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Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers

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Summary

Single human muscle fibers were analysed using a combination of histochemical and biochemical techniques. Routine myofibrillar adenosine triphosphatase (mATPase) histochemistry revealed a continuum of staining intensities between the fast fiber types IIA and IIB (type IIAB fibers) after preincubation at pH 4.6. Electrophoretic analysis of single, histochemically-identified fibers demonstrated a correlation between the staining intensity and the myosin heavy chain (MHC) composition. All fibers classified as type I contained exclusively MHCI and all type IIA fibers contained only MHCIIa. Type IIAB fibers displayed variable amounts of both MHCIIa and MHCIIb; the greater the staining intensity of these fibers after preincubation at pH 4.6, the greater the percentage of MHCIIb. Those fibers histochemically classified as type IIB contained either entirely MHCIIb or, in addition to MHCIIb, a small amount of MHCIIa. These data establish a correlation between the mATPase activity and MHC content in single human muscle fibers.

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References

  • Bär A, Pette D (1988) Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett 235:153–155

    Google Scholar 

  • Bergström J (1962) Muscle electrolytes in man. Scand J Clin Lab Invest 14 [Suppl 68]:1–110

    Google Scholar 

  • Biral D, Betto R, Danieli-Betto D, Salviati G (1988) Myosin heavy chain composition of single fibres from normal human muscle. Biochem J 250:307–308

    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 

  • Danieli-Betto D, Zerbato E, Betto R (1986) Type I, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers. Biochem Biophys Res Commun 138:981–987

    Google Scholar 

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

    Google Scholar 

  • Klitgaard H, Zhou M, Richter EA (1990) Myosin heavy chain composition of single fibres from m. biceps brachii of male body builders. Acta Physiol Scand 140:175–180

    Google Scholar 

  • Oakley BR, Kirsch DR, Morris NR (1980) A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 105:361–363

    Google Scholar 

  • Pavlath GK, Rich K, Webster SG, Blau HM (1989) Localization of muscle gene products in nuclear domains. Nature 337:570–573

    Google Scholar 

  • Perrie WT, Bumford SJ (1986) Electrophoretic separation of myosin isoenzymes. Implications for the histochemical demonstration of fibre types in biopsy specimens of human skeletal muscle. J Neurol Sci 73:89–96

    Google Scholar 

  • Pette D, Staron RS (1988) Molecular basis of the phenotypic characteristics of mammalian muscle fibres. In: Evered D, Whalen J (eds) Plasticity of the neuromuscular system. John Wiley & Sons, Chichester New York Brisbane, pp 22–34

    Google Scholar 

  • Pette D, Staron RS (1990) Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 116:1–76

    Google Scholar 

  • Schiaffino S, Saggin L, Viel A, Gorza L (1985) Differentiation of fibre types in rat skeletal muscle visualized with monoclonal antimyosin antibodies. J Muscle Res Cell Motil 6:60–61

    Google Scholar 

  • Staron RS, Pette D (1986) Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers. Histochemistry 86:19–23

    Google Scholar 

  • Staron RS, Pette D (1987a) The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle. Biochem J 243:687–693

    Google Scholar 

  • Staron RS, Pette D (1987b) The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibers. Rabbit tibialis anterior muscle. Biochem J 243:695–699

    Google Scholar 

  • Staron RS, Pette D (1987c) Nonuniform myosin expression along single fibers of chronically stimulated and contralateral rabbit tibialis anterior muscles. Pflugers Arch 409:67–73

    Google Scholar 

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

    Google Scholar 

  • Staron RS, Hikida RS, Hagerman FC (1983b) Myofibrillar ATPase activity in human muscle fast-twitch subtypes. Histochemistry 78:405–408

    Google Scholar 

  • Staron RS, Hikida RS, Hagerman FC, Dudley GA, Murray TF (1984) Human skeletal muscle fiber type adaptatiblity to various workloads. J Histochem Cytochem 32:146–152

    Google Scholar 

  • Termin A, Staron RS, Pette D (1989) Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 92:453–457

    Google Scholar 

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Staron, R.S. Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers. Histochemistry 96, 21–24 (1991). https://doi.org/10.1007/BF00266756

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