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Fine structural morphology and ATP-ase reaction in heart muscle at various sarcomere lengths

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Zeitschrift für Zellforschung und mikroskopische Anatomie Abt. Histochemie Aims and scope Submit manuscript

Summary

The fine structural morphology and the ATP-ase activity of heart muscle at various sarcomere lengths was studied. ATP-ase activity was found on endothelial cells, cell membrane, intercalated disc, sarcoplasmic reticulum and in the Z-line region. It appeared that the activity of the ATP-splitting in the Z-line region was sensitive to PCMB and could be reactivated with cysteine. This points to an activity of “true” ATP-ase according to the terminology ofPadykula et al. (1955) andFreiman et al. (1960). In addition, this cross striational enzyme was strongly activated by Mg++.

At intermediate sarcomere lengths and in hypercontraction no I-zones or H-zones were visible, while at intermediate sarcomere lengths and M-line was faintly indicated. In the stretched muscle, both I- and H-zones and N- and M-lines were present. In comparison with muscle tissue with intermediate sarcomere lengths, the Cz-bands of hypercontraction had markedly broadened, whereas in stretched muscle a relatively sharply defined electron-dispersing line indicated the presence of a Z-line.

The localization and spread of the precipitate formed as a result of ATP-ase activity changes with alterations of the sarcomere lengths exclusively in the Z-line region.

The probable identity of the Z-line region ATP-ase with Actomyosin is discussed.

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Literature

  • Bárány, M., andK. Bárány: Studies on “active centers” ofl-Myosin. Biochim. biophys. Acta (Amst.)35, 293–309 (1959).

    Google Scholar 

  • Barron, E. S. G.: Thiol groups of biological importance. Advanc. Enzymol.11, 201–266 (1951).

    Google Scholar 

  • Beyer, J. M. de, J. C. H. de Man andJ.-P. Persijn: ATP-ase activity on the intercalated disc and Cz bands of mouse heart muscle. J. Cell Biol.13, 452–456 (1962).

    Google Scholar 

  • Fawcett, D. W.: The sarcoplasmic reticulum of skeletal and cardiac muscle. Circulation24, 336–348 (1961).

    Google Scholar 

  • ——, andC. C. Selby: Observations on the fine structure of the turtle atrium. J. biophys. biochem. Cytol.4, 63–72 (1958).

    Google Scholar 

  • Freiman, D. G., andN. Kaplan: Studies on the histochemical differentiation of enzymes hydrolyzing adenosine triphosphate. J. Histochem. Cytochem.8, 159–170 (1960).

    Google Scholar 

  • Hanson, J., andH. E. Huxley: Structural basis of the cross-striations in muscle. Nature (Lond.)172, 530–532 (1953).

    Google Scholar 

  • Hasselbach, W.: Elektronenmikroskopische Untersuchungen an Muskelfibrillen bei totaler und partieller Extraktion desl-Myosins. Z. Naturforsch.8b, 449–454 (1953).

    Google Scholar 

  • Hodge, A. J.: Fibrous proteins of muscle. Rev. mod. Physics31, 409–425 (1959).

    Google Scholar 

  • Huxley, H. E.: Electronmicroscope studie's of the organisation of the filaments in striated muscle. Biochim. biophys. Acta (Amst.)12, 387–394 (1953).

    Google Scholar 

  • —— The double array of filaments in cross-striated muscle. J. biophys. biochem. Cytol.3, 631–648 (1957).

    Google Scholar 

  • Huxley, H. E.: Muscle cells. The Cell, vol. IV, pp. 365–481. New York: Academic Press 1960.

    Google Scholar 

  • —— The contractile structure of cardiac and skeletal muscle. Circulation24, 328–335 (1961).

    Google Scholar 

  • ——, andJ. Hanson: Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature (Lond.)173, 973, 976 (1954).

    Google Scholar 

  • Kielley, W. W., andO. Meyerhof: Studies on adenosinetriphosphatase of muscle. J. biol. Chem.176, 591–601 (1948).

    Google Scholar 

  • Morales, M. F., andS. Watanabe: The ATPases of muscle proteins. Circulation24, 390–398 (1961).

    Google Scholar 

  • Padykula, H. A., andE. J. Herman: The specificity of the histochemical method for adenosine triphosphate. J. Histochem. Cytochem.3, 170–195 (1955).

    Google Scholar 

  • Persijn, J.-P., W. Th. Daems, J. C. H. de Man andA. E. F. H. Meijers: The demonstration of adenosinetriphosphatase activity with the electronmicroscope. Histochemie2, 372–382 (1961).

    Google Scholar 

  • Singer, T. P., andE. S. G. Barron: Effect of sulfhydryl reagents on adenosine triphosphatase activity of myosin. Proc. Soc. exp. Biol. (N.Y.)56, 120–124 (1944).

    Google Scholar 

  • Stenger, R. J., andD. Spiro: The ultrastructure of mammalian cardiac muscle. J. biophys. biochem. Cytol.9, 325–352 (1961).

    Google Scholar 

  • Szent-Györgyi, A.: Chemistry of muscular contraction. New York: Academic Press 1947.

    Google Scholar 

  • Tice, L. W., andR. J. Barrnett: The adenosinetriphosphatases of striated muscle. J. Histochem. Cytochem.8, 352 (1960).

    Google Scholar 

  • —— —— Fine structural localization of adenosinetriphosphatase activity in heart muscle myofibrils. J. Cell Biol.15, 401–416 (1962).

    Google Scholar 

  • Wachstein, M., andE. Meisel: Histochemistry of hepatic phosphatases at a physiologicph. Amer. J. Path.27, 13–23 (1957).

    Google Scholar 

  • Willighagen, R. G. J.: Histochemisch onderzoek van enzymen in gezwellen. Ned. T. Geneesk.105, 412–418 (1961).

    Google Scholar 

  • --R. O. van der Heul andTh. G. van Rijssel: In press 1963.

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With 12 Figures in the Text

With technical assistance of Mr.W. Beens, MissA. J. v. Paridon and MissR. M. Meinders.

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de Man, J.C.H., de Beyer, J.M. & Persijn, J.P. Fine structural morphology and ATP-ase reaction in heart muscle at various sarcomere lengths. Histochemie 3, 269–282 (1963). https://doi.org/10.1007/BF00736444

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  • DOI: https://doi.org/10.1007/BF00736444

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