Advertisement

The adaptation of myoglobin with age and training and its relationship to the three fiber types of skeletal muscle in miniature pig

  • R. H. Fitts
  • F. J. Nagle
  • R. G. Cassens
Article

Abstract

Muscle biopsies were performed on 6 endurance and 6 sprint trained and 5 control miniature pigs after 3 and 7 months of training. The biopsied muscle was fixed, sectioned and stained for myoglobin. The darkest staining fibers were called dark fibers, the lightest staining were called light fibers and those of intermediate intensity were called moderate fibers. The distribution of the three fiber types, identified by myoglobin staining, did not change following either an endurance or sprint running regimen despite physiologically measured training effects. Myoglobin increased substantially with maturation as reflected by a significant increase in the number of dark myoglobin fibers in the biceps femoris at 11 compared to 7 months of age. It was suggested that the large increase in myoglobin content due to normal maturation may have obscured the differences among groups due to training. With enzyme histochemical analysis, dark myoglobin fibers were found to be slow red or fast intermediate fibers, but never fast white fibers. This relationship between myoglobin and the oxidative fibers (slow red and fast intermediate) supports the concept that myoglobin stores oxygen and aids its diffusion into muscle fibers in need of a constant oxygen supply.

Key words

Muscle Myoglobin Training 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Baldwin, K. M., Klinkerfuss, G. H., Terjung, R. L., Mole, P. A., Holloszy, J. O.: Respiratory capacity of white, red and intermediate muscle: adaptive responses to exercise. Amer. J. Physiol. 222, 373–378 (1972)Google Scholar
  2. Edgerton, V. R., Gerchman, L., Carrow, R.: Histochemical changes in rat skeletal muscle after exercise. Exp. Neurol. 24, 110–123 (1969)Google Scholar
  3. Edgerton, V. R., Simpson, D., Barnard, R. J., Peter, J. B.: Phosphorylase activity in acutely exercised muscle. Nature (Lond.) 225, 866–867 (1970)Google Scholar
  4. Engle, W. K., Brooke, M. H.: Muscle biopsy as a clinical diagnostic aid. In: Neurological diagnostic techniques, W. S. Fields, ed. Springfield, Ill.: Thomas 1966Google Scholar
  5. Fitts, R. H., Campion, D. R., Nagle, F. J., Cassens, R. G.: Contractile properties of skeletal muscle from trained miniature pig. Pflügers Arch. 343, 133–141 (1973b)Google Scholar
  6. Fitts, R. H., Nagle, F. J., Cassens, R. G.: Characteristics of skeletal muscle fiber types in the miniature pig and the effects of training. Canad. J. Physiol. 51, 825–831 (1973a)Google Scholar
  7. Lawrie, R. A.: Some observations on factors affecting myoglobin concentration in muscle. J. agric. Sci. 40, 356–366 (1950)Google Scholar
  8. Lawrie, R. A.: Effect of enforced exercise on myoglobin concentration in muscle. Nature (Lond.) 171, 1069–1070 (1953)Google Scholar
  9. Meijer, A. E. F. H.: Histochemical method for the demonstration of myosin adenosine triphosphate in muscle tissue. Histochemie 22, 51–58 (1970)Google Scholar
  10. Millikan, G. A.: Muscle hemoglobin. Physiol. Rev. 19, 503–523 (1939)Google Scholar
  11. Morita, S., Cassens, R. G., Briskey, E. J.: Localization of myoglobin in striated muscle of the domestic pig; benzidine and NADH2-TR reactions. Stain Technol. 44, 283–286 (1969)Google Scholar
  12. Pattengale, P. K., Holloszy, J. O.: Augmentation of skeletal muscle myoglobin by a program of treadmill running. Amer. J. Physiol. 213, 783–785 (1967)Google Scholar
  13. Wittenberg, J. B.: Myoglobin-facilitated oxygen diffusion: Role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50, 559–636 (1970)Google Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • R. H. Fitts
    • 1
  • F. J. Nagle
    • 1
  • R. G. Cassens
    • 1
  1. 1.Muscle Biology Laboratory and Department of PhysiologyUniversity of WisconsinMadison

Personalised recommendations