Specific effects of endurance and sprint training on protein expression of calsequestrin and SERCA in mouse skeletal muscle.
ABSTRACT Calsequestrin (CSQ) is the main Ca²⁺ binding protein inside the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. The present study demonstrates the specific effects of different training regimens on CSQ isoform 1 (CSQ1, the primary isoform) and SR Ca²⁺-ATPase (SERCA1, 2) expression in various skeletal muscles of mouse. CSQ1, SERCA1, and SERCA2 protein expression was determined with Western blot in m. soleus (SOL), m. extensor digitorum longus (EDL), m. gastrocnemius (GAS), m. rectus femoris (RF), and m. tibialis anterior (TA) muscles after completing a 6-week endurance or sprint training program. Endurance training induced decrease in CSQ1 concentration in SOL (p < 0.001) and in SERCA1 levels in GAS (p < 0.05), whereas increase in CSQ1 expression was detected in EDL (p < 0.01). After sprint training the concentration of CSQ1 increased in GAS (p < 0.01) and EDL (p < 0.01). Additionally, sprint exercise induced an increase in SERCA1 in GAS (p < 0.001) and a decline in TA (p < 0.05). SERCA2 was up-regulated with sprint training in GAS (p < 0.01). Myosin heavy chain (MHC) based fibre type composition altered differently depending on the muscle and the training regimen.These results indicate that (1) diverse training strategies used affect differently CSQ1 and SERCA1 concentrations in the skeletal muscle, (2) the regulation of CSQ1 and SERCA1 does not necessary follow the fast-slow definition despite the correlation between MHC isoforms, and (3) the changes in CSQ1 concentration occur prior to SERCA1 or SERCA2.
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ABSTRACT: The adaptations of muscle to sprint training can be separated into metabolic and morphological changes. Enzyme adaptations represent a major metabolic adaptation to sprint training, with the enzymes of all three energy systems showing signs of adaptation to training and some evidence of a return to baseline levels with detraining. Myokinase and creatine phosphokinase have shown small increases as a result of short-sprint training in some studies and elite sprinters appear better able to rapidly breakdown phosphocreatine (PCr) than the sub-elite. No changes in these enzyme levels have been reported as a result of detraining. Similarly, glycolytic enzyme activity (notably lactate dehydrogenase, phosphofructokinase and glycogen phosphorylase) has been shown to increase after training consisting of either long (>10-second) or short (<10-second) sprints. Evidence suggests that these enzymes return to pre-training levels after somewhere between 7 weeks and 6 months of detraining. Mitochondrial enzyme activity also increases after sprint training, particularly when long sprints or short recovery between short sprints are used as the training stimulus. Morphological adaptations to sprint training include changes in muscle fibre type, sarcoplasmic reticulum, and fibre cross-sectional area. An appropriate sprint training programme could be expected to induce a shift toward type IIa muscle, increase muscle cross-sectional area and increase the sarcoplasmic reticulum volume to aid release of Ca(2+). Training volume and/or frequency of sprint training in excess of what is optimal for an individual, however, will induce a shift toward slower muscle contractile characteristics. In contrast, detraining appears to shift the contractile characteristics towards type IIb, although muscle atrophy is also likely to occur. Muscle conduction velocity appears to be a potential non-invasive method of monitoring contractile changes in response to sprint training and detraining. In summary, adaptation to sprint training is clearly dependent on the duration of sprinting, recovery between repetitions, total volume and frequency of training bouts. These variables have profound effects on the metabolic, structural and performance adaptations from a sprint-training programme and these changes take a considerable period of time to return to baseline after a period of detraining. However, the complexity of the interaction between the aforementioned variables and training adaptation combined with individual differences is clearly disruptive to the transfer of knowledge and advice from laboratory to coach to athlete.Sports Medicine 01/2001; 31(15):1063-82. · 5.24 Impact Factor
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ABSTRACT: We recently reported that 19 wk of heavy resistance training caused a decrease in the percentage of type IIb and an increase in the percentage of type IIa fibers as determined by qualitative histochemical analyses of myofibrillar adenosinetriphosphatase activity of biopsies of musculus vastus lateralis (Hather et al. Acta Physiol. Scand. 143: 177-185, 1991). These data were interpreted to suggest that resistance training had caused transformation among the fast-twitch fiber subtypes. To more clearly establish the influence of resistance training on muscle fiber composition, biopsies from the original study were analyzed biochemically for myosin heavy chain (MHC) composition by use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and histochemically for fiber types by use of myofibrillar adenosinetriphosphatase activity. The results show that after training (n = 13), IIb MHC composition decreased (P < 0.05) from 19 +/- 4 to 7 +/- 1%. IIa MHC, in contrast, increased (P < 0.05) from 48 +/- 3 to 60 +/- 2%. These responses were essentially mirrored by alterations in fiber type distribution. The percentage of type IIb fibers decreased (P < 0.05) from 18 +/- 3 to 1 +/- 1%, whereas the percentage of type IIa fibers increased from 46 +/- 4 to 60 +/- 3% (P < 0.05). Neither I MHC composition nor type I fiber percentage changed with training. The control group (n = 4) showed no changes in MHC composition or fiber type distribution. These results suggest that heavy resistance training alters MHC composition in human skeletal muscle, presumably reflecting a change in genetic expression.Journal of Applied Physiology 03/1993; 74(2):911-5. · 3.48 Impact Factor
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ABSTRACT: The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+ binding protein localized in the lumen of sarcoplasmic reticulum, are the products of two different genes (Fliegel, L., Leberer, E., Green, N.M. and MacLennan, D.H. (1982) FEBS Lett. 242, 297-300), and can be both purified from slow-twitch skeletal muscle of the rabbit (Damiani, E., Volpe, P. and Margreth, A. (1990) J. Muscle Res. Cell Motil. 11, 522-530). Here we show that both CS isoforms coexist in slow-twitch muscle fibers as indicated by indirect immunofluorescent staining of cryosections with affinity-purified antibodies specific for each CS isoform.FEBS Letters 04/1992; 299(2):175-8. · 3.58 Impact Factor