Isomyosins and Isoactins in Mammalian Myocardium

  • J. J. Mercadier
  • A. M. Lompre
  • D. de la Bastie
  • J. L. Samuel
  • B. Swynghedauw
  • L. Rappaport
  • K. Schwartz
Part of the Developments in Cardiovascular Medicine book series (DICM, volume 66)


Myosin and actin are the major components of the thick and the thin filaments of the sarcomere, respectively. The existence of several isomyosins with different heavy chains and different enzymatic activities was demonstrated more than 20 years ago when adult fast-twitch and slow-twitch muscles were compared to cardiac ventricular tissue and it is clear now that the sarcomeric myosin heavy chains (MHC) are coded by a highly conserved multigene family (l). The classical experiments of Barany (2) who showed that maximal velocity of a given muscle fiber is correlated to the ATPase activity of its constituent myosin, and of Buller, Eccles and Eccles (3) in which the nerve was shown to modulate the properties of a muscle, opened an exciting new era in muscle research and neurobiology.


Myosin Heavy Chain Mitral Stenosis Thin Filament Cardiac Gene White Syndrome 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Nguyen, H.T., Gubits, R.M., Wydro, R.M. and Nadal-Ginard, B. Proc. Natl. Acad. Sci. USA 79: 5230–5234, 1982.PubMedCrossRefGoogle Scholar
  2. 2.
    Barany, M. J. Gen. Physiol. 150: 197–216, 1967.CrossRefGoogle Scholar
  3. 3.
    Buller, A.J., Eccles, J.C. and Eccles, R.M. J. Physiol. 150: 417–439, 1960.PubMedGoogle Scholar
  4. 4.
    Hoh, J.F.Y., McGrath, P.A. and Hale, P.T. J. Mol. Cell. Cardiol. 10: 1053–1076, 1978.PubMedCrossRefGoogle Scholar
  5. 5.
    Schwartz, K. and Mercadier, J.J. In: The Developing Heart (Ed. M. Legato), Martinus Nijhoff Publishing, Boston, The Hague, Dordrecht, Lancaster, 1984, pp. 149–171.Google Scholar
  6. 6.
    Schwartz, K., Lecarpentier, Y., Martin, J.L., Lompré, A.M., Mercadier, J.J. and Swynghedauw, B. J. Moll. Cell. Cardiol. 13: 1071–1075, 1981.CrossRefGoogle Scholar
  7. 7.
    Alpert, N.R. and Mulieri, L.A. Circ. Res. 50: 491–500, 1982.PubMedGoogle Scholar
  8. 8.
    Goldman, S., Olajos, M. and Morkin, E. Cardiovasc. Res. 18: 604–612, 1984.PubMedCrossRefGoogle Scholar
  9. 9.
    Yazaki, Y., Ueda, S., Nagai, R. and Shimada, K. Circ. Res. 45: 522–527, 1979.PubMedGoogle Scholar
  10. 10.
    Buckingham, M.E. Essays in Biochemistry 20: 77–109, 1985.PubMedGoogle Scholar
  11. 11.
    Mayer, Y., Czosnek, H., Zeelon, P.E., Yaffe, D. and Nudel, U. Nucleic Acids Res. 12: 1087–2000, 1984.PubMedCrossRefGoogle Scholar
  12. 12.
    Minty, A.J., Alonso, S., Caravatti, M. and Buckingham, M.E. Cell 30: 185–192, 182.Google Scholar
  13. 13.
    Lompre, A.M., Schwartz, K., d’Albis, A., Lacombe, G., Van Thiem, N.G. and Swynghedauw, B. Nature 282: 105–107, 1979.PubMedCrossRefGoogle Scholar
  14. 14.
    Litten, R.Z., Martin, B.J., Low, R.B. and Alpert, N.R. Circ Res. 50: 856–864, 1982.PubMedGoogle Scholar
  15. 15.
    Mercadier, J.J., Bouveret, P., Gorza, L., Schiaffino, S., Clark, W.A., Zak, R., Swynghedauw, B. and Schwartz, K. Circ. Res. 53: 52–62, 1983.PubMedGoogle Scholar
  16. 16.
    Gorza, L., Mercadier, J.J., Schwartz, K., Thornell, L.E. Sartore, S. and Schiaffino, S. Circ. Res. 54: 694–702, 1984.PubMedGoogle Scholar
  17. 17.
    Tsuchimochi, H., Sugi, M., Kuro-o, M., Ueda, S., Takaku, F., Furuta, S.I., Shirai, T. and Yazaki, Y. J. Clin. Invest. 74: 662–665, 1984.PubMedCrossRefGoogle Scholar
  18. 18.
    Bouvagnet, P., Léger, J., Dechesne, C.A., Dureau, G., Anoal, M. and Legér, J.J. Circulation 72: 272–279, 1985.PubMedCrossRefGoogle Scholar
  19. 19.
    Schwartz, K. and Mercadier, J.J. In: Methods of Enzymatic Analysis (Ed. U.V. Bergmeyers), VHC, Weinheim, vol.IV, 1986, pp. 225–238.Google Scholar
  20. 20.
    Izumo, S., Nadal-Ginard, B. and Mahdavi, V. Science 231: 597–600, 1986.PubMedCrossRefGoogle Scholar
  21. 21.
    Chizzonite, R.A., Everett, A.W., Prior, G. and Zak, R. J. Biol. Chem. 259: 15564–15571, 1984.PubMedGoogle Scholar
  22. 22.
    Banerjee, S.K. Circ. Res. 52: 131–136, 1983.PubMedGoogle Scholar
  23. 23.
    Samuel, J.L., Rappaport, L., Syrovy, I., Wisnewsky, C, Marotte, F., Whalen, R.G. and Schwartz, K. Am. J. Physiol. 250: 331–341, 1986.Google Scholar
  24. 24.
    Vandekerckhove, J., Bugaisky, G. and Buckingham, M. J. Biol. Chem. 241: 1836–1843, 1986.Google Scholar
  25. 25.
    Gunning, P., Ponte, P., Blau, H. and Kedes, L. Molec. Cell. Biol. 3: 1985–1995, 1983.PubMedGoogle Scholar
  26. 26.
    Schwartz, K., de la Bastie, D., Bouveret, P., Oliviero, P., Alonso, S. and Buckingham, M. Circ. Res. in press.Google Scholar
  27. 27.
    Alonso, S., Minty, A., Bourlet, Y. and Buckingham, M.E. J. Mol. Evol. 23 in press, 1986.Google Scholar

Copyright information

© Martinus Nijhoff Publishing, Boston 1987

Authors and Affiliations

  • J. J. Mercadier
    • 1
  • A. M. Lompre
    • 1
  • D. de la Bastie
    • 1
  • J. L. Samuel
    • 1
  • B. Swynghedauw
    • 1
  • L. Rappaport
    • 1
  • K. Schwartz
    • 1
  1. 1.Unité 127 I.N.S.E.R.MHopital LariboisièreParisFrance

Personalised recommendations