Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Myofibril and sarcoplasmic reticulum changes with exercise and growth

  • 51 Accesses

  • 12 Citations


The intent of this study was to observe the effects of different treadmill running programs upon selected biochemical properties of soleus muscle from young rats. Young 10 day litter-mates were assigned to endurance (E), sprint (S) and control (C) groups. Each was partitioned into either 21 or 51 day exercising groups and 10 day controls. For C the myofibril ATPase activity at 21 and 51 days were lower than 10 day activity (p≤0.05). In the 51 day E group ATPase activity (0.378±0.009 Μmol Pi·mg−1·min−1) was greater than at 10 and 21 days (0.307±0.006 and 0.323±0.008 Μmol Pi·mg−1·min−1) (p≤0.05). No change occurred in the S group from 10 to 21 and 51 days (p≥0.05). Both the 21 and 51 day S (0.318±0.011 and 0.399±0.010 Μmol Pi·mg−1·min−1) and E (0.323±0.008 and 0.378±0.009 Μmol Pi·mg−1·min−1) groups had higher activity compared to the C group (0.193±0.029 and 0.172±0.031 Μmol Pi·mg−1·min−1) (p≤0.05). Maturation (10–51 day) resulted in a lowered sarcoplasmic reticulum (SR) yield and Ca2+ binding (p≤0.05) while Ca2+ uptake ability did not change (p≥0.05). SR yield, Ca2+ binding and uptake were not altered with S training (p≥0.05). The E training resulted in greater Ca2+ uptake at 51 days compared to C and S (p≤0.05), with no change in Ca2+ binding (p≥0.05). The data suggest that E training alters the normal development pattern of young rat soleus muscle.

This is a preview of subscription content, log in to check access.


  1. Ariano MA, Armstrong RB, Edgerton VR (1973) Hindlimb muscle fiber populations of five animals. J Histochem cytochem 21: 51–55

  2. Baldwin KM, Winder WW, Holloszy JO (1975) Adaptation of actomyosin ATPase in different types of muscle endurance exercise. Am J Physiol 229: 422–426

  3. Belcastro AN, Wenger H, Nihei T, Secord D, Bonen A (1980) Functional overload of rat fast twitch skeletal muscle during development. J Appl Physiol: Respirat Environ Exerc Physiol 49: 583–588

  4. Belcastro AN, Pierce GN, Sopper MM, Low M, Bonen A (1979) Cyclic adenosine monophosphate sensitivity of skeletal muscle myofibrillar adenosine triphosphatase in young and mature rats. Physiologist 22: 8

  5. Bonner HW, Buffington CK, Simpson LR, Leslie SW (1977) The effects of training on the in vivo 45Ca distribution within the mitochondrial and microsomal fractions. Med Sci Sports 9: 66

  6. Crews EL, Fuge KW, Oscai LB (1969) Weight food intake and body composition: effects of exercise and of protein deficiency. Am J Physiol 216: 359–363

  7. Drachman DB, Johnston DM (1973) Development of a mammalian fast muscle: dynamic and biochemical properties correlated. J Physiol 234: 29–42

  8. Fabiato A, Fabiato F (1977) Calcium release from the sarcoplasmic reticulum. Circ Res 40: 119–129

  9. Fitts FH, Holloszy JO (1977) Contractile properties of rat soleus muscle: effects of training and fatigue. Am J Physiol 233: C86-C91

  10. Gawehn KI (1974) Inorganic pyrophosphate. In: Bergmeyer HU (ed) Methods of enzymatic analysis, 4th edn. Academic Press, New York, pp 2239–2242

  11. Goldspink G, Waterson SE (1971) 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 40: 16–22

  12. Gutmann E, Melichna J (1972) Contractile properties of different skeletal muscles of the rat during development. Physiol Biochem 21: 1–7

  13. Gutmann E, Melichna J, Syrovy I (1974a) Developmental changes in contraction time, myosin properties and fiber patterns of fast and slow skeletal muscles. Physiol Bohemoslov 23: 19–27

  14. Gutmann E, Melichna J, Syrovy I (1974b) Developmental changes in contraction time and muscle fiber pattern of fast and slow muscles. Experimentia 29: 435–436

  15. Harigaya S, Schwartz A (1969) Rate of calcium binding and uptake in normal animal and failing human cardiac muscle. Circ Res 25: 781–794

  16. Lehninger AL (1974) Ca2+ transport by mitochondria and its possible role in the cardiac contraction-relaxation cycle. Circ Res [Suppl III] 34–35: 111-83–111-88

  17. Lowry OH, Roseborough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275

  18. Morehouse CA, Stull GA (1975) Statistical principles and procedures with applications for physical education. Lea and Febiger, Philadelphia

  19. Oscai LB, Babirak SP, Dubach FB, McGarr JA, Spirakis CN (1974) Exercise or food restriction: effect on adipose tissue cellularity. Am J Physiol 227: 901–904

  20. Pelloni-Muller G, Dermini M, Jenny E (1976) Changes in myosin light and heavy chain stiochiometry during development of rabbit fast, slow and cardiac muscle. FEBS Lett 70: 113–117

  21. Perry SV, Corsi A (1958) Extraction of proteins other than myosin from the isolated rabbit myofibril. Biochem J 68: 5–12

  22. Ray KP, England PJ (1976) Phosphorylation of the inhibitory subunit of troponin and its effect on the calcium dependence of cardiac myofibril adenosine triphosphatase. FEBS Lett 79: 11–15

  23. Rockstein M, Chesky JA, Lopez T (1978) Calcium sensitivity of myocardial actomyosin ATPase in young and mature male Fischer rats. A brief note. Mech Aging Dev 8: 413–416

  24. Sreter FA, Gergely J, Luff AL (1974) The effect of cross reinnervation on the synthesis of myosin light chains. Biochem Biophys Res Commun 56: 84–89

  25. Staudte HW, Exner GV, Pette D (1973) Effects of short-term, high intensity (sprint) training on some contractile and metabolic characteristics of fast and slow muscles of the rat. Pflügers Arch 344: 159–164

  26. Syrovy I, Gutmann E (1977) Differentiation of myosin in soleus and extensor digitorum longus muscle in different animal species during development. Pflügers Arch 369: 85–89

  27. Syrovy E, Gutmann E, Melichna J (1972) Effect of exercise on skeletal muscle myosin ATPase activity. Physiol Bohemoslov 21: 633–638

Download references

Author information

Correspondence to Angelo N. Belcastro.

Additional information

Supported by grants A-6449 and A-0425 from the Natural Sciences and Engineering Research Council of Canada

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Belcastro, A.N., Wenger, H. Myofibril and sarcoplasmic reticulum changes with exercise and growth. Europ. J. Appl. Physiol. 49, 87–95 (1982). https://doi.org/10.1007/BF00428967

Download citation

Key words

  • Myofibril ATPase
  • Sarcoplasmic reticulum
  • Ca2+ binding
  • Ca2+ uptake