Myosin heavy chain composition in young and old rat skeletal muscle: effects of endurance exercise

Sullivan, Vicki K.; Powers, Scott K.; Criswell, David S.; Tümer, Nihal; LaRochelle, Jeffrey; Löwenthal, David

doi:10.1152/jappl.1995.78.6.2115

Cited by 85 publications

(82 citation statements)

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“…Silver staining of MHC bands revealed a transition from fast MHC-IIb to MHC-IIa to slow MHC-I in 8-month-versus 22-month-old muscles. This altered pattern of MHC expression agrees in general with the molecular processes that occur during fast-to-slow transitions, such as adaptations following chronic low-frequency stimulation of fast muscles (Pette and Staron, 2001) or endurance exercise (Sullivan et al, 1995).…”

Section: Discussionsupporting

confidence: 79%

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Gannon

Doran

Kirwan

et al. 2009

European Journal of Cell Biology

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The age-dependent decline in skeletal muscle mass and function is believed to be due to a multi-factorial pathology and represents a major factor that blocks healthy aging by increasing physical disability, frailty and loss of independence in the elderly. This study has focused on the comparative proteomic analysis of contractile elements and revealed that the most striking age-related changes seem to occur in the protein family representing myosin light chains (MLCs). Comparative screening of total muscle extracts suggests a fast-to-slow transition in the aged MLC population. The mass spectrometric analysis of the myofibril-enriched fraction identified the MLC2 isoform of the slow-type MLC as the contractile protein with the most drastically changed expression during aging. Immunoblotting confirmed an increased abundance of slow MLC2, concomitant with a switch in fast versus slow myosin heavy chains. Staining of two-dimensional gels of crude extracts with the phospho-specific fluorescent dye ProQ-Diamond identified the increased MLC2 spot as a muscle protein with a drastically enhanced phosphorylation level in aged fibres. Comparative immunofluorescence microscopy, using antibodies to fast and slow myosin isoforms, confirmed a fast-to-slow transformation process during muscle aging. Interestingly, the dramatic increase in slow MLC2 expression was restricted to individual senescent fibres. These findings agree with the idea that aged skeletal muscles undergo a shift to more aerobic-oxidative metabolism in a slower-twitching fibre population and suggest the slow MLC2 isoform as a potential biomarker for fibre type shifting in sarcopenia of old age.

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Section: Discussionsupporting

confidence: 79%

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Gannon

Doran

Kirwan

et al. 2009

European Journal of Cell Biology

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“…It was also conceivable that the intensity or period of exercise in this experiment was not so strong as to cause notable change of skeletal muscle fiber types. Sullivan et al showed that exercise training, which was 18-20 m/min treadmill running (60 min) 5 d/wk for 8 wk, resulted in a decrease in the percentage of type IIb MyHC (untrained, 43.0%; trained, 29.9%) and an increase in the percentage of type IIa MyHC (untrained, 14.0%; trained, 17.5%) in plantaris muscle in rats (16). Therefore, it is necessary to examine high intensity or long term effects of exercise training in order to check the synergistic effect of beef extract and exercise.…”

Section: Discussionmentioning

confidence: 99%

“…Each dietary group was furthermore subdivided into aerobically exercised and nonexercised groups (total 4 groups); Control: nonexercised, nonsupplemented, BE: nonexercised, supplemented, CE: exercised, nonsupplemented, BE ϩ CE: exercised, supplemented. Exercised subjects engaged in compulsory exercise for 30 min every other day with a treadmill running tool having 5% grade and 15 m/min speed and this protocol was assumed as low intensity endurance exercise compared with previous reports ( 16 ). The body weight of each group at the beginning of the experiment (after pre-feeding) was adjusted to be as identical as possible [276.8 Ϯ 9.4 (SD) g in Control, 265.6 Ϯ 17.4 g in BE, 275.1 Ϯ 10.8 g in CE, 265.2 Ϯ 13.7 g in BE ϩ CE].…”

Section: Methodsmentioning

confidence: 99%

Beef Extract Supplementation Increases Leg Muscle Mass and Modifies Skeletal Muscle Fiber Types in Rats

Yoshihara

Wakamatsu

Kawabata

et al. 2006

J Nutr Sci Vitaminol

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SummaryThe objective of this research was to investigate the effects of beef extract on fat metabolism, muscle mass and muscle fiber types in rats. We also investigated the synergetic effect of endurance exercise. Twenty-four male rats weighing about 270 g were assigned to two diets containing 0 or 6% beef extract (BE). Half the rats fed each diet were subjected to compulsory exercise (CE) for 30 min every other day. After 4 weeks feeding, the blood was collected and various organs were dissected. The muscle fiber type of the soleus and extensor digitorum longus (EDL) muscles were evaluated by histochemical and electrophoretical analyses. Rats supplemented with BE showed a decrease in fat content in liver and abdomen and an increase in the activity of carnitine palmitoyl transferase II in liver. BE as well as exercise increased the relative weights of both soleus and EDL. BE alone and BE plus CE did not affect the distribution of muscle fiber types in soleus. BE without exercise decreased in type IIb of EDL from 54% to 44% with compensatory increase in type IIa from 41% to 49% and type I from 5% to 7% compared with the nonsupplemented, nonexercised control group. No synergetic effect on a fast to slow fiber conversion due to the combination of BE and CE was detected. Thus, BE supplement increased muscle mass and slow type fiber in EDL. The effects of BE supplement on muscle characteristics were similar to those of exercise. Key Words beef extract, fat metabolism, muscle fiber type, muscle mass, L -carnitine A great deal of research has been done to elucidate the general nutritional value of beef on the growth of human subjects and the effects of protein quality and exercise on the growth and protein metabolism of animals and human beings ( 1-3 ). However, existing information about the nutritional effects of beef extract on muscle metabolism is not sufficient.Skeletal muscle is composed of at least three fiber types on the basis of their contractile and energy metabolic properties; type I fibers exhibit an aerobic energy metabolism (slow-twitch fiber), type IIb fibers are predominantly glycolytic (fast-twitch fiber) and type IIa fibers are the intermediate type exhibiting both oxidative and glycolytic metabolisms. Lipids are easily accumulated in type I fibers ( 4 ), while glycogen depletion occurs primarily in the type II ( 5 ). It is well known that cross-reinnervation, electrical stimulation or exercise evokes the fiber type conversion, although the molecular mechanisms mediating the transformation are not clearly elucidated ( 6 , 7 ). This means that skeletal muscle cells possess a capacity to respond and adapt to metabolic changes imposed by physical stimulation or neural stimulation. Concretely, endurance exercise requiring the consumption of oxygen stimulates a shift to the slow twitch, oxidative muscle fibers ( 8 ). The fiber types of adult skeletal muscle are closely related to energy metabolic characteristics as described above. Nutrition-induced regulation in mRNA levels for a number of metabolic gene...

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“…This is reflected in the composition and level of expression of MyHC isoforms within these muscle. Various factors such as development, innervation, increased and decreased neuromuscular activity, physical activity (overloading and unloading), hormones and ageing, have been shown to influence the phenotypic expression of skeletal muscle fibers (Sullivan et al, 1995;Schiaffino and Reggiani, 1996;Pette and Staron, 2000). Skeletal muscle plasticity has been studied extensively by myosin isoform transitions in different experimental animal models, i.e.…”

Section: Introductionmentioning

confidence: 99%

Myosin heavy chain isoforms in postnatal muscle development of mice

Agbulut¹,

Noirez²,

Beaumont³

et al. 2003

Biology of the Cell

230

220

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In this study, using a high-resolution gel electrophoresis technique, we have characterized the myosin heavy chain composition in different skeletal muscle of the mouse during postnatal development. The pattern of myosin heavy chain expression was studied in four hind limb muscles, the diaphragm, the tongue and the masseter. All of these muscles displayed the usual sequential transitions from embryonic to neonatal and to adult myosin heavy chain isoforms but more interestingly these transitions occur with a distinct chronology in the different muscles. In addition, our results demonstrated a transitory pattern of expression for certain adult myosin heavy chain isoforms in the soleus and the tongue. In the soleus muscle IIB and in the tongue IIA myosin heavy chain isoforms were detected only for a short time during postnatal life. Our results demonstrate that muscles of the mouse with different functions are subjected to a distinct programs of myosin isoform transitions during postnatal muscle development. This study describes new data which will help us to understand both postnatal muscle development in transgenic mouse muscles as well as in muscle pathology.

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Myosin heavy chain composition in young and old rat skeletal muscle: effects of endurance exercise

Cited by 85 publications

References 0 publications

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Drastic increase of myosin light chain MLC-2 in senescent skeletal muscle indicates fast-to-slow fibre transition in sarcopenia of old age

Beef Extract Supplementation Increases Leg Muscle Mass and Modifies Skeletal Muscle Fiber Types in Rats

Myosin heavy chain isoforms in postnatal muscle development of mice

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