Summary
Representative lysosomal enzyme activities were measured in muscles taken 0 h and 24 h after an acute exercise run that was completed without any overt signs of fatigue. The animals had progressed 2 and 4 weeks into a standard exercise program which typically produces adaptive changes in the working muscles. There was an increase in acetylglucosaminidase activity (12%) in the fast-twitch red muscle section of all animals that participated in the training program. This small increase may be representative of a delayed response found after more exhausting exercise. The single exercise bout, however, did not cause any acute change in lysosomal activity nor alter the partition of lysosomal enzymes between the “free” and particulate fractions. Thus, altered lysosomal enzyme activity does not appear to be a contributing influence that challenges muscle fiber homeostasis during moderately intense running.
Similar content being viewed by others
References
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. 225, 1045–1050 (1973)
Barrett, A. J.: Lysosomal enzymes. In: Lysosomes, a laboratory handbook, Dingle, J. T. (ed.), pp. 110–126. Amsterdam: North-Holland 1972
Bird, J. W. C.: Skeletal muscle lysosomes. In: Lysosomes in biology and pathology, Dingle, J. T., Dean, R. T. (eds.), pp. 75–109. New York. American Elsevier 1975
Goldberg, A. L., St. John, A. C.: Intracellular protein degradation in mammalian and bacterial cells: part II. Ann. Rev. Biochem. 45, 747–803 (1976)
Gollnick, P. D., Ianuzzo, C. D.: Colonic temperature response of rats during exercise. J. Appl. Physiol. 24, 747–750 (1968)
Hermansen, L., Osnes, J. B.: Blood and muscle pH after maximal exercise in man. J. Appl. Physiol. 32, 304–308 (1972)
Holloszy, J. O., Booth, F. W.: Biochemical adaptations to endurance exercise in muscle. Ann. Rev. Physiol. 38, 273–291 (1976)
Kanter, Y.: The role of insulin in regulating protein catabolism in mammalian cells. Int. J. Biochem. 7, 253–257 (1976)
Karlsson, J.: Lactate and phosphagen concentrations in working muscle of man. Acta Physiol. Scand. [Suppl.] 358, 1–72 (1971)
Lloyd, J. B.: A study of permeability of lysosomes to amino acids and small peptides. Biochem. J. 121, 245–248 (1971)
Lowry, D. H., Rosenbrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)
Pugh, D., Leaback, D. H., Walker, P. G.: Studies on glucosaminidase. N-Acetyl-Β-glucosaminidase in rat kidney. Biochem. J. 65, 464–469 (1957)
Segal, H. L., Matsuzawa, T., Waider, M., Abraham, G. J.: What determines the half-life of proteins in vivo? Some experiences with alanine amino transferase of rat tissues. Biochem. Biophys. Res. Commun. 36, 764–770 (1969)
Steel, R. G. D., Torrie, J. W.: Principles and procedures of statistics. New York: McGraw-Hill 1960
Terjung, R. L., Baldwin, K. M., Molé, P. A., Klinkerfuss, G. H., Holloszy, J. O.: Effect of running to exhaustion on skeletal muscle mitochondria: a biochemical study. Am. J. Physiol. 223, 549–554 (1972)
Terjung, R. L.: Muscle fiber involvement during training of different intensities and durations. Am. J. Physiol. 230, 946–950 (1976)
Tullson, P. C., Armstrong, R. B.: Exercise-induced muscle inflammation. Fed. Proc. 37, 663 (1978)
Vihko, V., RantamÄki, J., Salminen, A.: Exhaustive exercise and acid hydrolase activity in mouse skeletal muscle. Histochemistry 57, 237–249 (1978a)
Vihko, V., Salminen, A., RantamÄki, J.: Acid hydrolase activity in red and white skeletal muscle of mice during two-week period following exhaustive exercise. Pflügers Arch. Eur. J. Physiol. 378, 99–106 (1978b)
Vihko, V., Salminen, A., RantamÄki, J.: Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities. Acta Physiol. Scand. 104, 74–81 (1978c)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schott, L.H., Terjung, R.L. The influence of exercise on muscle lysosomal enzymes. Europ. J. Appl. Physiol. 42, 175–182 (1979). https://doi.org/10.1007/BF00431024
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00431024