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Further histochemical properties of rabbit skeletal muscle fibres

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Summary

The histochemical activities of succinic dehydrogenase (SDH), creatine kinase (CK), sarcoplasmic reticular ATPase (SR-ATPase) and myosin ATPase were studied in serial sections of rabbit adductor muscle. Three fibre types were distinguished depending upon the distribution of the enzyme activities. The type II “white” fibres posessing minimal SDH showed high myosin ATPase, SR-ATPase and ATPase dependent CK activities. “Red” oxidative fibres showing high SDH fell into two distinct groups: One category had mainly a peripheral localization of SDH and showed an enzymatic profile identical to that of type II white fibres. The second category of “red” fibres displayed both a homogeneous distribution of small diformazan granules throughout the fibre as well as a sub-sarcolemmal collection when tested for SDH activity but possessed very low amounts of reaction product of the various enzymes of the energetic metabolism studied. Since it is well established that the myosin ATPase of a fibre correlates with its contraction time, the present histochemical investigation provides further support for this concept by demonstrating the presence of high SR-ATPase and ATPase dependent CK activities in all white and red fibres rich in myosin ATPase.

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References

  • Ashmore, C. R., Doerr, L.: Oxidative metabolism in skeletal muscle of normal and dystrophic chicks. Biochem. Med. 4, 246–259 (1970).

    Google Scholar 

  • Ashmore, C. R., Doerr, L.: Comparative aspects of muscle fiber types in different species. Exp. Neurol. 31, 402–412 (1971).

    Google Scholar 

  • Ashmore, C. R., Tompkins, G., Doerr, L.: Comparative aspects of mitochondria isolated from αW, αR and βR muscle fibres of the chick. Exp. Neurol. 35, 413–120 (1972).

    Google Scholar 

  • Azzone, G. F., Carafoli, E., Museatello, U.: Biochemical properties of skeletal muscle mitochondria. II. The ATPase activity and the albumin effect. Exp. Cell Res. 21, 456–467 (1960).

    Google Scholar 

  • Barany, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol. 50, 197–218 (1967).

    Google Scholar 

  • Barany, M., Barany, K., Reckard, T., Volpe, A.: Myosin of fast and slow muscles of the rabbit. Arch. Biochem. Biophys. 109, 185–191 (1965).

    Google Scholar 

  • Barka, T., Anderson, P.: Histochemistry, theory, practice and bibliography, p. 313 New York: Harper Row Publishers, Inc. 1963.

    Google Scholar 

  • Barnard, R. J., Edgerton, V. R., Furukawa, T., Peter, J. B.: Histochemical, biochemical and contractile properties of red, white and intermediate fibres. Amer. J. Physiol. 220, 410–414 (1971).

    Google Scholar 

  • Baskin, R. J.: Ultrastructure and calcium transport in dystrophic chicken muscle microsomes. Lab. Invest. 23, 521–529 (1970).

    Google Scholar 

  • Baskin, R. J., Deamer, D. W.: A membrane bound creatine phosphokinase in fragmented sarcoplasmic reticulum. J. biol. Chem. 245, 1345–1347 (1970).

    Google Scholar 

  • Blanchaer, M. C.: Respiration of mitochondria of red and white skeletal muscle. Amer. J. Physiol. 206, 1015–1020 (1964).

    Google Scholar 

  • Brooke, M. H., Kaiser, K. K.: Muscle fiber types: How many and what kind? Arch. Neurol. (Chic.) 23, 369–370 (1970).

    Google Scholar 

  • Buller, A. J., Mommaerts, W. F. H. M.: Myofibrillar adenosine triphosphatase as a determining factor for contractile velocity. Its changes upon experimental cross-innervation. J. Physiol. (Lond.) 201, 46p (1969).

    Google Scholar 

  • Buller, A. J., Mommaerts, W. F. H. M., Seraydarian, K.: Neural control of myofibrillar ATPase activity in rat skeletal muscle. Nature (Lond.) 233, 31–32 (1971).

    Google Scholar 

  • Burke, R. E., Levine, D. N., Zajac, F. E., Tsairis, P., Engel, W. K.: Mammalian motor units: Physiological-histochemical correlation in three types in cat gastrocnemius. Science 174, 709–712 (1971).

    Google Scholar 

  • Dubowitz, V., Pearse, A. G. E.: A comparative histochemical study of oxidative enzyme and phosphorylase activity in skeletal muscle. Histochemie 2, 105–117 (1960).

    Google Scholar 

  • Ebashi, S., Lipmann, F.: Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J. Cell Biol. 14, 389–398 (1962).

    Google Scholar 

  • Edgerton, V. R., Simpson, D. R.: The intermediate muscle fiber of rats and guinea pigs. J. Histochemie Cytochem. 17, 888–838 (1969).

    Google Scholar 

  • Edgerton, V. R., Simpson, D. R.: Dynamic and metabolic relationships in the rat extensor digitorum longus muscle. Exp. Neurol. 30, 374–376 (1971).

    Google Scholar 

  • Engel, W. K.: The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease. Neurology (Minneap.) 12, 778–794 (1962).

    Google Scholar 

  • Gauthier, G. F.: On the localization of sarcotubular ATPase activity in mammalian skeletal muscle. Histochemie 11, 97–111 (1967).

    Google Scholar 

  • Gauthier, G. F., Padykula, H. A.: Cytochemical studies of adenosine triphosphatase activity in the sarcoplasmic reticulum. J. Cell Biol. 27, 252–260 (1965).

    Google Scholar 

  • Gillespie, C. A., Simpson, D. R., Edgerton, V. R.: High glycogen content of rat as opposed to white skeletal muscle fibers of guinea pigs. J. Histochem. Cytochem. 18, 552–558 (1970).

    Google Scholar 

  • Hall-Craggs, E. C. B.: The contraction times and enzyme activity of two rabbit laryngeal muscles. J. Anat. (Lond.) 102, 241–155 (1968).

    Google Scholar 

  • Keutel, H. J., Okabe, K., Jacobs, H. K., Ziter, F., Maland, L., Kuby, S. A.: Studies on adenosine triphosphate transphosphorylases. XI. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylases from the muscle and brain of man, calf and rabbit; and a preparation of their enzymatically active hybrids. Arch. Biochem. Biophys. 150, 648–678 (1972).

    Google Scholar 

  • Khan, M. A., Holt, P. G., Knight, J. O., Kakulas, B. A.: Incubation film technique for the histochemical localization of creatine kinase. Histochemie 26, 120–125 (1971).

    Google Scholar 

  • Khan, M. A., Holt, P. G., Papadimitriou, J. M., Knight, J. O., Kakulas, B. A.: Creatine kinase, a histochemical study by the gelatin film-lead precipitation technique. Histochemie 32, 49–58 (1972a).

    Google Scholar 

  • Khan, M. A., Papadimitriou, J. M., Holt, P. G., Kakulas, B. A.: A calcium citro-phosphate technique for the histochemical localization of myosin ATPase. Stain Technol. 47, 277–281 (1972b).

    Google Scholar 

  • Khan, M. A., Papadimitriou, J. M., Holt, P. G., Kakulas, B. A.: A modified histochemical technique for sarcoplasmic reticular ATPase. Histochemie 30, 329–333 (1972c).

    Google Scholar 

  • Khan, M. A., Papadimitriou, J. M., Holt, P. G., Kakulas, B. A.: A histochemical analysis of mammalian oxidative skeletal muscle fibers using the enzymes of energetic metabolism. Histochemie 33, 301–312 (1973).

    Google Scholar 

  • Kielly, W. A.: Mitochondrial ATPase. In: Methods in enzymology, eds. S. P. Colowich and N. O. Kaplan, vol. 2., p. 593–595. New York: Academic Press 1955.

    Google Scholar 

  • Kuby, S. A., Noda, L., Lardy, H. A.: Adenosine triphosphate creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. biol. Chem. 209, 191–201 (1954a).

    Google Scholar 

  • Kuby, S. A., Noda, L., Lardy, H. A.: Adenosine triphosphate creatine transphosphorylase. III. Kinetic studies. J. biol. Chem. 210, 65–82 (1954b).

    Google Scholar 

  • Lorand, L., Molnar, J.: In: Muscle as a tissue, 1960 conference, eds. K. Rodahl and S. W. Horvath, p. 97. New York: McGraw-Hill 1962.

    Google Scholar 

  • Lorand, L., Schuel, H., Demovsky, R. A., Messler, J.: In: Molecular biology of muscle contraction, eds. S. Ebashi, F. Oosawa, T. Sekine, and Y. Tonomura, p. 160–162. New York: Elsevier Publishing Co. 1965.

    Google Scholar 

  • MacLennan, D. H.: Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J. biol. Chem. 245, 4508–4518 (1970).

    Google Scholar 

  • Mahowald, T. A., Noltmann, E. A., Kuby, S. A.: Studies on adenosine triphosphate transphosphorylases. III. Inhibition reactions, J. biol. Chem. 237, 1532–1542 (1962).

    Google Scholar 

  • Maier, A., Eldred, E., Edgerton, V. R.: Types of muscle fibres in the extraocular muscles of birds. Exp. Eye Res. 13, 255–265 (1972).

    Google Scholar 

  • Martonosi, A., Feretos, R.: Sarcoplasmic reticulum. I. The uptake of Ca++ by sarcoplasmic reticulum. II. Correlation between adenosine triphosphatase activity and Ca++ uptake. J. biol. Chem. 239, 648–688 (1964).

    Google Scholar 

  • Noda, L., Kuby, S. A., Lady, H.: ATP-creatine transphosphorylase. In: Methods in enzymology, eds. S. P. Colowich and N. O. Kaplan, vol.2, p. 605–610. New York: Academic Press 1955.

    Google Scholar 

  • Padykula, H. A., Gauthier, G. F.: Cytochemical studies of adenosinetriphosphatases in skeletal muscle fibers. J. Cell Biol. 18, 87–107 (1963).

    Google Scholar 

  • Peter, J. B., Barnard, R. J., Edgerton, V. R., Gillespie, C. A., Stempel, K. E.: Metabolic profiles of three fibre types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11, 2627–2633 (1972).

    Google Scholar 

  • Pette, D.: In: Regulation of matabolic processes in mitochondria, eds. J. M. Tager, S. Papa, E. Quagliariello and E. C. Slater, p. 28, Amsterdam: Elsevier Publication Co. 1966.

    Google Scholar 

  • Schulze, W., Wollenberger, A.: Elektronmicroskopischer Nachweis von mitochondialer adenosinetriphosphataseaktivitat in tierischen Geweben. Histochemie 5, 417–429 (1965).

    Google Scholar 

  • Stein, J. M., Padykula, H. A.: Histochemical classification of individual skeletal muscle fibers of the rat. Amer. J. Anat. 110, 103–123 (1962).

    Google Scholar 

  • Syrovy, I., Gutmann, E.: ATPase activity of two rabbit latyngeal muscles. Experientia (Basel) 27, 242 (1971).

    Google Scholar 

  • Yellin, H.: Differences in histochemical attributes between diaphragm and hind leg muscles of the rat. Anat. Rec. 173, 333–340 (1972).

    Google Scholar 

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Khan, M.A., Papadimitriou, J.M., Holt, P.G. et al. Further histochemical properties of rabbit skeletal muscle fibres. Histochemie 36, 173–183 (1973). https://doi.org/10.1007/BF00304392

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