The Histochemical Journal

, Volume 17, Issue 6, pp 699–706 | Cite as

Fibre-type specificity and effect of thyroid hormone on glucose 6-phosphate dehydrogenase activity in normal and denervated skeletal muscles of the rat

  • Stephen R. Max
  • E. C. B. Hall-Craggs
  • Marco Chacon
Papers
Received:
Revised:
  • 23 Downloads

Summary

Glucose-6-phosphate dehydrogenase activity increases following denervation of rat skeletal muscle. The specificity of this effect to muscle fibre type was studied. Basal activity of the dehydrogenase was higher in soleus, a muscle composed predominantly of type I fibres, than in extensor digitorum longus, a muscle composed predominantly of type IIa and b fibres. The enzymatic activity of the soleus was also greater than that of the red (RQ) and white (WQ) portions of quadriceps muscle (predominantly type IIa and type IIb fibres, respectively). Following denervation, glucose-6-phosphate dehydrogenase increased in extensor digitorum longus and RQ, but not in WQ or the soleus. Following chronic treatment of rats with 3,3′,5-triiodothyronine, which converts type I muscle fibres to type II, the dehydrogenase activity increased in both denervated soleus and extensor digitorum longus. It is concluded that the effect of denervation on glucose-6-phosphate dehydrogenase activity is selective for type IIa (fast oxidative-glycolytic) muscle fibres.

Keywords

Skeletal Muscle Muscle Fibre Thyroid Hormone Dehydrogenase Activity Fibre Type 
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.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ariano, M. A., Armstrong, R. B. &Edgerton, V. R. (1973). Hindlimb muscle fiber populations of five mammals.J. Histochem. Cytochem. 21, 51–5.Google Scholar
  2. Bonner, W. D. (1955) Succinic dehydrogenase.Meth. Enzym. 1, 722–9.Google Scholar
  3. Capo, L. A. &Sillau, A. H. (1983) The effect of hyperthyroidism on capillarity and oxidative capacity in rat soleus and gastrocnemius muscles.J. Physiol., Lond. 34, 1–14.Google Scholar
  4. Fitts, R. H., Winder, W. W., Brooke, M. H., Kaiser, K. K. &Holloszy, J. O. (1980) Contractile, biochemical and histochemical properties of thyrotoxic rat soleus muscle.Am. J. Physiol. 238, C15–20.Google Scholar
  5. Glock, G. E. &McLean, P. (1953) Further studies on the properties and assay of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver.Biochem. J. 55, 400–8.Google Scholar
  6. Hall-Craggs, E. C. B., Max, S. R., Wines, M. M., Moreland, T. M. &Hebel, J. R. (1983a) Central core degeneration after tenotomy in soleus muscles of hyperthyroid rats.Expl Neurol. 81, 722–32.Google Scholar
  7. Hall-Craggs, E. C. B., Wines, M. M. &Max, S. R. (1983b) Fiber type changes in denervated soleus muscles of the hyperthyroid rat.Expl Neurol. 80, 252–7.Google Scholar
  8. Hogan, E. L., Dawson, D. M. &Romanul, F. C. A. (1965) Enzymatic changes in denervated muscle. II. Biochemical studies.Archs Neurol. 13, 274–82.Google Scholar
  9. Ianuzzo, C. D., Chen, V., O'Brien, P. &Keens, T. G. (1984) Effect of experimental dysthyroidism on the enzymatic character of the diaphragm.J. appl. Physiol: Respirat. Environ. Exercise Physiol. 56, 117–21.Google Scholar
  10. Ilyin, V. S., Razumovskaya, N. I. &Usatenko, M. S. (1975) Influence of nerve impulse on enzyme synthesis in skeletal muscle.Adv. Enz. Reg. 13, 219–34.Google Scholar
  11. King, D. B., King, C. R. &Jacuruso, R. B. (1981) Avian muscular dystrophy: Thyroidal influence on pectoralis muscle growth and glucose 6-phosphate dehydrogenase activity.Life Sci. 28, 577–85.Google Scholar
  12. Koski, C. L. &Max, S. R. (1974) Substrate utilization by the denervated rat hemidiaphragm.Expl Neurol. 43, 544–54.Google Scholar
  13. Lowry, O. H., Rosebrough, N. J., Farr, A. L. &Randall, R. J. (1951) Protein measurement with the Folin phenol reagent.J. biol. Chem. 193, 265–75.Google Scholar
  14. Mano, Y., Mano, K., Mayer, R. F., Deshpande, S. S. &Albuquerque, E. X. (1979) Effect of paraplegia produced by intrathecal 6-aminonicotinamide on motor units in the rat.Expl Neurol. 65, 435–56.Google Scholar
  15. Nwoye, L., Mommaerts, W. F. H. M., Simpson, D. R., Seraydarian, K. &Marusich, M. (1982) Evidence for a direct action of thyroid hormone in specifying muscle properties.Am. J. Physiol. 242, R401–8.Google Scholar
  16. Oppenheimer, J. H., Mariash, C. N., Towle, H. C., Schwartz, H. L. &Kaiser, F. E. (1981) Interaction of T3 and carbohydrate in the induction of lipogenic enzymes.Life Sci. 28, 1693–9.Google Scholar
  17. Robbins, N. &Carlson, D. (1979) Early changes in muscle glucose 6-phosphate dehydrogenase activity after denervation: Locus and dependence on nerve stump length.Brain Res. 177, 145–6.Google Scholar
  18. Schaerf, F. W., Patz, T. &Max, S. R. (1982) Estrogens modulate neural control of muscle glucose 6-phosphate dehydrogenase.J. Neurochem. 38, 1765–7.Google Scholar
  19. Snedecor, G. W. &Cochran, W. G. (1967)Statistical Methods (6th edn), pp. 271–5. Ames: Iowa State University Press.Google Scholar
  20. Wagner, K. R., Kauffman, F. C. &Max, S. R. (1978) The pentose phosphate pathway in regenerating skeletal muscle.Biochem. J. 170, 17–22.Google Scholar
  21. Wagner, K. R. &Max, S. R. (1979) Neurotrophic regulation of glucose 6-phosphate dehydrogenase in rat skeletal muscle.Brain Res. 170, 572–6.Google Scholar
  22. Winder, W. (1980) Effects of thyroid hormones on different types of skeletal muscle. InPlasticity of Muscle (edited byPette, D.), pp. 582–91. New York: DeGruyter & Co.Google Scholar

Copyright information

© Chapman and Hall Ltd. 1985

Authors and Affiliations

  • Stephen R. Max
    • 1
  • E. C. B. Hall-Craggs
    • 2
  • Marco Chacon
    • 3
  1. 1.Department of NeurologyUniversity of Maryland School of MedicineBaltimoreUSA
  2. 2.Department of AnatomyUniversity of Maryland School of MedicineBaltimoreUSA
  3. 3.Department of PediatricsUniversity of Maryland School of MedicineBaltimoreUSA

Personalised recommendations