3'-triiodo-L-thyronine (T3)] for 21 days depressed isometric forces of whole soleus muscle across a range of stimulus frequencies (P < 0.01). In fiber bundles, hyperthyroidism also led to pronounced reductions (P < 0.01) in both K+ - and 4-chloro-m-cresol-induced contracture forces. The degrees of the reductions were similar between these two contractures that were induced by distinct reagents. Treatment with T3 elicited a significant decrease ( approximately 14%; P < 0.05) in the relative content of MHC contained in myofibrillar proteins. The content of carbonyl groups in myofibrillar protein extracts was elevated (P < 0.05) by approximately 50% in T3-treated muscles. Immunoblot analyses on T3-treated muscles showed a greater increase (106%; P < 0.05) of the carbonyl content in MHC than in myofibrillar protein extracts. These data suggest that in hyperthyroidism the decrease in force production of skeletal muscles may stem primarily from failure in myofibrillar protein function resulting from oxidative modification of MHC.

Animals↗
PubMed2003

Carrier doping effect into quasi-one-dimensional bromo-bridged Ni(III) complexes with strong electron-correlation by Cu(II) ions, [Ni1-xCux(chxn)2Br]Br2-x.

This communication will describe the electron doping effect into Ni(III) complexes by Cu(II) ions, [Ni(1-x)Cu(x)(chxn)(2)Br]Br(2-x) (x = 0.038 and 0.101) by using an electrochemical oxidation method. A drastic increase of electrical conductivity as well as a new absorption band around 0.5 eV in single crystal reflectance spectra was observed by doping Cu(II) ions, indicating the electron doping was successfully made. An ESR result shows unpaired electrons locate in the d(x2-y2) orbitals of Cu(II) and have almost no interaction with those of other ions.

Journal Article↗
PubMed2003

Oxidation of sarcoplasmic reticulum Ca(2+)-ATPase induced by 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.

Animals↗
PubMed2003

Effect of endurance training and acute exercise on sarcoplasmic reticulum function in rat fast- and slow-twitch skeletal muscles.

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.

Animals↗
PubMed2003

Endurance training-induced changes in alkali light chain patterns in type IIB fibers of the rat.

The effects of endurance training on the expression of myosin were electrophoretically analyzed in the deep portion of vastus lateralis muscle from the rat. A 10-wk running program led to increases (P < 0.01) in myosin heavy chain (MHC) 2a and 2d with a decrease (P < 0.01) in MHC(2b). Training also evoked a rearrangement of the isomyosin pattern with decreases in fast isomyosin (FM) 1 (P < 0.01) and FM2 (P < 0.05) and a rise in intermediate isomyosin (P < 0.01). These changes were accompanied by a 61% decrease (P < 0.01) in myosin light chain (MLC) 3F (11.8 +/- 2.7 vs. 4.6 +/- 4.2%). Two-dimensional electrophoresis made it possible to separate the triplet of isomyosins (FMb) consisting of MHC(2b). Training elicited a 26% decrease (P < 0.05) in the FM1b fraction within FMb, i.e., FM1b/(FM1b + FM2b + FM3b) (24.2 +/- 5.5 vs. 18.0 +/- 4.3%). These changes resulted in a 10% decrease (P < 0.05) in the MLC(3F) fraction, i.e., MLC(3F)/(MLC(1F) + MLC(3F)), in FMb (44.9 +/- 4.5 vs. 40.3 +/- 3.2%). These results suggest that endurance training may exert the depressive effect on the contractile velocity of type IIB fibers and that a training-induced decrease in the contractile velocity of whole muscle may be caused by alterations in fast alkali MLC complements within a given fiber type as well as by transitions in MHC-based fiber populations.

Alkalies↗