Plasticity of skeletal myosin in endurance-trained rats (I). A quantitative study

Wahrmann, J.P.; Winand, René; Rieu, M

doi:10.1007/s004210100402

Cited by 13 publications

(21 citation statements)

References 25 publications

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“…Wahrmann, Winand and Rieu [27] quantified changes in MyLC isoforms in different muscles during exercise. They claim that, in order to better understand the function of MyLC in skeletal muscle it is necessary to study changes in MyLC in parallel with the quantification of MyHC under the same conditions.…”

Section: Discussionmentioning

confidence: 99%

“…Most exercise studies focus on the assessment of the composition of MyHC, because of its regulatory role in myosin ATPase activity and therefore in the velocity of muscle fiber shortening [5,9]. Only in a few studies has attention been paid to the simultaneous effect of exercise on the composition of MyHC and MyLC isoforms [23,27]. It is particularly unclear how exercise of different intensity and duration affects the changes in the relative content of MyLC isoforms and their distribution in different muscles.…”

Section: Introductionmentioning

confidence: 99%

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Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: effect of exercise

Alev¹,

Kaasik²,

Pehme³

et al. 2009

Biol Sport

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Abstract:The aims of the present study were to show the distribution of individual myosin light chain (MyLC) isoforms in fast-twitch (FT) and slowtwitch (ST) muscles and between FT muscles in order to find differences between MyLC isoforms in these muscles, to identify similarities with the distribution of myosin heavy chain (MyHC) isoforms and to investigate changes in these relations during adaptation to endurance and resistance training. Male Wistar strain rats were used in this study. One-dimensional electrophoresis was used for separation of MyHC and MyLC isoforms and two-dimensional electrophoresis was used for identification of MyLC different isoforms. A difference in the relative content of MyLC isoforms between FT muscles exists only in the case of MyLC 1 slow and 2 slow isoforms. Differences in the relative content of MyHC between FT muscles are considerably larger than differences in the MyLC isoforms. MyHC and MyLC isoforms both participate in the remodelling of contractile proteins during exercise training. In conclusion: The present study shows some discrepancy between the modulation of MyHC and MyLC isoforms in muscles with different oxidative potential during adaptation to endurance and resistance training. In ST muscles, there is full agreement between the increase in the relative content of MyHC IIa isoform and MyLC 2 fast and 3 fast isoforms during resistance training without significant changes during endurance training. The ratio of MyLC 3 and MyLC 2 isoforms increases during both types of exercise training, but it is two times higher during resistance training.(Biol.Sport 26:215-234, 2009)

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: effect of exercise

Alev¹,

Kaasik²,

Pehme³

et al. 2009

Biol Sport

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“…The effects of endurance training on muscle MHC isoforms are well established. Many investigations (6,15,17,20,25,37,38,39) have demonstrated that this type of muscular activity promotes significant transformation of fast-to-slow MHC isoforms within both slow and fast skeletal muscles. Such shift in the total muscle MHC pool is not due to selective changes in fiber size but is due to a training-induced transformation in MHC isoforms expressed by individual fibers.…”

Section: Discussionmentioning

confidence: 99%

Paradoxical effects of endurance training and chronic hypoxia on myofibrillar ATPase activity

Roels¹,

Reggiani²,

Reboul³

et al. 2008

American Journal of Physiology-Regulatory, Integrative and Comp

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This study aimed to determine the changes in soleus myofibrillar ATPase (m-ATPase) activity and myosin heavy chain (MHC) isoform expression after endurance training and/or chronic hypoxic exposure. Dark Agouti rats were randomly divided into four groups: control, normoxic sedentary (N; n = 14), normoxic endurance trained (NT; n = 14), hypoxic sedentary (H; n = 10), and hypoxic endurance trained (HT; n = 14). Rats lived and trained in normoxia at 760 mmHg (N and NT) or hypobaric hypoxia at 550 mmHg (approximately 2,800 m) (H and HT). m-ATPase activity was measured by rapid flow quench technique; myosin subunits were analyzed with mono- and two-dimensional gel electrophoresis. Endurance training significantly increased m-ATPase (P < 0.01), although an increase in MHC-I content occurred (P < 0.01). In spite of slow-to-fast transitions in MHC isoform distribution in chronic hypoxia (P < 0.05) no increase in m-ATPase was observed. The rate constants of m-ATPase were 0.0350 +/- 0.0023 s(-1) and 0.047 +/- 0.0050 s(-1) for N and NT and 0.033 +/- 0.0021 s(-1) and 0.038 +/- 0.0032 s(-1) for H and HT. Thus, dissociation between variations in m-ATPase and changes in MHC isoform expression was observed. Changes in fraction of active myosin heads, in myosin light chain isoform (MLC) distribution or in MLC phosphorylation, could not explain the variations in m-ATPase. Myosin posttranslational modifications or changes in other myofibrillar proteins may therefore be responsible for the observed variations in m-ATPase activity.

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“…CB administration or HU. These two models were chosen for several reasons: (i) they permitted us to achieve a large range of slow-to-fast muscular modifications with the appearance of a large diversity of transformed fibres, (ii) insofar as the studies on MHC and MLC isoforms in transformed fibres have been based essentially on increased neuromuscular activity experiments, for instance chronic, low-frequency stimulation [1,13,20] or endurance training [29], these models will add to our understanding of the concept of muscle plasticity all over the (slow↔fast) spectrum of fibre types and (iii) they will allow us to determine whether, according to our previous studies on MHC and MLC isoforms at the whole muscle level, differences exist at the single fibre level between the adaptive responses of soleus muscle. The slow postural soleus muscle was particularly affected by these two conditions, other hindlimb muscles being less modified (extensor digitorum longus<red gastrocnemius<soleus) [25].…”

Section: Introductionmentioning

confidence: 99%

Hybrid fibres under slow-to-fast transformations: expression is of myosin heavy and light chains in rat soleus muscle

Stevens¹,

Bastide²,

Bozzo³

et al. 2004

Pflugers Arch - Eur J Physiol

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The aim of this study was to examine the expression pattern of myosin heavy chain (MHC) and myosin light chain (MLC) isoforms in single fibres from the rat soleus muscle under control (Cont) conditions and under conditions inducing slow-to-fast phenotype transitions. Two models of muscle phenotype modification, namely 2 weeks clenbuterol (CB) administration or hindlimb unloading (HU), were chosen to achieve a full range of appearance of hybrid fibres, i.show $132#e. fibres co-expressing slow and fast myosin isoforms. MHC and MLC compositions were analysed in parallel by one-dimensional-gel electrophoresis. We showed that (i) the slow-to-fast fibre type transitions at the MHC level were accompanied by exchanges of slow with fast MLC isoforms and (ii) that these transitions were characterized by increased proportions of hybrid profiles of both MHC and MLC isoforms, under both CB (27.5%) and HU (18%) conditions when compared with Cont (7%). This suggested a MHC-MLC coordinated program for myosin regulation during fibre type transitions. However, mismatched hybrid co-expression of MHC and MLC was also observed, probably resulting from differences in post-transcriptional regulation. Finally, in all the muscle fibre groups, specific favourable correlations between one MHC (IIa, IId or IIb) and one MLC (regulatory or essential) type were found.

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Plasticity of skeletal myosin in endurance-trained rats (I). A quantitative study

Cited by 13 publications

References 25 publications

Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: effect of exercise

Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: effect of exercise

Paradoxical effects of endurance training and chronic hypoxia on myofibrillar ATPase activity

Hybrid fibres under slow-to-fast transformations: expression is of myosin heavy and light chains in rat soleus muscle

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