Post-receptor responses to hormonal stimuli

  • P. Cohen
Chapter
Part of the Biological Council book series (BCSDA)

Abstract

It is now recognised that hormones bind to specific receptors on the outer membranes of their target cells, and can exert their effects without entering the cells whose metabolic activities they regulate. However, the molecular events which follow the hormone-receptor interaction are very incompletely understood. This short review will mainly centre on a critical assessment of the current state of our knowledge regarding the regulation of glycogen metabolism by adrenalin, glucagon and insulin. This is not only the system for which the nature of the post-receptor responses are known in the greatest molecular detail, but is also that in which cyclic AMP was identified, a discovery which opened up the area of secondary hormone messengers as the intracellular mediators of hormone action. The implication of cyclic AMP in the action of a growing number of hormonal effects (Robison, Butcher and Sutherland, 1971) therefore makes an analysis of this system a model of unique general interest.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ashby, C. D. and Walsh, D. A. (1972). J. Biol. Chem., 248, 1255Google Scholar
  2. Bishop, J. S. (1970). Biochim. Biophys. Acta, 208, 208PubMedCrossRefGoogle Scholar
  3. Bishop, J. S. and Lamer, J. (1967). J. Biol. Chem., 242, 1355Google Scholar
  4. Brostrom, C. O., Hunkeler, F. L. and Krebs, E. G. (1971). J. Biol. Chem., 246, 1961PubMedGoogle Scholar
  5. Chen, L. J. and Walsh, D. A. (1971). Biochemistry, 10, 3614PubMedCrossRefGoogle Scholar
  6. Cheung, W. Y. (1970). Biochem. Biophys. Res. Comm., 38, 533PubMedCrossRefGoogle Scholar
  7. Cohen, P.(1973 a). European J. Biochem. 34, 1CrossRefGoogle Scholar
  8. Cohen, P. (1973 b). Calcium and Cell Regulation (ed. R. M. S. Smellie), Biochemical Society Symposia Series, Vol. 39, p. 51Google Scholar
  9. Cohen, P. and Antoniw, J. F. (1973). FEBS Lett. 34, 43PubMedCrossRefGoogle Scholar
  10. Cohen, P. T. W. and Cohen, P. (1973). FEBS Lett., 29, 113PubMedCrossRefGoogle Scholar
  11. Corbin, J. D., Reimann, E. M., Walsh, D. A. and Krebs, E. G. (1970). J. Biol. Chem., 245, 4849PubMedGoogle Scholar
  12. Cori, C. F. and Cori, G. T. (1936). Proc. Soc. Exp. Biol. Med., 34, 702CrossRefGoogle Scholar
  13. Cuatracasas, P. (1969). Proc. Nat. Acad. Sci. U.S., 63, 450CrossRefGoogle Scholar
  14. Danforth, W. H. (1965). J. Biol. Chem., 240, 588PubMedGoogle Scholar
  15. Danforth, W. H., Helmreich, E. and Cori, C. F. (1962). Proc. Nat. Acad. Sci. U.S., 48, 1191CrossRefGoogle Scholar
  16. Delange, R. J., Kemp, R. G., Riley, W. D., Cooper, R. A. and Krebs, E. G. (1968). J. Biol. Chem., 243, 2200PubMedGoogle Scholar
  17. Deter, R. L. and De Duve, C. (1967). J. Cell Biol., 33, 437PubMedPubMedCentralCrossRefGoogle Scholar
  18. Drummond, G. I., Horwood, J. P. and Powell, C. A. (1969). J. Biol. Chem., 244, 4235PubMedGoogle Scholar
  19. Friedman, D. L. and Lamer, J. (1963). Biochemistry, 2, 669PubMedCrossRefGoogle Scholar
  20. Haddox, M. K., Newton, N. E., Hartle, D. K. and Goldberg, N. D. (1972). Biochem. Biophys. Res. Comm., 47, 653PubMedCrossRefGoogle Scholar
  21. Hayakawa, T., Perkins, J. P. and Krebs, E. G. (1973a). Biochemistry, 12, 574PubMedCrossRefGoogle Scholar
  22. Hayakawa, T., Perkins, J. P., Walsh, D. A. and Krebs, E. G. (1973 b). Biochemistry, 12, 567PubMedCrossRefGoogle Scholar
  23. Heilmeyer, L. M. G., Meyer, F., Haschke, R. H. and Fischer, E. H. (1970). J. Biol. Chem. 245, 6649PubMedGoogle Scholar
  24. Huston, R. B. and Krebs, E. G. (1968). Biochemistry, 7, 2116PubMedCrossRefGoogle Scholar
  25. Huttenen, J. K., Steinburg, D. and Meyer, S. E. (1970). Proc. Nat. Acad. Sci. U.S., 67, 290CrossRefGoogle Scholar
  26. Krebs, E. G. (1972). Current Topics in Cellular Regulation, 5, 99PubMedCrossRefGoogle Scholar
  27. Krebs, E. G. and Fischer, E. H. (1956). Biochem. Biophys. Acta, 20, 150PubMedCrossRefGoogle Scholar
  28. Krebs, E. G., Love, D. S., Bratvold, G. E., Trayser, K. A., Mayer, W. L. and Fischer, E. H. (1964). Biochemistry, 3, 1022PubMedCrossRefGoogle Scholar
  29. Kuo, J. F. and Greengard, P. (1969). Proc. Nat. Acad. Sci. U.S., 64, 234CrossRefGoogle Scholar
  30. Langan, T. A. (1969). Proc. Nat. Acad. Sci. U.S. 64, 1276CrossRefGoogle Scholar
  31. Langan, T. A. (1973). Protein Phosphorylation in Control Mechanisms (ed. F. Huijing and E. Y. C. Lee), Miami Winter Symposium, vol. 5, Academic Press, London, p. 287CrossRefGoogle Scholar
  32. Langan, T. A. and Hohmann, P. (1974). Fed. Proc., 33, 1597 (Abstr. 2111 )Google Scholar
  33. Langan, T. A., Rall, S. C. and Cole, R. D. (1971). J. Biol. Chem., 246, 1942PubMedGoogle Scholar
  34. Lamer, J., Villar-Palasi, C., Goldberg, N. D., Bishop, J. S., Huijing, F., Wenger, J. I., Sasko, H. and Brown, N. D. (1968). Advan. Enzyme Reg., 6, 409CrossRefGoogle Scholar
  35. Loten, E. G. and Sneyd, J. G. T. (1970). Biochem. J., 120, 187PubMedPubMedCentralCrossRefGoogle Scholar
  36. Lyon, J. B. and Porter, J. (1963). J. Biol. Chem., 238, 1PubMedGoogle Scholar
  37. Meyer, F., Heilmeyer, L. M. G., Haschke, R. H. and Fischer, E. H. (1970). J. Biol. Chem., 245, 6642PubMedGoogle Scholar
  38. Meyer, S. E. and Krebs, E. G. (1970). J. Biol. Chem., 245, 3153Google Scholar
  39. Osawa, E., Hosoi, K. and Ebashi, S. (1967). J. Biochem. (Tokyo), 61, 531Google Scholar
  40. Oye, I. and Sutherland, E. W. (1966). Biochim. Biophys. Acta 127 347PubMedCrossRefGoogle Scholar
  41. Passonneau, J. V. and Lowry, O. H. (1962). Biochem. Biophys. Res. Comm., 7, 10PubMedCrossRefGoogle Scholar
  42. Piras, R., Rothman, L. B. and Cabib, E. (1968). Biochemistry, 7, 56PubMedCrossRefGoogle Scholar
  43. Posner, J. B., Stern, R. and Krebs, E. G. (1965). J. Biol. Chem., 240, 982PubMedGoogle Scholar
  44. Rail, T. W., Sutherland, E. W. and Berthet, J. (1957). J. Biol. Chem., 224, 463Google Scholar
  45. Rall, T. W., Wosilait, W. D. and Sutherland, E. W. (1956). J. Biol. Chem., 218, 483PubMedGoogle Scholar
  46. Reimann, E. M., Walsh, D. A. and Krebs, E. G. (1971). J. Biol. Chem., 246, 1986PubMedGoogle Scholar
  47. Robison, G. A., Butcher, R. W. and Sutherland, E. W. (1971). Cyclic AMP, Academic Press, LondonGoogle Scholar
  48. Schiender, K. K., Wei, S. H. and Villar-Palasi, C. (1969). Biochim. Biophys. Acta, 191, 272CrossRefGoogle Scholar
  49. Söderling, T. R., Hickenbottom, J. P., Reimann, E. M., Hunkeler, F. L., Walsh, D. A. and Krebs, E. G. (1970). J. Biol. Chem., 245, 6317PubMedGoogle Scholar
  50. Sutherland, E. W. (1950). Recent Progr. Horm. Res., 5, 441Google Scholar
  51. Sutherland, E. W. and Rall, T. W. (1958). J. Biol. Chem., 232, 1077PubMedGoogle Scholar
  52. Taylor, C., Cox, A. J., Kernohan, J. C. and Cohen, P. (1975). European J. Biochem., 51, 105CrossRefGoogle Scholar
  53. Vaes, G. (1958). Nature, 219, 939CrossRefGoogle Scholar
  54. Villar-Palasi, C. and Lamer, J. (1960). Biochim. Biophys. Acta, 39, 171PubMedCrossRefGoogle Scholar
  55. Walsh, D. A. and Ashby, C. D. (1973). Recent Progr. Horm. Res., 29, 329PubMedGoogle Scholar
  56. Walsh, D. A., Ashby, C. D., Gonzales, C., Calkins, C., Fischer, E. H. and Krebs, E. G. (1971 a). J. Biol. Chem., 246, 1977Google Scholar
  57. Walsh, D. A. and Krebs, E. G. (1973). The Enzymes, 8, 855Google Scholar
  58. Walsh, D. A., Perkins, J. P., Brostrom, C. O., Ho, E. S. and Krebs, E. G. (1971 b). J. Biol. Chem., 246, 1968Google Scholar
  59. Walsh, D. A., Perkins, J. P. and Krebs, E. G. (1968). J. Biol. Chem., 243, 3763PubMedGoogle Scholar
  60. Wosilait, W. D. and Sutherland, E. W. (1956). J. Biol. Chem., 218, 469PubMedGoogle Scholar
  61. Yeaman, S. J. and Cohen, P. (1974). Biochem. Soc. Trans., 2, 931CrossRefGoogle Scholar
  62. Zieve, F. J. and Glinsmann, W. H. (1973). Biochem. Biophys. Res. Comm., 50, 872PubMedCrossRefGoogle Scholar

Copyright information

© Institute of Biology Endowment Trust Fund 1976

Authors and Affiliations

  • P. Cohen
    • 1
  1. 1.Medical Sciences InstituteDundee UniversityUK

Personalised recommendations