Summary
Ca2+-ATPase activity and light chains of myosin prepared from fast and slow muscles of rat, guinea-pig and rabbit were studied during development from embryonic to old age to establish further correlation with the well-known developmental changes in contraction properties of these muscles. The changes involve the slow soleus muscle much more than the fast extensor digitorum longus muscle. Myosin-ATPase activity of the soleus muscle before or at birth is higher than in the muscle of adult animals. Myosin from the soleus muscle of embryos or newborn animals reveales light chains of myosin of both fast and slow type (with a preponderance of light chains of fast type in 26-days-old rabbit embryos). During postnatal development the amount of light chains of the fast type decreases, that of the slow type increases. Myosin from the soleus muscle of adult animals contains only light chains of the slow type. However, myosin from the soleus muscle of 30-months-old rats exhibits high myosin ATPase activity and contains light chains of myosin of both slow and fast type as in perinatal development. This is in agreement with the shortening of contraction time observed in this muscle in very old age. Thus developmental differentiation of myosin in the soleus muscle is followed by a trend of levelling out of the differences between fast and slow muscles of senescent animals. No such “biphasic” development is observed with respect to the fast extensor digitorum longus muscle.
Similar content being viewed by others
Abbreviations
- EDL:
-
extensor digitorum longus
- SDS:
-
sodium dodecyl sulfate
- LC:
-
light chain
- LC1 :
-
light chain 1
References
Amphlett, G. W., Syska, H., Perry, S. V.: The polymorphic forms of tropomyosin and troponin I in developing rabbit skeletal muscle. FEBS Letters63, 22–26 (1976)
Bárány, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol.50, 197–216 (1967)
Brody, I. A.: Regulation of isometric contraction in skeletal muscle. Exp. Neurol.50, 673–683 (1976)
Chaplin, E. R., Nell, G. W., Walker, S. M.: Excitation contraction latencies in postnatal rat skeletal muscle fibers. Exp. Neurol.29, 142–151 (1970)
Chibnall, A. C., Rees, M. V., Williams, E. F.: The total nitrogen content of egg albumin and other proteins. Biochem. J.37, 354–359 (1943)
Close, R. I.: Dynamic properties of mammalian skeletal muscles. Physiol. Rev.52, 129–197 (1972)
Close, R.: Dynamic properties of fast and slow skeletal muscles of the rat during development. J. Physiol. (Lond.)173, 74–95 (1964)
Conway, E. J.: Microdiffusion analysis and volumetric error, 4th ed., p. 98. London: Crosby Lockwood 1957
Drachman, D. B., Johnston, D. M.: Development of a mammalian fast muscle: dynamic and biochemical properties correlated. J. Physiol. (Lond.)232, 29–42 (1973)
Engel, W. K.: The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease. Neurology (Minneap.)12, 778–784 (1962)
Fenner, C., Traut, R. R., Mason, D. T., Wikman-Coffelt, J.: Quantification of Coomassie blue stained proteins in polyacrylamide gels based on analysis of eluted dye. Analyt. Biochem.63, 595–602 (1975)
Gutmann, E., Syrový, I.: Contractile properties and myosin ATPase activity of fast and slow senile muscles of the rat. Gerontologia20, 239–244 (1974)
Gutman, E., Melichna, J., Syrový, I.: Developmental changes in contraction time, myosin properties and fibre pattern of fast and slow skeletal muscles. Physiol. bohemoslov.23, 19–27 (1974)
Guth, L., Samaha, F. J.: Erroneous interpretations which may result from application of the “myofibrillar ATPase” histochemical procedure to developing muscle. Exp. Neurol.34, 465–475 (1972)
Kugelberg, E.: Adaptive transformation of rat soleus motor units during growth. J. neurol. Sci.27, 269–289 (1976)
Johnson, P., Perry, S. V.: Biological activity and the 3-methyl-histidine content of actin and myosin. Biochem. J.119, 293–298 (1970)
Masaki, T., Yoshizaki, C.: Differentiation of myosin in chick embryos. J. Biochem.76, 123–131 (1974)
Pelloni-Mueller, G., Ermini, M., Jenny, E.: Myosin light chains of developing fast and slow rabbit skeletal muscle. FEBS Letters67, 68–74 (1976)
Perry, S. V.: Myosin adenosinetriphosphatase. In: Methods in enzymology, vol. 2 (S. P. Colowick and N. V. Kaplan, eds.), pp. 582–588. New York: Academic Press 1955
Perry, S. V.: The role of myosin in muscular contraction. In: Aspects of cell motility. Symp. Soc. exp. Biol.22, 1–16 (1968)
Sarkar, S., Sréter, F. A., Gergely, J.: Light chains of myosins from white, red and cardiac muscles. Proc. nat. Acad. Sci. (Wash.)68, 946–950 (1971)
Sarkar, S.: Stoichiometry and sequential removal of light chains of myosin. Cold Spr. Harb. Symp. quant. Biol.37, 14–17 (1972)
Sréter, F. A., Bálint, M., Gergely, J.: Structural and functional changes of myosin during development. Comparison with adult fast, slow and cardiac myosin. Develop. Biol.46, 317–325 (1975)
Takahashi, M., Tonomura, Y.: Developmental changes in the structure and kinetic properties of myosin adenosinetriphosphatase of rabbit skeletal fast muscle. J. Biochem.78, 1123–1133 (1975)
Trayer, I. P., Perry, S. V.: The myosin of developing skeletal muscle. Biochem. Z.345, 87–100 (1966)
Weber, K., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. biol. Chem.244, 4406–4412 (1969)
Weeds, A. G., Lowey, S.: Substructure of the myosin molecule. II. The light chains of myosin. J. molec. Biol.61, 701–725 (1971)
Weeds, A. G., Hall, R., Spurway, N. C. S.: Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle. FEBS Letters49, 320–324 (1975)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Syrový, I., Gutmann, E. Differentiation of myosin in soleus and extensor digitorum longus muscle in different animal species during development. Pflugers Arch. 369, 85–89 (1977). https://doi.org/10.1007/BF00580815
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00580815