The Anabolic Effects of Pituitary Growth Hormone

  • Jack L. Kostyo
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 2)

Abstract

During the past 10 years many of the details of the molecular mechanism involved in the process of protein synthesis and its control have been revealed. This advance in our understanding of the fundamental process which underwrites the growth of cells has made possible an extensive study of the mechanism of the anabolic action of pituitary growth hormone. The following will be a brief review of our present understanding of the sequence of events which occurs when target cells interact with growth hormone. In the main, the review will deal primarily with the action of growth hormone on skeletal muscle. It should be noted, however, that much recent work has been devoted to defining the mechanism of action of growth hormone on the liver. In instances where comparisons can be made, there appears to be a basic similarity in the mode of action of the hormone on both types of tissue.

Keywords

Manganese Polypeptide Leucine Dition Nucleoside 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Kostyo, J. L. Endocrinology 75: 113, 1964.PubMedCrossRefGoogle Scholar
  2. 2.
    Knobil, E. The Physiologist 9: 25, 1966.Google Scholar
  3. 3.
    Martin, T. E. and F. G. Young. Nature 208: 684, 1965.CrossRefGoogle Scholar
  4. 4.
    Kostyo, J. L. Ann. N. Y. Acad. Sci. (in press) 1967.Google Scholar
  5. 5.
    Wool, I. G. Biochim. Biophys. Acta 52: 574, 1961.PubMedCrossRefGoogle Scholar
  6. 6.
    Kostyo, J. L. Program of The Endocrine Society, 49th Meeting, 1967, p. 71.Google Scholar
  7. 7.
    Kostyo, J. L. Biochim. Biophys. Acta 129: 294, 1966.CrossRefGoogle Scholar
  8. 8.
    Riggs, T. R. and L. M. Walker. J. Biol. Chem. 235: 3503, 1960.Google Scholar
  9. 9.
    Hjalmarson, Å. and K. Ahren. Life Sciences 4: 863, 1965.PubMedCrossRefGoogle Scholar
  10. 10.
    Kostyo, J. L., J. Hotchkiss and E. Knobil. Science 130: 1653, 1959.PubMedCrossRefGoogle Scholar
  11. 11.
    Reiss, E. and D. M. Kipnis. J. Lab. Clin. Med. 54: 937, 1959.Google Scholar
  12. 12.
    Florini, J. R. and C. B. Breuer. Biochemistry 5: 1870, 1966.PubMedCrossRefGoogle Scholar
  13. 13.
    Breuer, C. B. and J. R. Florini. Biochemistry 5: 3857, 1966.CrossRefGoogle Scholar
  14. 14.
    Widnell, C. C. and J. R. Tata. Biochem J. 98: 621, 1966.PubMedGoogle Scholar
  15. 15.
    Pegg, A. E. and A. Korner. Naturee (London) 205: 904, 1965.CrossRefGoogle Scholar
  16. 16.
    Chamberlain, M. and P. Berg. Proc. Nat. Acad. Sci. U.S.A. 48: 81, 1962.CrossRefGoogle Scholar
  17. 17.
    Earl, D. C. N. and A. Korner. Arch. Biochem. Biophys. 115: 445, 1966.PubMedCrossRefGoogle Scholar
  18. 18.
    Korner, A. Biochem. J. 92: 449, 1964.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1968

Authors and Affiliations

  • Jack L. Kostyo
    • 1
  1. 1.Duke UniversityDurhamUSA

Personalised recommendations