Favourable associations between the myosin heavy-chain and light-chain isoforms in human skeletal muscle

Wada, Masanobu; Katsuta, Shigeru; Doi, Takehiko; Kuno, S.

doi:10.1007/bf00370616

Cited by 13 publications

(4 citation statements)

References 31 publications

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“…The low affinity of MyLC 3 fast and the higher affinity of MyLC 1 fast isoform with MyHC IIa isoform shows differences between myosin isoforms in FT muscles [24]. Our study does not support the standpoint that, in FT muscles, the relative content of alkali MyLC isoforms is higher than in ST [3].…”

Section: Discussioncontrasting

confidence: 92%

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: Discussioncontrasting

confidence: 92%

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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“…In this sense, the slow and fast ELC isoforms can be viewed as corresponding pairs. Given the notion that in human muscles ELC 3f appears to be preferentially associated with the IIB myosin heavy chain and ELC If with IIA (Wada et al, 1990), one could hypothesize that there might be a preference of ELC 1sa to be co-expressed with a second human Type I heavy-chain mRNA that is expressed in a Type I subpopulation only, as recently proposed by Schiaffino and Reggiani (1994), whereas ELC 1sb would be associated with the P-Type I heavy chain.…”

Section: Discussionmentioning

confidence: 86%

Fiber-type-specific expression of essential (alkali) myosin light chains in human skeletal muscles.

Jostarndt¹,

Puntschart²,

Hoppeler³

et al. 1996

J Histochem Cytochem.

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We studied the expression patterns of the essential (alkali) myosin light-chain isoforms in adult human skeletal muscles, using in situ hybridization and single-fiber protein analysis. In analogy to other species, we found that the fiber type-specific expression of essential myosin light chains is regulated via the availability of the respective "As in a given fiber. In contrast to other species, the slow isoform Isa was only expressed in the most oxidative Type I fibers (Subtype IA) in addition to lsb. These fibers also contained high levels of carbonic anhydrase III. Within the fibers, the essential myosin light-chain "As were located preferentially in the perinuclear regions and to a lesser extent in the

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“…In human skeletal muscles, slow MHC has been found to associate preferentially with slow isoforms of both alkaline and regulatory MLC [26]. Fast MHC isoforms preferentially associate with fast MLC isoforms [26].…”

Section: Discussionmentioning

confidence: 99%

Fibre types in skeletal muscles of chronic obstructive pulmonary disease patients related to respiratory function and exercise tolerance

Satta¹,

Migliori²,

Spanevello³

et al. 1997

Eur Respir J

136

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F Fi ib br re e t ty yp pe es s iin n s sk ke el le et ta al l m mu us sc cl le es s o of f c ch hr ro on ni ic c o ob bs st tr ru uc ct ti iv ve e p pu ul lm mo on na ar ry y d di is se ea as se e p pa at ti ie en nt ts s r re el la at te ed d t to o r re es sp pi ir ra at to or ry y f fu un nc ct ti io on n a an nd d e ex xe er rc ci is se e t to ol le er ra an nc ce e A group of 22 COPD patients and 10 healthy control subjects were studied. In COPD patients, vital capacity (VC) and forced expiratory volume in one second (FEV1) were reduced to 79% and 51%, respectively. Diffusion indices (transfer factor of the lung for carbon monoxide (TL,CO) and carbon monoxide transfer coefficient (KCO)) were also reduced. Arterial oxygen tension (Pa,O 2 ) was normal or slightly altered. A maximal exercise test was performed and anaerobic threshold was calculated. Muscle samples from vastus lateralis were obtained by needle biopsy. Myosin heavy chain (MHC) and light chain (MLC) isoforms were separated by gel electrophoresis and quantified by densitometry. MHC isoforms were considered as molecular markers of fibre types.The proportion of the fast MHC-2B isoform was increased in COPD patients. TL,CO, KCO, VC and FEV1 were positively correlated with slow MHC isoform content. TL,CO and KCO were also negatively correlated with the content of the fast MHC-2B isoform. No correlation was found between exercise parameters and MHC isoform composition. The co-ordinated expression between MHC and MLC isoforms was altered in COPD patients.We conclude that reduced oxygen availability, probably in combination with muscle disuse, may determine muscle alterations in chronic obstructive pulmonary disease patients. The altered correlations between myosin heavy chain and light chain isoforms suggest that co-ordinated protein expression is lost in chronic obstructive pulmonary disease muscles. Eur Respir J 1997; 10: 2853-2860 Patients with chronic obstructive pulmonary disease (COPD) are characterized by poor quality of life and various degrees of limitation in their daily activity, mainly due to breathlessness. They are often self-limiting their level of activity into a downward spiral leading to further inactivity and muscle deconditioning. Exercise tolerance of COPD patients is determined by the level of ventilation that they can reach. Even at a rather low work rate the increase in ventilatory response and blood lactate concentration are higher than in normal subjects.Rehabilitation of COPD patients involves general exercise reconditioning. This is suggested as the best approach to the rehabilitation of COPD patients, and is usually performed by training large muscles of the lower and, less frequently, upper limbs [1]. The mechanisms underlying the improvement of the performance after general training in COPD subjects are still unclear.There is evidence that skeletal muscle function and structure are altered in COPD patients. Contractile strength is reduced [2] and energetic and oxidative metabolism are impaired [3][4][5]. Fibre-type compos...

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Favourable associations between the myosin heavy-chain and light-chain isoforms in human skeletal muscle

Cited by 13 publications

References 31 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

Fiber-type-specific expression of essential (alkali) myosin light chains in human skeletal muscles.

Fibre types in skeletal muscles of chronic obstructive pulmonary disease patients related to respiratory function and exercise tolerance

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