Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1985 Aug 15;230(1):117–123. doi: 10.1042/bj2300117

The effect of insulin and intermittent mechanical stretching on rates of protein synthesis and degradation in isolated rabbit muscle.

R M Palmer, P A Bain, P J Reeds
PMCID: PMC1152594  PMID: 3902005

Abstract

Tyrosine balance and protein synthesis were studied during the same incubation in isolated rabbit forelimb muscles. From these measurements, protein degradation was calculated. Isolated muscles were usually in a state of negative amino acid balance, principally as a result of the 75% decrease in protein synthesis. Muscles from rabbits starved for 18 h had lower rates of both protein synthesis and degradation compared with muscles from normally fed rabbits. Intermittent mechanical stretching and the addition of insulin at 100 microunits/ml increased rates of both protein synthesis and degradation. Increases in the rate of protein synthesis were proportionately greater in the muscles from starved animals. In muscles from both fed and starved donors, increases in protein-synthesis rates owing to intermittent stretching and insulin were proportionately greater than the increases in degradation rates. For example, insulin increased the rate of protein synthesis in the muscles from starved donors by 111% and the rate of degradation by 31%. Insulin also increased the rate of protein synthesis when added at a higher concentration (100 munits/ml); at this concentration, however, the rate of protein degradation was not increased. The suppressive effect of insulin on high rates of protein degradation in other skeletal-muscle preparations may reflect a non-physiological action of the hormone.

Full text

PDF
121

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Clark A. S., Mitch W. E. Comparison of protein synthesis and degradation in incubated and perfused muscle. Biochem J. 1983 Jun 15;212(3):649–653. doi: 10.1042/bj2120649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Flaim K. E., Li J. B., Jefferson L. S. Protein turnover in rat skeletal muscle: effects of hypophysectomy and growth hormone. Am J Physiol. 1978 Jan;234(1):E38–E43. doi: 10.1152/ajpendo.1978.234.1.E38. [DOI] [PubMed] [Google Scholar]
  3. Frayn K. N., Maycock P. F. Regulation of protein metabolism by a physiological concentration of insulin in mouse soleus and extensor digitorum longus muscles. Effects of starvation and scald injury. Biochem J. 1979 Nov 15;184(2):323–330. doi: 10.1042/bj1840323. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fulks R. M., Li J. B., Goldberg A. L. Effects of insulin, glucose, and amino acids on protein turnover in rat diaphragm. J Biol Chem. 1975 Jan 10;250(1):290–298. [PubMed] [Google Scholar]
  5. Garlick P. J., Fern M., Preedy V. R. The effect of insulin infusion and food intake on muscle protein synthesis in postabsorptive rats. Biochem J. 1983 Mar 15;210(3):669–676. doi: 10.1042/bj2100669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Garlick P. J., McNurlan M. A., Preedy V. R. A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]phenylalanine. Biochem J. 1980 Nov 15;192(2):719–723. doi: 10.1042/bj1920719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Garlick P. J., Waterlow J. C., Swick R. W. Measurement of protein turnover in rat liver. Analysis of the complex curve for decay of label in a mixture of proteins. Biochem J. 1976 Jun 15;156(3):657–663. doi: 10.1042/bj1560657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goldspink D. F., Garlick P. J., McNurlan M. A. Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy. Biochem J. 1983 Jan 15;210(1):89–98. doi: 10.1042/bj2100089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jefferson L. S., Li J. B., Rannels S. R. Regulation by insulin of amino acid release and protein turnover in the perfused rat hemicorpus. J Biol Chem. 1977 Feb 25;252(4):1476–1483. [PubMed] [Google Scholar]
  10. Millward D. J., Garlick P. J., Nnanyelugo D. O., Waterlow J. C. The relative importance of muscle protein synthesis and breakdown in the regulation of muscle mass. Biochem J. 1976 Apr 15;156(1):185–188. doi: 10.1042/bj1560185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Millward D. J., Garlick P. J., Stewart R. J., Nnanyelugo D. O., Waterlow J. C. Skeletal-muscle growth and protein turnover. Biochem J. 1975 Aug;150(2):235–243. doi: 10.1042/bj1500235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Millward D. J., Waterlow J. C. Effect of nutrition on protein turnover in skeletal muscle. Fed Proc. 1978 Jul;37(9):2283–2290. [PubMed] [Google Scholar]
  13. Pain V. M., Albertse E. C., Garlick P. J. Protein metabolism in skeletal muscle, diaphragm, and heart of diabetic rats. Am J Physiol. 1983 Dec;245(6):E604–E610. doi: 10.1152/ajpendo.1983.245.6.E604. [DOI] [PubMed] [Google Scholar]
  14. Palmer R. M., Reeds P. J., Lobley G. E., Smith R. H. The effect of intermittent changes in tension on protein and collagen synthesis in isolated rabbit muscles. Biochem J. 1981 Sep 15;198(3):491–498. doi: 10.1042/bj1980491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rannels D. E., Kao R., Morgan H. E. Effect of insulin on protein turnover in heart muscle. J Biol Chem. 1975 Mar 10;250(5):1694–1701. [PubMed] [Google Scholar]
  16. Reeds P. J., Hay S. M., Glennie R. T., Mackie W. S., Garlick P. J. The effect of indomethacin on the stimulation of protein synthesis by insulin in young post-absorptive rats. Biochem J. 1985 Apr 1;227(1):255–261. doi: 10.1042/bj2270255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Reeds P. J., Palmer R. M., Smith R. H. Protein and collagen synthesis in rat diaphragm muscle incubated in vitro: the effect of alterations in tension produced by electrical or mechanical means. Int J Biochem. 1980;11(1):7–14. doi: 10.1016/0020-711x(80)90274-8. [DOI] [PubMed] [Google Scholar]
  18. Reeds P. J., Palmer R. M. The possible involvement of prostaglandin F2 alpha in the stimulation of muscle protein synthesis by insulin. Biochem Biophys Res Commun. 1983 Nov 15;116(3):1084–1090. doi: 10.1016/s0006-291x(83)80253-8. [DOI] [PubMed] [Google Scholar]
  19. Smith R. H., Palmer R. M., Reeds P. J. Protein synthesis in isolated rabbit forelimb muscles. The possible role of metabolites of arachidonic acid in the response to intermittent stretching. Biochem J. 1983 Jul 15;214(1):153–161. doi: 10.1042/bj2140153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Stirewalt W. S., Low R. B. Effects of insulin in vitro on protein turnover in rat epitrochlearis muscle. Biochem J. 1983 Feb 15;210(2):323–330. doi: 10.1042/bj2100323. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. TROWELL O. A. The culture of mature organs in a synthetic medium. Exp Cell Res. 1959 Jan;16(1):118–147. doi: 10.1016/0014-4827(59)90201-0. [DOI] [PubMed] [Google Scholar]
  22. Tischler M. E., Desautels M., Goldberg A. L. Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? J Biol Chem. 1982 Feb 25;257(4):1613–1621. [PubMed] [Google Scholar]
  23. WAALKES T. P., UDENFRIEND S. A fluorometric method for the estimation of tyrosine in plasma and tissues. J Lab Clin Med. 1957 Nov;50(5):733–736. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES