Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence.

Stienen, G. J. M.; Kiers, J.L.; Bottinelli, Roberto; Reggiani, Carlo

doi:10.1113/jphysiol.1996.sp021384

Cited by 226 publications

(229 citation statements)

References 27 publications

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“…However, there is extensive evidence that intact mammalian fibres maintain their contractile performance in vitro at temperatures between 30 and 37°C (Barclay, 1994;Close, 1964Close, , 1965Close and Luff, 1974;Luff, 1981;McCrorey et al, 1966;Ranatunga, 1982) and lizard muscle performs well at 40°C . In contrast, skinned fibre performance declines rapidly with repeated activation, which prevents reliable measurements of maximum power Stienen et al, 1996). We encountered the same problem in the current set of experiments with skinned rabbit fibres at 33°C.…”

Section: Discussionmentioning

confidence: 71%

Skinned fibres produce the same power and force as intact fibre bundles from muscle of wild rabbits

Curtin

Diack

West

et al. 2015

Journal of Experimental Biology

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Skinned fibres have advantages for comparing the muscle properties of different animal species because they can be prepared from a needle biopsy taken under field conditions. However, it is not clear how well the contractile properties of skinned fibres reflect the properties of the muscle fibres in vivo. Here, we compare the mechanical performance of intact fibre bundles and skinned fibres from muscle of the same animals. This is the first such direct comparison. Maximum power and isometric force were measured at 25°C using peroneus longus (PL) and extensor digiti-V (ED-V) muscles from wild rabbits (Oryctolagus cuniculus). More than 90% of the fibres in these muscles are fast-twitch, type 2 fibres. Maximum power was measured in force-clamp experiments. We show that maximum power per volume was the same in intact (121.3 ±16.1 W l −1 , mean±s.e.m.; N=16) and skinned (122.6±4.6 W l −1 ; N=141) fibres. Maximum relative power ( power/F IM L o , where F IM is maximum isometric force and L o is standard fibre length) was also similar in intact (0.645±0.037; N=16) and skinned (0.589±0.019; N=141) fibres. Relative power is independent of volume and thus not subject to errors in measurement of volume. Finally, maximum isometric force per cross-sectional area was also found to be the same for intact and skinned fibres (181.9 kPa±19.1; N=16; 207.8 kPa ±4.8; N=141, respectively). These results contrast with previous measurements of performance at lower temperatures where skinned fibres produce much less power than intact fibres from both mammals and non-mammalian species.

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Section: Discussionmentioning

confidence: 71%

Skinned fibres produce the same power and force as intact fibre bundles from muscle of wild rabbits

Curtin

Diack

West

et al. 2015

Journal of Experimental Biology

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“…1A, the slow fibres are oxidative and have more mitochondria and myoglobin, whereas fast fibres are more glycolytic and exhibit more glycogen and phosphocreatine. Muscle measurements in the steady state or during developed tension revealed that ATPase activity was higher in fast type IIb fibres than that in IIa and IIx fibres, which all have higher activity than slow type I fibres (Stienen et al 1996). During muscle contraction, the ATP hydrolysis rate increases in all fibre types proportionally to the ATP production speed of each fibre type, which is higher in fast fibres than in the slow ones.…”

Section: Introductionmentioning

confidence: 96%

Role of thyroid hormone in skeletal muscle physiology

Bloise

Cordeiro

Ortiga-Carvalho

2018

Journal of Endocrinology

146

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Thyroid hormones (TH) are crucial for development, growth, differentiation, metabolism and thermogenesis. Skeletal muscle (SM) contractile function, myogenesis and bioenergetic metabolism are influenced by TH. These effects depend on the presence of the TH transporters MCT8 and MCT10 in the plasma membrane, the expression of TH receptors (THRA or THRB) and hormone availability, which is determined either by the activation of thyroxine (T 4 ) into triiodothyronine (T 3 ) by type 2 iodothyronine deiodinases (D2) or by the inactivation of T 4 into reverse T 3 by deiodinases type 3 (D3). SM relaxation and contraction rates depend on T 3 regulation of myosin expression and energy supplied by substrate oxidation in the mitochondria. The balance between D2 and D3 expression determines TH intracellular levels and thus influences the proliferation and differentiation of satellite cells, indicating an important role of TH in muscle repair and myogenesis. During critical illness, changes in TH levels and in THR and deiodinase expression negatively affect SM function and repair. This review will discuss the influence of TH action on SM contraction, bioenergetics metabolism, myogenesis and repair in health and illness conditions.

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“…This difference in energy utilization between fibre types undoubtedly reflects differences in cross-bridge cycling kinetics and actomyosin ATPase activities of the different MyHC isoforms [16,[55][56][57][58].…”

Section: Relationship Between Myhc Isoform Expression and Atp Consumpmentioning

confidence: 99%

Cross-bridge kinetics in respiratory muscles

Sieck¹,

Prakash²

1997

Eur Respir J

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In respiratory muscles, force generation and shortening depend on the cyclical interaction of actin and myosin (cross-bridge cycling). During crossbridge cycling, adenosine triphosphate (ATP) is hydrolysed. The globular head region of the myosin heavy chain (MyHC) possesses both the binding site to actin and the site for ATP hydrolysis. Therefore, the MyHC is both a structural and enzymatic protein.Different isoforms of MyHC are expressed in skeletal muscle fibres, and these MyHC isoforms provide mechanical and metabolic diversity. In the present study, the relationships between MyHC isoform expression in single rat diaphragm muscle fibres and their mechanical and energetic properties were evaluated. The expression of MyHC isoforms in single diaphragm muscle fibres was identified using electrophoretic and immunohistochemical techniques. Cross-bridge cycling kinetics in diaphragm muscle fibres clearly depend on MyHC isoform expression, and these differences are interpreted in the context of Huxley's two-state crossbridge model.It is concluded that the unique mechanical and energetic properties of myosin heavy chain isoforms are designed to accomplish different motor behaviours of the diaphragm muscle, and that, as a result of these unique properties, a selective recruitment of diaphragm muscle fibres is essential to avoid fatigue. Eur Respir J 1997; 10: 2147-2158 In respiratory muscles, as in other skeletal muscles, mechanical action results from the cyclical interaction between two contractile proteins, actin and myosin, which is regulated by Ca 2+ release from the sarcoplasmic reticulum (SR) and binding to troponin C. The myosin molecule, a hexameric protein, comprises two myosin heavy chains (MyHC) and four myosin light chains (MyLC). Different isoforms of MyHC exist in skeletal muscle, and the pattern of expression of MyHC isoforms provides the underlying basis for classification of different muscle fibre types. The expression of different MyHC isoforms also provides the underlying basis for the varying mechanical properties of muscle fibres.The dependence of muscle fibre mechanical and energetic properties on MyHC isoform expression stems from the fact that each MyHC contains the binding site of the myosin molecule to actin for cross-bridge formation, as well as the site for the hydrolysis of adenosine triphosphate (ATP) (actomyosin adenosine triphosphatase (ATPase)) during cross-bridge cycling [1][2][3]. Indeed, a smaller proteolytic fragment of the MyHC, comprising the globular head region (subfragment 1), possesses both the actin-binding site and the site for ATP hydrolysis [4]. This review will focus on the mechanical and energetic significance of MyHC isoform expression in diaphragm muscle fibres. Myosin heavy chain expression in skeletal muscle fibresThe genetic regulation of MyHC isoform expression in skeletal muscle fibres is responsive to a number of intrinsic factors, including preprogrammed embryonic and postnatal development, hormonal influences and the pattern of innervation, as well a...

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Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence.

Cited by 226 publications

References 27 publications

Skinned fibres produce the same power and force as intact fibre bundles from muscle of wild rabbits

Skinned fibres produce the same power and force as intact fibre bundles from muscle of wild rabbits

Role of thyroid hormone in skeletal muscle physiology

Cross-bridge kinetics in respiratory muscles

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