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Exercise-induced fibre type transitions with regard to myosin, parvalbumin, and sarcoplasmic reticulum in muscles of the rat

  • Heart, Circulation, Respiration and Blood; Environmental and Exercise Physiology
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Abstract

Effects of a long-term, high intensity training program upon histochemically assessed myofibrillar actomyosin ATPase, myosin composition, peptide pattern of sarcoplasmic reticulum (SR), and parvalbumin content were analysed in muscles from the same rats which were used in a previous study (Green et al. 1983). Following 15 weeks of extreme training, an increase in type I and type IIA fibres and a decrease in type IIB fibres occurred both in plantaris and extensor digitorum longus (EDL) muscles. In the deep portion of vastus lateralis (VLD), there was a pronounced increase from 10±5% to 27±11% in type I fibres. No type I fibres were detected in the superficial portion of vastus lateralis (VLS) both in control and trained animals. An increase in slow type myosin light chains accompanied the histochemically observed fibre type transition in VLD. Changes in the peptide pattern of SR occurred both in VLS and VLD and suggested a complete transition from type IIB to IIA in VLS and from type IIA to I in VLD. A complete type IIA to I transition in the VLD was also suggested by the failure to detect parvalbumin in this muscle after 15 weeks of training. Changes in parvalbumin content and SR tended to precede the transitions in the myosin light chains. Obviously, high intensity endurance training is capable of transforming specific characteristics of muscle fibres beyond the commonly observed changes in the enzyme activity pattern of energy metabolism. The time courses of the various changes which are similar to those in chronic nerve stimulation experiments, indicate that various functional systems of the muscle fibre do not change simultaneously.

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References

  • Andersen P, Henriksson J (1977) Training induced changes in the subgroups of human type II skeletal muscle fibres. Acta Physiol Scand 99:123–125

    Google Scholar 

  • Baldwin KM, Klinkerfuss GH, Terjung RL, Molé PA, Holloszy JO (1972) Respiratory capacity of white, red and intermediate muscle: adaptive response to exercise. Am J Physiol 222:373–378

    Google Scholar 

  • Billeter R, Heizmann CW, Howald H, Jenny E (1981) Analysis of myosin light and heavy chain types in single human skeletal muscle fibers. Eur J Biochem 116:389–395

    Google Scholar 

  • Blum HE, Lehky P, Kohler L, Stein EA, Fischer EH (1977) Comparative properties of vertebrate parvalbumins. J Biol Chem 252:2834–2838

    Google Scholar 

  • Brooke MH, Kaiser KK (1970) Three ‘Myosin ATPase’ systems: The nature of their pH lability and sulfhydryl dependence. J Histochem Cytochem 18:670–672

    Google Scholar 

  • Celio MR, Heizmann CW (1982) Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres. Nature (Lond) 297:504–506

    Google Scholar 

  • Gollnick D, Parsons D, Oakley CR (1983) Differentiation of fiber types in skeletal muscle from the sequential inactivation of myofibrillar actomyosin ATPase during acid preincubation. Histochemistry 77:543–555

    Google Scholar 

  • Green HJ, Thomson JA, Daub WD, Houston ME, Ranney DA (1979) Fiber composition, fiber size and enzyme activities in vastus lateralis of elite athletes involved in high intensity exercise. Eur J Appl Physiol 41:109–117

    Google Scholar 

  • Green HJ, Reichmann H, Pette D (1983) Fibre type specific transformations in the enzyme activity pattern of rat vastus lateralis muscle by prolonged endurance training. Pflügers Arch 399:216–222

    Google Scholar 

  • Harris B, Heilig A, Hudlická O, Leberer E, Pette D, Tyler K (1982) Changes in rabbit muscle enzyme activities in response to chronic stimulation with different frequency patterns. In: Semigonovský B, Tucêk S (eds) Metabolic and functional changes during exercise. Charles University, Prague, pp 27–31

    Google Scholar 

  • Heilmann C, Pette D (1979) Molecular transofrmations in sarcoplasmic reticulum of fast twitch muscle by electrostimulation. Eur J Biochem 93:437–446

    Google Scholar 

  • Hoffer JA, O'Donovan MJ, Pratt CA, Loeb GE (1981) Discharge patterns of hindlimb motoneurons during normal cat locomotion. Science 213:466–468

    Google Scholar 

  • Holloszy JO, Booth FW (1976) Biochemical adaptations to endurance exercise in muscle. Ann Rev Physiol 38:273–291

    Google Scholar 

  • Hudlická O, Tyler KR, Aitman T (1980) The effect of long-term electrical stimulation on fuel uptake and performance in fast skeletal muscles. In: Pette D (ed) Plasticity of muscle. Walter de Gruyter, Berlin New York, pp 401–408

    Google Scholar 

  • Hudlická O, Tyler KR, Srihari T, Heilig A, Pette D (1982) The effect of different patterns of long-term stimulation on contractile properties and myosin light chains in rabbit fast muscles. Pflügers Arch 393:164–170

    Google Scholar 

  • Ianuzzo CD, Patal P, Chen V, O'Brien P (1980) A possible thyroidal trophic influence on fast and slow skeletal muscle myosin. In: Pette D (ed) Plasticity of muscle. Walter de Gruyter, Berlin New York, pp 593–605

    Google Scholar 

  • Ingier F (1979) Effects of endurance training on muscle fibre ATPase activity, capillary supply and mitochondrial content in man. J Physiol (Lond) 294:419–432

    Google Scholar 

  • Jansson E, Sjödin B, Thorstensson A, Hultén B, Frith K (1978) Changes in muscle fibre type distribution in man after exercise. A sign of fibre type transformation? Acta Physiol Scand 104:235–237

    Google Scholar 

  • Kim DH, Wible GS, Witzmann FA, Fitts RH (1981) The effect of exercise training on sarcoplasmic reticulum function in fast and slow skeletal muscle. Life Sci 28:2671–2677

    Google Scholar 

  • Klug G, Reichmann H, Pette D (1983a) Rapid reduction in parvalbumin concentration during chronic stimulation of rabbit fast twitch muscle. FEBS Lett 152:180–182

    Google Scholar 

  • Klug G, Wiehrer W, Reichmann H, Leberer E, Pette D (1983b) Relationships between early alterations in parvalbumins, sarcoplasmic reticulum and metabolic enzymes in chronically stimulated fast twitch muscle. Pflügers Arch 399:280–284

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227:680–685

    Google Scholar 

  • Lehky P, Blum HE, Stein EA, Fischer EH (1974) Isolation and characterization of parvalbumins from skeletal muscle of higher vertebrates. J Biol Chem 249:4332–4334

    Google Scholar 

  • Nemeth P, Hofer HW, Pette D (1979) Metabolic heterogeneity of muscle fibres classified by myosin ATPase. Histochemistry 63:191–201

    Google Scholar 

  • Nemeth P, Pette D (1980) The interrelationship of two systems of fiber classification in rat EDL muscle. J Histochem Cytochem 28:193

    Google Scholar 

  • Nemeth P, Pette D (1981) Succinate dehydrogenase activity in fibres classified by myosin ATPase in three hind limb muscles of rat. J Physiol (Lond) 320:73–81

    Google Scholar 

  • Peter JB, Barnard RJ, Edgerton VR, Gillespie CA, Stempel KE (1972) Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11:2627–2633

    Google Scholar 

  • Pette D (ed) Plasticity of muscle. Walter de Gruyter, Berlin New York, 1980

    Google Scholar 

  • Pette D, Smith ME, Staudte HW, Vrbová G (1973) Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit muscles. Pflügers Arch 338:257–272

    Google Scholar 

  • Pette D, Müller W, Leisner E, Vrbová G (1976) Time dependent effects on contractile properties, fibre population, myosin light chains and enzymes of energy metabolism in intermittently and continuously stimulated fast twitch muscles of the rabbit. Pflügers Arch 364:103–112

    Google Scholar 

  • Pette D, Schnez U (1977a) Myosin light chain patterns of individual fast and slow-twitch fibres of rabbit muscles. Histochemistry 54:97–107

    Google Scholar 

  • Pette D, Schnez U (1977b) Coexistence of fast and slow type myosin light chains in single muscle fibres during transformation as induced by long term stimulation. FEBS Lett 83:128–130

    Google Scholar 

  • Pette D, Tyler KR (1983) Response of succinate dehydrogenase activity in fibres of rabbit tibialis anterior muscle to chronic nerve stimulation. J Physiol (Lond) 338:1–9

    Google Scholar 

  • Reichmann H, Pette D (1982) A comparative microphotometric study of succinate dehydrogenase activity levels in Type I, IIA and IIB fibres of mammalian and human muscles. Histochemistry 74:27–41

    Google Scholar 

  • Schantz P, Billeter R, Henriksson J, Jansson E (1982) Training-induced increase in myofibrillar ATPase intermediate fibers in human skeletal muscle. Muscle & Nerve 5:628–636

    Google Scholar 

  • Seedorf K, Seedorf U, Pette D (1983) Coordinate expression of alkali and DTNB myosin light chains during transformation of rabbit fast muscle by chronic stimulation. FEBS Lett 158:321–324

    Google Scholar 

  • Sréter FA, Gergely J, Salmons S, Romanul R (1973) Synthesis by fast muscle of myosin light chains characteristic of slow muscle in response to long-term stimulation. Nature New Biol (Lond) 241:17–19

    Google Scholar 

  • Sréter FA, Pinter K, Jolesz F, Mabuchi K (1982) Fast to slow transformation of fast muscles in response to long-term phasic stimulation. Exptl Neurol 75:95–102

    Google Scholar 

  • Staron RS, Hikida RS, Hagerman FC (1983) Reevaluation of human muscle fast-twitch subtypes: evidence for a continuum. Histochemistry 78:33–39

    Google Scholar 

  • Wiehrer W, Pette D (1983) The ratio between intrinsic 115,000-and 30,000-Mr peptides as a marker of fibre type specific sarcoplasmic reticulum in mammalian muscle. FEBS Lett 158:317–320

    Google Scholar 

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Green, H.J., Klug, G.A., Reichmann, H. et al. Exercise-induced fibre type transitions with regard to myosin, parvalbumin, and sarcoplasmic reticulum in muscles of the rat. Pflugers Arch. 400, 432–438 (1984). https://doi.org/10.1007/BF00587545

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