Advertisement

The Role of the Interaction of Ca2+ with Troponin in the Regulation of Muscle Contraction

  • J. D. Potter
  • B. Nagy
  • J. H. Collins
  • J. C. Seidel
  • P. Leavis
  • S. S. Lehrer
  • J. Gergely
Conference paper
Part of the 26. Colloquium der Gesellschaft für Biologische Chemie 10.–12. April 1975 in Mosbach/Baden book series (MOSBACH, volume 26)

Abstract

In introducing this paper, that is dedicated to the memory of Professor H.H. Weber and deals with some aspects of the interaction of calcium and one of the regulatory proteins of muscle, it is fitting to recall that the Institute of which Professor Weber was Director pioneered in the development of our current concepts concerning the regulation of muscle contraction by Ca2+. This is attested to in greater detail by Professor Hasselbach's paper at this Symposium; it is also a pleasant duty to recall that it was the work of Annemarie Weber, independently carried out in the United States, that played a key role in bringing to light the important function of the free Ca2+ concentration in the regulation of actinmyosin interaction. Her work, and that of Ebashi and his colleagues (for reviews see Ebashi and Endo, 1968; Ebashi et al., 1969; Weber and Murray, 1973) led to the clear recognition that the interaction of aetin and myosin, the key step in the contraction process, depends on tiny amounts of free Ca++. Ebashi and his colleagues went on to show that while the system consisting of purified actin and myosin had no calcium sensitivity, in the presence of what at first was known as native tropomyosin the interaction between actin and myosin — reflected in superprecipitation and actin activation of myosin ATPase in the presence of Mg2+ — is dependent on Ca++. Native tropomyosin was soon recognized to consist of Bailey's tropomyosin (1948) and a new entity for which the name troponin (Tn) was coined (Ebashi and Kodama, 1965; Ebashi et al., 1972).

Keywords

ATPase Activity Cold Spring Harbor Spin Label Calcium Binding Protein High Affinity Site 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bailey, K.: Biochem. J. 43, 271–279 (1948).Google Scholar
  2. Balint, M., Sreter, F.A., Wolf, I., Nagy, B., Gergely, J.: J. Biol. Chem. 250, 6168–6177 (1975).PubMedGoogle Scholar
  3. Barker, W.C., Dayhoff, M.O. : Biophys. J. 15, 121a (1975).Google Scholar
  4. Bremel, R.D., Murray, J.M., Weber, A.: Cold Spring Harbor Symp. Quant. Biol. 37, 267–275 (1972).Google Scholar
  5. Bremel, R.D., Weber, A.: Nature (New Biol.) 238, 97–101 (1972).Google Scholar
  6. Bremel, R.D., Weber, A.: Biochim. Biophys. Acta 376, 366–374 (1975).PubMedCrossRefGoogle Scholar
  7. Cohen, C, Caspar, D.L.D., Johnson, J.P., Nauss, K., Margossian, S.S., Parry, D.A.D.: Cold Spring Harbor Symp. Quant. Biol. 37, 287–297 (1972).Google Scholar
  8. Collins, J.H.: Biochem. Biophys. Res. Commun. 58, 301–308 (1974).PubMedCrossRefGoogle Scholar
  9. Collins, J.H.: Fed. Proc. 34, 539 (1975).Google Scholar
  10. Collins, J.H., Potter, J.D., Horn, M.J., Wilshire, G., Jackman, N.: FEBS Lett. 36, 268–272 (1973).PubMedCrossRefGoogle Scholar
  11. Drabikowski, W., Barylko, B. : Acta Biochem. Polonica 18 ,353–366 (1971).Google Scholar
  12. Ebashi, S., Endo, M.: Progr. Biophys. Molec. Biol. 18, 123–183 (1968).CrossRefGoogle Scholar
  13. Ebashi, S., Endo, M., Ohtsuki, I.: Quart. Rev. Biophysics 2, 351–384 (1969).CrossRefGoogle Scholar
  14. Ebashi, S., Kodama, A.: J. Biochem. 58, 107–108 (1965).PubMedGoogle Scholar
  15. Ebashi, S., Kodama, A., Ebashi, F.: J. Biochem. 58, 465–477 (1968).Google Scholar
  16. Ebashi, S., Ohnishi, S., Abe, S., Maruyama, K.: J. Biochem. 75, 211–213 (1974).PubMedGoogle Scholar
  17. Ebashi, S., Ohtsuki, I., Mihashi, K.: Cold Spring Harbor Symp. Quant. Biol. 37, 215–223 (1972).Google Scholar
  18. Ellman, G.L.: Arch. Biochem. Biophys. 82, 70–77 (1959).PubMedCrossRefGoogle Scholar
  19. Fuchs, F.: Int. J. Peptide Res. 4, 147–149 (1972).CrossRefGoogle Scholar
  20. Fuchs, F., Briggs, F.N. : J. Gen. Physiol. 51, 655–676 (1968).PubMedCrossRefGoogle Scholar
  21. Gaffin, L., Oplatka, A.: J. Biochem. 75, 277–281 (1974).PubMedGoogle Scholar
  22. Greaser, M.L., Gergely, J.: J. Biol. Chem. 246, 4226–4233 (1971).PubMedGoogle Scholar
  23. Greaser, M.L., Gergely, J.: J. Biol. Chem. 248, 2125–2133 (1973).PubMedGoogle Scholar
  24. Greaser, M.L., Yamaguchi, M., Brekke, C., Potter, J., Gergely, J.: Cold Spring Harbor Symp. Quant. Biol. 37, 235–244 (1972).Google Scholar
  25. Gruda, J., Therien, H.M., Lermakian, E.: Biochem. Biophys. Res. Commun. 52, 1307–1313 (1973).PubMedCrossRefGoogle Scholar
  26. Hartshorne, D.J., Pyun, H.Y.: Biochim. Biophys. Acta 229, 698–711 (1971).PubMedGoogle Scholar
  27. Haselgrove, J.C.: Cold Spring Harbor Symp. Quant. Biol. 37, 341–352 (1972).Google Scholar
  28. Haselgrove, J.C.: J. Molec. Biol. 92, 113–143 (1975).PubMedCrossRefGoogle Scholar
  29. Head, J.F., Perry, S.V.: Biochem. J. 137, 145–154 (1974).PubMedGoogle Scholar
  30. Hellam, D.C., Podolsky, R.J.: J. Physiol. 200, 807–819 (1969).PubMedGoogle Scholar
  31. Hitchcock, S.E.: Eur. J. Biochem. 52, 255–263 (1975).PubMedCrossRefGoogle Scholar
  32. Hitchcock, S.E., Huxley, H.E., Szent-Györgyi, A.G.: J. Molec. Biol. 80, 825–836 (1973).PubMedCrossRefGoogle Scholar
  33. Huxley, H.E.: Cold Spring Harbor Symp. Quant. Biol. 37, 361–376 (1972).Google Scholar
  34. Julian, F.J.: J. Physiol. 218, 117–145 (1971).PubMedGoogle Scholar
  35. Kawasaki, Y., Van Eerd, J.P. : Biochem. Biophys. Res. Commun. 49, 898 to 905 (1972) .PubMedCrossRefGoogle Scholar
  36. Kendrick-Jones, J.: Nature 249, 631–634 (1974).PubMedCrossRefGoogle Scholar
  37. Kerrick, W., Donaldson, S.: Biochim. Biophys. Acta 275, 117–122 (1972).PubMedCrossRefGoogle Scholar
  38. Klotz, I.M. : Accounts of Chemical Res. 7, 162–168 (1974).CrossRefGoogle Scholar
  39. Kretsinger, R.H.: In: Perspectives in Membrane Biology (eds. S. Estra-da-O, C. Gitler), pp. 229–262. New York: Academic Press 1974.Google Scholar
  40. Kretsinger, R.H., Barry, CD.: Biochim. Biophys. Acta. In press (1975).Google Scholar
  41. Kretsinger, R.H., Nockolds, C.E.: J. Biol. Chem. 248, 3313–3326 (1973).PubMedGoogle Scholar
  42. Leavis, P., Lehrer, S.S.: Biochemistry 13, 3042–3048 (1974).PubMedCrossRefGoogle Scholar
  43. Leavis, P., Lehrer, S.S., Potter, J.D., Gergely, J.: Fed. Proc. 33, 1293 (1974).Google Scholar
  44. Lehman, W., Kendrick-Jones, J., Szent-Györgyi, A.G.: Cold Spring Harbor Symp. Quant. Biol. 37, 319–330 (1972).Google Scholar
  45. Margossian, S.S., Cohen, C.: J. Molec. Biol. 81, 409–413 (1973).PubMedCrossRefGoogle Scholar
  46. Mercola, D., Bullard, B., Priest, J.: Nature 254, 634–635 (1975).PubMedCrossRefGoogle Scholar
  47. Morimoto, K., Harrington, W. : J. Molec. Biol. 88, 693–709 (1974).PubMedCrossRefGoogle Scholar
  48. Murray, A.C., Kay, CM.: Biochemistry 11, 1622–2627 (1972).CrossRefGoogle Scholar
  49. Nagy, B., Potter, J.D., Gergely, J.: Abstract, Biophys. Soc., p. 35a (1975).Google Scholar
  50. Parry, D.A.D., Squire, J.M. : J. Molec. Biol. 75 ,33–55 (1973).PubMedCrossRefGoogle Scholar
  51. Pechere, J.-L., Capony, J.-P., Demaille, J.: Systematic Zoology 22, 533–548 (1973).CrossRefGoogle Scholar
  52. Perry, S.V., Cole, H.A., Head, J.F., Wilson, F.J.: Cold Spring Harbor Symp. Quant. Biol. 37, 251–262 (1972).Google Scholar
  53. Potter, J.D.: Arch. Biochem. Biophys. 162, 436–441 (1974).PubMedCrossRefGoogle Scholar
  54. Potter, J.D.: Fed. Proc. 34, 2569 (1975a).Google Scholar
  55. Potter, J.D.: Abstract, Biophys. Soc, p. 36a (1975b).Google Scholar
  56. Potter, J.D., Gergely, J.: Biochemistry 13, 2697–2703 (1974).PubMedCrossRefGoogle Scholar
  57. Potter, J.D., Gergely, J.: J. Biol. Chem. 250, 4628–4633 (1975).PubMedGoogle Scholar
  58. Potter, J.D., Seidel, J.C., Gergely, J.: Fed. Proc. 32, 1988 (1973).Google Scholar
  59. Potter, J.D., Seidel, J.C., Leavis, P.C., Lehrer, S.S., Gergely, J.: In: Calcium Binding Proteins (eds. W. Drabikowski, H., Strzelecka-Golaszewska, E. Carafoli), pp. 129–152. Amsterdam: Elsevier 1974.Google Scholar
  60. Regenstein, J.M., Szent-Györgyi, A.G.: Biochemistry 14, 917–925 (1975).PubMedCrossRefGoogle Scholar
  61. Solaro, R.J., Wise, R.M., Shiner, J.S., Briggs, F.N.: Circulation Res. 34, 525–530 (1974).PubMedGoogle Scholar
  62. Spudich, J.A., Huxley, H.E., Finch, J.T.: J. Molec. Biol. 72, 619–632 (1972) .PubMedCrossRefGoogle Scholar
  63. Tufty, R.M., Kretsinger, R.H. : Science 187., 167–169 (1975).PubMedCrossRefGoogle Scholar
  64. Van Eerd, J.P., Kawasaki, Y.: Biochem. Biophys. Res. Commun. 47 ,859 to 865 (1972).PubMedCrossRefGoogle Scholar
  65. Van Eerd, J.P., Kawasaki, Y. : Biochemistry 12, 4972–4980 (1973).PubMedCrossRefGoogle Scholar
  66. Vibert, P.J., Haselgrove, J.C., Lowy, J., Paulson, F.R. : J. Molec. Biol. 71, 757–767 (1972).PubMedCrossRefGoogle Scholar
  67. Wakabayashi, T., Huxley, H.E., Amos, L.A., Klug, A.: J. Molec. Biol. 93, 477–497 (1975).PubMedCrossRefGoogle Scholar
  68. Weber, A., Herz, R.: J. Biol. Chem. 238, 599–605 (1963).PubMedGoogle Scholar
  69. Weber, A., Murray, J.M.: Physiol. Rev. 53, 612–673 (1973).PubMedGoogle Scholar
  70. Weeds, A., McLachlan, A.D.: Nature 252, 646–649 (1974).PubMedCrossRefGoogle Scholar
  71. Werber, M.M., Oplatka, A.: Biochem. Biophys. Res. Commun. 57, 823–830 (1974).PubMedCrossRefGoogle Scholar
  72. Wilkinson, J.M., Perry, S.V., Cole, H.A., Trayer, I.P.: Biochem. J. 127, 215–228 (1972).PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1976

Authors and Affiliations

  • J. D. Potter
  • B. Nagy
  • J. H. Collins
  • J. C. Seidel
  • P. Leavis
  • S. S. Lehrer
  • J. Gergely

There are no affiliations available

Personalised recommendations