Skip to main content
NCBI home page
The Journal of Physiology logoLink to The Journal of Physiology
. 1979 Nov;296:453–469. doi: 10.1113/jphysiol.1979.sp013016

Changes in rodent muscle fibre types during post-natal growth, undernutrition and exercise.

G Goldspink, P S Ward
PMCID: PMC1279089  PMID: 160929

Abstract

1. Using histochemical staining methods for myosin ATPase oxidative and glycolytic enzymes, three major types of muscle fibre could be identified in the skeletal muscle of hamsters and mice. 2. Muscle fibre counts showed that the proportions of the different fibres were not entirely stable with age. In the hamster biceps brachii which is predominantly composed of ATPase-high fibres there was a decrease in the number of ATPase-low fibres. In the soleus muscle which is predominantly composed of ATPase-low fibres there was a decrease in ATPase-high fibres with age. 3. Although there was a change in the proportions of fibre types there was no change in the total number of fibres within the muscles with age. It is suggested that some reinnervation may take place during growth and that this is why the less dedominant fibre type decreases. 4. The response of the different fibre types to partial starvation was studied. The ATPase-high fibres showed the greatest decrease in size. Of these, the ATPase-high glycolytic type responded more than the ATPase-high oxidative type. The effects of the under-nutrition on the different fibre types were found to be completely reversible. Starvation did not affect the total number of fibres or the numbers of any fibre type. 5. The response of the different types to high intensity exercise (weight lifting) was studied. This type of exercise resulted in hypertrophy of all three major fibre types. However, the extent of the response varied according to the fibre type and the exact nature of the exercise. In most cases the ATPase-high fibres underwent hypertrophy more readily than the ATPase-low fibres. Where distinction was made between the two types of ATPase-high fibres, the ATPase-high glycolytic were found to hypertrophy more than the ATPase-high oxidative fibres. The effects of post exercise recovery (return to relative inactivity) were also studied and the changes in size of the fibres were found to be completely reversible.

Full text

PDF
453

Images in this article

468-2Plate 2
on p.468-2
468-1Plate 1
on p.468-1

Selected References

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

  1. Baldwin K. M., Klinkerfuss G. H., Terjung R. L., Molé P. A., Holloszy J. O. Respiratory capacity of white, red, and intermediate muscle: adaptative response to exercise. Am J Physiol. 1972 Feb;222(2):373–378. doi: 10.1152/ajplegacy.1972.222.2.373. [DOI] [PubMed] [Google Scholar]
  2. Baldwin K. M., Reitman J. S., Terjung R. L., Winder W. W., Holloszy J. O. Substrate depletion in different types of muscle and in liver during prolonged running. Am J Physiol. 1973 Nov;225(5):1045–1050. doi: 10.1152/ajplegacy.1973.225.5.1045. [DOI] [PubMed] [Google Scholar]
  3. Brooke M. H., Kaiser K. K. Muscle fiber types: how many and what kind? Arch Neurol. 1970 Oct;23(4):369–379. doi: 10.1001/archneur.1970.00480280083010. [DOI] [PubMed] [Google Scholar]
  4. Brooke M. H., Kaiser K. K. Trophic functions of the neuron. II. Denervation and regulation of muscle. The use and abuse of muscle histochemistry. Ann N Y Acad Sci. 1974 Mar 22;228(0):121–144. doi: 10.1111/j.1749-6632.1974.tb20506.x. [DOI] [PubMed] [Google Scholar]
  5. Burke R. E., Levine D. N., Zajac F. E., 3rd Mammalian motor units: physiological-histochemical correlation in three types in cat gastrocnemius. Science. 1971 Nov 12;174(4010):709–712. doi: 10.1126/science.174.4010.709. [DOI] [PubMed] [Google Scholar]
  6. Cooper R. R. Alterations during immobilization and regeneration of skeletal muscle in cats. J Bone Joint Surg Am. 1972 Jul;54(5):919–953. [PubMed] [Google Scholar]
  7. DAWSON D. M., GOODFRIEND T. L., KAPLAN N. O. LACTIC DEHYDROGENASES: FUNCTIONS OF THE TWO TYPES RATES OF SYNTHESIS OF THE TWO MAJOR FORMS CAN BE CORRELATED WITH METABOLIC DIFFERENTIATION. Science. 1964 Feb 28;143(3609):929–933. doi: 10.1126/science.143.3609.929. [DOI] [PubMed] [Google Scholar]
  8. ERANKO O., PALKAMA A. Improved localization of phosphorylase by the use of polyvinyl pyrrolidone and high substrate concentration. J Histochem Cytochem. 1961 Sep;9:585–585. doi: 10.1177/9.5.585. [DOI] [PubMed] [Google Scholar]
  9. Edgerton V. R., Barnard R. J., Peter J. B., Gillespie C. A., Simpson D. R. Overloaded skeletal muscles of a nonhuman primate (Galago senegalensis). Exp Neurol. 1972 Nov;37(2):322–339. doi: 10.1016/0014-4886(72)90077-5. [DOI] [PubMed] [Google Scholar]
  10. FARBER E., STERNBERG W. H., DUNLAP C. E. Histochemical localization of specific oxidative enzymes. I. Tetrazolium stains for diphosphopyridine nucleotide diaphorase and triphosphopyridine nucleotide diaphorase. J Histochem Cytochem. 1956 May;4(3):254–265. doi: 10.1177/4.3.254. [DOI] [PubMed] [Google Scholar]
  11. Faulkner J. A., Maxwell L. C., Lieberman D. A. Histochemical characteristics of muscle fibers from trained and detrained guinea pigs. Am J Physiol. 1972 Apr;222(4):836–840. doi: 10.1152/ajplegacy.1972.222.4.836. [DOI] [PubMed] [Google Scholar]
  12. GOLDSPINK G. Biochemical and physiological changes associated with the postnatal development of the biceps brachii. Comp Biochem Physiol. 1962 Nov;7:157–168. doi: 10.1016/0010-406x(62)90090-7. [DOI] [PubMed] [Google Scholar]
  13. GOLDSPINK G. CYTOLOGICAL BASIS OF DECREASE IN MUSCLE STRENGTH DURING STARVATION. Am J Physiol. 1965 Jul;209:100–104. doi: 10.1152/ajplegacy.1965.209.1.100. [DOI] [PubMed] [Google Scholar]
  14. GOLDSPINK G. THE COMBINED EFFECTS OF EXERCISE AND REDUCED FOOD INTAKE ON SKELETAL MUSCLE FIBERS. J Cell Physiol. 1964 Apr;63:209–216. doi: 10.1002/jcp.1030630211. [DOI] [PubMed] [Google Scholar]
  15. Goldspink G. The proliferation of myofibrils during muscle fibre growth. J Cell Sci. 1970 Mar;6(2):593–603. doi: 10.1242/jcs.6.2.593. [DOI] [PubMed] [Google Scholar]
  16. Goldspink G., Waterson S. E. The effect of growth and inanition on the total amount of nitroblue tetrazolium deposited in individual muscle fibres of fast and slow rat skeletal muscle. Acta Histochem. 1971;40(1):16–22. [PubMed] [Google Scholar]
  17. Gollnick P. D., Armstrong R. B., Saltin B., Saubert C. W., 4th, Sembrowich W. L., Shepherd R. E. Effect of training on enzyme activity and fiber composition of human skeletal muscle. J Appl Physiol. 1973 Jan;34(1):107–111. doi: 10.1152/jappl.1973.34.1.107. [DOI] [PubMed] [Google Scholar]
  18. Gollnick P. D., Armstrong R. B., Sembrowich W. L., Shepherd R. E., Saltin B. Glycogen depletion pattern in human skeletal muscle fibers after heavy exercise. J Appl Physiol. 1973 May;34(5):615–618. doi: 10.1152/jappl.1973.34.5.615. [DOI] [PubMed] [Google Scholar]
  19. Gollnick P. D., Karlsson J., Piehl K., Saltin B. Selective glycogen depletion in skeletal muscle fibres of man following sustained contractions. J Physiol. 1974 Aug;241(1):59–67. doi: 10.1113/jphysiol.1974.sp010640. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Gollnick P. D., Piehl K., Saltin B. Selective glycogen depletion pattern in human muscle fibres after exercise of varying intensity and at varying pedalling rates. J Physiol. 1974 Aug;241(1):45–57. doi: 10.1113/jphysiol.1974.sp010639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Gonyea W. J., Ericson G. C. An experimental model for the study of exercise-induced skeletal muscle hypertrophy. J Appl Physiol. 1976 Apr;40(4):630–633. doi: 10.1152/jappl.1976.40.4.630. [DOI] [PubMed] [Google Scholar]
  22. Gordon E. E. Anatomical and biochemical adaptations of muscle to different exercises. JAMA. 1967 Sep 4;201(10):755–758. [PubMed] [Google Scholar]
  23. Guth L., Samaha F. J. Procedure for the histochemical demonstration of actomyosin ATPase. Exp Neurol. 1970 Aug;28(2):365–367. [PubMed] [Google Scholar]
  24. Gutmann E., Hájek I., Horský P. Effect of excessive use on contraction and metabolic properties of cross-striated muscle. J Physiol. 1969 Jul;203(1):46P–47P. [PubMed] [Google Scholar]
  25. HAGAN S. N., SCOW R. O. Effect of fasting on muscle proteins and fat in young rats of different ages. Am J Physiol. 1957 Jan;188(1):91–94. doi: 10.1152/ajplegacy.1956.188.1.91. [DOI] [PubMed] [Google Scholar]
  26. HELANDER E. A. Influence of exercise and restricted activity on the protein composition of skeletal muscle. Biochem J. 1961 Mar;78:478–482. doi: 10.1042/bj0780478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. HENNEMAN E., OLSON C. B. RELATIONS BETWEEN STRUCTURE AND FUNCTION IN THE DESIGN OF SKELETAL MUSCLES. J Neurophysiol. 1965 May;28:581–598. doi: 10.1152/jn.1965.28.3.581. [DOI] [PubMed] [Google Scholar]
  28. Hall-Craggs E. C. The significance of longitudinal fibre division in skeletal muscle. J Neurol Sci. 1972;15(1):27–33. doi: 10.1016/0022-510x(72)90119-0. [DOI] [PubMed] [Google Scholar]
  29. Hayashi M., Freiman D. G. An improved method of fixation for formalin-sensitive enzymes with special reference to myosin adenosine triphosphatase. J Histochem Cytochem. 1966 Aug;14(8):577–581. doi: 10.1177/14.8.577. [DOI] [PubMed] [Google Scholar]
  30. Herbison G. J., Gordon E. E. Exercise of normal muscle: biochemical effects. Arch Phys Med Rehabil. 1973 Sep;54(9):409–passim. [PubMed] [Google Scholar]
  31. Holloszy J. O., Booth F. W. Biochemical adaptations to endurance exercise in muscle. Annu Rev Physiol. 1976;38:273–291. doi: 10.1146/annurev.ph.38.030176.001421. [DOI] [PubMed] [Google Scholar]
  32. Kendrick-Jones J., Perry S. V. The enzymes of adenine nucleotide metabolism in developing skeletal muscle. Biochem J. 1967 Apr;103(1):207–214. doi: 10.1042/bj1030207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Kowalski K., Gordon E. E., Martinez A., Adamek J. Changes in enzyme activities of various muscle fiber types in rat induced by different exercises. J Histochem Cytochem. 1969 Sep;17(9):601–607. doi: 10.1177/17.9.601. [DOI] [PubMed] [Google Scholar]
  34. Kugelberg E. Adaptive transformation of rat soleus motor units during growth. J Neurol Sci. 1976 Mar;27(3):269–289. doi: 10.1016/0022-510x(76)90001-0. [DOI] [PubMed] [Google Scholar]
  35. MONTGOMERY R. D. Growth of human striated muscle. Nature. 1962 Jul 14;195:194–195. doi: 10.1038/195194a0. [DOI] [PubMed] [Google Scholar]
  36. Macková E., Hník P. Compensatory muscle hypertrophy induced by tenotomy of synergists is not true working hypertrophy. Physiol Bohemoslov. 1973;22(1):43–49. [PubMed] [Google Scholar]
  37. Müller W. Isometric training of young rats--effects upon hind limb muscles. Histochemical, morphometric, and electron microscopic studies. Cell Tissue Res. 1975 Aug 18;161(2):225–237. doi: 10.1007/BF00220371. [DOI] [PubMed] [Google Scholar]
  38. NACHLAS M. M., TSOU K. C., DE SOUZA E., CHENG C. S., SELIGMAN A. M. Cytochemical demonstration of succinic dehydrogenase by the use of a new p-nitrophenyl substituted ditetrazole. J Histochem Cytochem. 1957 Jul;5(4):420–436. doi: 10.1177/5.4.420. [DOI] [PubMed] [Google Scholar]
  39. PADYKULA H. A., HERMAN E. Factors affecting the activity of adenosine triphosphatase and other phosphatases as measured by histochemical techniques. J Histochem Cytochem. 1955 May;3(3):161–169. doi: 10.1177/3.3.161. [DOI] [PubMed] [Google Scholar]
  40. Peter J. B., Barnard R. J., Edgerton V. R., Gillespie C. A., Stempel K. E. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry. 1972 Jul 4;11(14):2627–2633. doi: 10.1021/bi00764a013. [DOI] [PubMed] [Google Scholar]
  41. Reis D. J., Wooten G. F. The relationship of blood flow to myoglobin, capillary density, and twitch characteristics in red and white skeletal muscle in cat. J Physiol. 1970 Sep;210(1):121–135. doi: 10.1113/jphysiol.1970.sp009199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Rowe R. W. Effect of low nutrition on size of striated muscle fibres in the mouse. J Exp Zool. 1968 Mar;167(3):353–358. doi: 10.1002/jez.1401670307. [DOI] [PubMed] [Google Scholar]
  43. Tomanek R. J. A histochemical study of postnatal differentiation of skeletal muscle with reference to functional overload. Dev Biol. 1975 Feb;42(2):305–314. doi: 10.1016/0012-1606(75)90337-1. [DOI] [PubMed] [Google Scholar]
  44. Tuffery A. R. Growth and degeneration of motor end-plates in normal cat hind limb muscles. J Anat. 1971 Nov;110(Pt 2):221–247. [PMC free article] [PubMed] [Google Scholar]
  45. VAN LINGE B. The response of muscle to strenuous exercise. An experimental study in the rat. J Bone Joint Surg Br. 1962 Aug;44-B:711–721. doi: 10.1302/0301-620X.44B3.711. [DOI] [PubMed] [Google Scholar]
  46. Van der Meulen J. P., Peckham P. H., Mortimer J. T. Trophic functions of the neuron. 3. Mechanisms of neurotrophic interactions. Use and disuse of muscle. Ann N Y Acad Sci. 1974 Mar 22;228(0):177–189. doi: 10.1111/j.1749-6632.1974.tb20509.x. [DOI] [PubMed] [Google Scholar]
  47. WATTENBERG L. W., LEONG J. L. Effects of coenzyme Q10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction. J Histochem Cytochem. 1960 Jul;8:296–303. doi: 10.1177/8.4.296. [DOI] [PubMed] [Google Scholar]
  48. Woods D. J., Routtenberg A. "Self-starvation" in activity wheels: developmental and chlorpromazine interactions. J Comp Physiol Psychol. 1971 Jul;76(1):84–93. doi: 10.1037/h0031047. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Physiology are provided here courtesy of The Physiological Society

RESOURCES