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Fibre size and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle

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Abstract

Cross-sectional area (CSA), succinate dehydrogenase (SDH), and α-glycerophosphate dehydrogenase (GPD) activities were measured in single fibres of adult rat medial gastrocnemius muscle (deep region) using quantitative histochemical procedures. The same fibres were identified in serial sections stained by immunohistochemistry with monoclonal antibodies specific for selected myosin heavy chain (MyHC) isoforms. The values of CSA, SDH and GPD activities formed a continuum, but significant differences in mean values were observed among fibre types of presumed homogeneous MyHC content. Type IIA fibres were the smallest, type IIB fibres were the largest, and type I and IIX fibres were intermediate. Type IIA fibres had the highest SDH activity, followed in rank order by type IIX, type I and type IIB. The average GPD activity was ranked according to fibre type such that IIB>IIX>IIA>I. Hybrid fibres co-expressing two MyHC isoforms generally showed intermediate mean CSA, SDH a nd GPD values lying between their respective pure MyHC fibre types. Across all fibres, there was an inverse relationship between SDH activity and CSA and between GPD and SDH activities, and a positive correlation between GPD and CSA. Moreover, a significant interdependence between CSA, SDH activity, GPD activity and MyHC content existed on a fibre-to-fibre basis, suggesting that the MyHC isoform expressed in a fibre is associated with differences in size, oxidative and glycolytic capabilities of muscle fibres. In fact, most of the fibres could be discriminated into discrete groups with the same MyHC content when their CSA, SDH and GPD values were considered together.

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References

  • ARMSTRONG, R. B. & PHELPS, R. O. (1984) Muscle fibre composition of the rat hindlimb. Am. J. Anat. 171, 259–72.

    Google Scholar 

  • BLANCO, C. E., MICEVYCH, P. E., ZHAN, W. Z. & SIECK, G. C. (1995) Succinate dehydrogenase activity of sexually dimorphic muscles of rats. J. Appl. Physiol. 78, 2147–52.

    Google Scholar 

  • BLANCO, C. E., SIECK, G. C. & EDGERTON, V. R. (1988) Quantitative histochemical determination of succinic dehydrogenase activity in skeletal muscle fibres. Histochem. J. 20, 230–43.

    Google Scholar 

  • BOTTINELLI, R., BETTO, R., SCHIAFFINO, S. & REGGIANI, C. (1994) Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle. J. Muscle Res. Cell Motil. 15, 413–19.

    Google Scholar 

  • BROOKE, M. H. & KAISER, K. K. (1970) Three ''myosin adenosine triphosphatase'' systems: the nature of their pH lability and sulfhydryl dependence. J. Histochem. Cytochem. 18, 670–2.

    Google Scholar 

  • DELP, M. D. & DUAN, C. (1996) Composition and size of type I, IIA, IID/X, and IIB fibres and citrate synthase activity of rat muscle. J. Appl. Physiol. 80, 261–70.

    Google Scholar 

  • ENAD, J. G., FOURNIER, M. & SIECK, G. C. (1989) Oxidative capacity and capillary density of diaphragm motor units. J. Appl. Physiol. 67, 620–27.

    Google Scholar 

  • GORZA, L. (1990) Identification of a novel type 2 fibre population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies. J. Histochem. Cytochem. 38, 257–65.

    Google Scholar 

  • JARVIS, J. C., BROWNSON, C., SUTHERLAND, H. & SALMONS, S. (1991) Comparison between the effects of continuous long-term stimulation of rabbit skeletal muscle at 2.5 Hz and 10 Hz. In Basic and Applied Myology: Perspectives for the 90s (edited by CARRARO, U. & SALMONS, S.) pp. 109–13. Padova: Unipress.

    Google Scholar 

  • JIANG, B., ROY, R. R. & EDGERTON, V. R. (1990) Enzymatic plasticity of medial gastrocnemius fibres in the adult chronic spinal cat. Am. J. Physiol. 259, C507–14.

    Google Scholar 

  • LARSSON, L. (1992) Is the motor unit uniform? Acta Physiol. Scand. 144, 143–54.

    Google Scholar 

  • MARTIN, T. P., BODINE-FOWLER, S., ROY, R. R., ELDRED, E. & EDGERTON, V. R. (1988a) Metabolic and fibre size properties of cat tibialis anterior motor units. Am. J. Physiol. 255, C43–50.

    Google Scholar 

  • MARTIN, T. P., BODINE-FOWLER, S. & EDGERTON, V. R. (1988b) Co-ordination of electromechanical and meta-Quantitative histochemistry in rat muscle 741 bolic properties of cat soleus motor units. Am. J. Physiol. 255, C684–93.

    Google Scholar 

  • MARTIN, T. P., VAILAS, A. C., DURIVAGE, J. B., EDGERTON, V. R. & CASTLEMAN, K. R. (1985) Quantitative histochemical determination of muscle enzymes: biochemical verification. J. Histochem. Cytochem. 33, 1053–9.

    Google Scholar 

  • NEMETH, P. M., SOLANSKI, L., GORDON, D. A., HAMM, T. M., REINKING, R. M. & STUART, D. G. (1986) Uniformity of metabolic enzymes within individual motor units. J. Neurosci. 6, 892–8.

    Google Scholar 

  • PETTE, D. & STARON, S. (1990) Cellular and molecular diversities of mammalian skeletal muscle fibres. Rev. Physiol. Biochem. Pharmacol. 116, 1–76.

    Google Scholar 

  • PETTE, D. & SPAMER, C. (1986) Metabolic properties of muscle fibres. Fed. Proc. 45, 2910–14.

    Google Scholar 

  • PIEROTTI, D. J., ROY, R. R., HODGSON, J. A. & EDGERTON, V. R. (1994) Level of independence of motor unit properties from neuromuscular activity. Muscle Nerve 17, 1324–35.

    Google Scholar 

  • RIVERO, J. L. L., TALMADGE, R. J. & EDGERTON, V. R. (1996) Correlation between myofibrillar ATPase activity and myosin heavy chain composition in equine skeletal muscle and the influence of training. Anat. Rec. 246, 195–207.

    Google Scholar 

  • SAS INSTITUTE (1986) SAS User's Guide: Statistics, pp. 139–200. Cary, NC: SAS Institute.

    Google Scholar 

  • SCHIAFFINO, S., GORZA, L., SARTORE, S., SAGGIN, L., AUSONI, S., VIANELLO, M., GUNDERSEN, K. & LOMO, T. (1989) Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J. Muscle Res. Cell Motil. 10, 197–205.

    Google Scholar 

  • SCHIAFFINO, S. & REGGIANI, C. (1996) Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76, 371–423.

    Google Scholar 

  • SIECK, G. C., ZHAN, W., PRAKASH, Y. S., DAOOD, M. J. & WATCHKO, J. F. (1995) SDH and actomyosin ATPase activities of different fibre types in rat diaphragm muscle. J. Appl. Physiol. 79, 1629–39.

    Google Scholar 

  • SPURWAY, N. C. (1980) Histochemical typing of muscle fibres by microphotometry. In Plasticity of Muscle (edited by PETTE, D.) pp. 31–44. Berlin: de Gruyter.

    Google Scholar 

  • SPURWAY, N. C., MURRAY, M. G., GILMOUR, W. H. & MONTGOMERY, I. (1996) Quantitative skeletal muscle histochemistry of four East African ruminants. J. Anat. 188, 455–72.

    Google Scholar 

  • TALMADGE, R. J., ROY, R. R. & EDGERTON, V. R. (1993) Muscle fiber types and function. Curr. Opin. Rheumatol. 5, 695–705.

    Google Scholar 

  • VAN DER LAARSE, W. J., LANNERGREN, J. & DIEGENBACH, P. C. (1991) Resistance to fatigue of single muscle fibres from Xenopus related to succinate dehydrogenase and myofibrillar ATPase activities. Exp. Physiol. 76, 589–96.

    Google Scholar 

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Rivero, JL.L., Talmadge, R.J. & Edgerton, V.R. Fibre size and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle. J Muscle Res Cell Motil 19, 733–742 (1998). https://doi.org/10.1023/A:1005482816442

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