Skip to main content
SpringerLink
Log in

Myosin light chain patterns of individual fast and slow-twitch fibres of rabbit muscles

  • Published:
Histochemistry Aims and scope Submit manuscript

Summary

Single muscle fibres were isolated by microdissection from freeze-dried samples of rabbit psoas and soleus muscles. The individual fibres were typed according to qualitative histochemical reactions for succinate dehydrogenase or NADH-tetrazolium reductase and for alkaline Ca2+-activated myofibrillar myosin ATPase after acid or alkaline preincubation. Methods are described for electrophoretic analysis by means of polyacrylamide disc electrophoresis in the presence of SDS of total myofibrillar proteins in single fibres after pre-extraction of soluble proteins. Fast-twitch white fibres revealed a myosin light chain pattern characteristic of “fast-type” myosin with three light chains of apparent molecular weights of 22,300 (LC1), 18,400 (LC2) and 16,000 (LC3). Fast-twitch red fibres were indistinguishable in this respect from fast-twitch white fibres and showed an identical pattern of myosin light chains. Slow-twitch fibres could be characterized by a myosin light chain pattern typical of myosin of slow-twitch muscles with peptides of the apparent molecular weights of 23,500 (LC1Sa), 23,000 (LC1Sb) and 18,500 (LS2S). Slow-twitch fibres isolated from soleus as well as from psoas muscle were indistinguishable with regard to their myosin light chain patterns, thus suggesting that fibres of the same histochemical type correspond in their myosin light chain patterns irrespective of their origin from different muscles.

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Ariano, M.A., Armstrong, R.B., Edgerton, V.R.: Hindlimb muscle fiber populations of five mammals. J. Histochem. Cytochem. 21, 51–55 (1973)

    Google Scholar 

  • Bárány, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol. 50, (Suppl., part 2) 197–218 (1967)

    Google Scholar 

  • Bárány, M., Bárány, K., Reckard, T., Volpe, A.: Myosin of fast and slow muscles of the rabbit. Arch. Biochem. Biophys. 109, 185–191 (1965)

    Google Scholar 

  • Barnard, J., Edgerton, V.R., Furukawa, T., Peter, J.B.: Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers. Amer. J. Physiol. 220, 410–414 (1971)

    Google Scholar 

  • Brooke, M.H., Kaiser, K.K.: Muscle fibre types: How many and what kind? Arch. Neurol. (Chic.) 23, 369–379 (1970)

    Google Scholar 

  • Close, R.I.: Dynamic properties of mammalian skeletal muscles. Physiol. Rev. 52, 129–197 (1972)

    Google Scholar 

  • Essén, B., Jansson, E., Henriksson, J., Taylor, A.W., Saltin, B.: Metabolic characteristics of fibre types in human skeletal muscle. Acta physiol. scand. 95, 153–165 (1975)

    Google Scholar 

  • Furukawa, T., Sugita, H., Toyokura, Y.: Comparative studies on myofibrillar proteins in different types of skeletal muscle fibers. Exptl. Neurol. 37, 515–521 (1972)

    Google Scholar 

  • Guth, L., Samaha, F.J.: Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exptl. Neurol. 25, 138–152 (1969)

    Google Scholar 

  • Heilmann, C., Brdiczka, D., Nickel, E., Pette, D.: ATPase activities, Ca2+ transport and phosphoprotein formation in sarcoplasmic reticulum subfractions of fast and slow rabbit muscles. Europ. J. Biochem., in press

  • Karpati, G., Eisen, A.E., Carpenter, S.: Subtypes of the histochemical type I muscle fibers. J. Histochem. Cytochem. 23, 89–91 (1975)

    Google Scholar 

  • Khan, M.A.: Histochemical characteristics of vertebrate striated muscle — A review. Progr. Histochem. Cytochem. 8, 1–47 (1976)

    Google Scholar 

  • Khan, M.A., Papadimitriou, J.M., Holt, P.G., Kakulas, B.A.: Further histochemical properties of rabbit skeletal muscle fibres. Histochemie 36, 173–183 (1973)

    Google Scholar 

  • Kugelberg, E.: Histochemical composition, contraction speed and fatiguability of rat soleus motor units. J. neurol. Sci. 20, 177–198 (1973)

    Google Scholar 

  • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227, 680–685 (1970)

    Google Scholar 

  • Locker, R.H., Hagyard, C.J.: The myosin of rabbit red muscles. Arch. Biochem. Biophys. 127, 370–375 (1968)

    Google Scholar 

  • Lowey, S., Risby, D.: Light chains from fast and slow muscle myosins. Nature (Lond.) 234, 81–85 (1971)

    Google Scholar 

  • Lowry, O.H., Passonneau, J.V.: A flexible system of enzymatic analysis. New York and London: Academic Press 1972

    Google Scholar 

  • Padykula, H.A., Gauthier, G.F.: Morphological and cytochemical characteristics of fiber types in normal mammalian skeletal muscle. In: Exploratory Concepts in Muscular Dystrophy and Related Disorders, (ed. A.T. Milhorat) p. 117–128. Amsterdam: Excerpta Medica Foundation 1967

    Google Scholar 

  • Padykula, H.A., Herman, E.: The specificity of the histochemical method for adenosine triphosphatase. J. Histochem. Cytochem. 3, 170–195 (1955)

    Google Scholar 

  • Perrie, W.T., Perry, S.V.: An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119, 31–38 (1970)

    Google Scholar 

  • Peter, J.B., Barnard, R.J., Edgerton, V.R., Gillepsie, C.A., Stempel, K.E.: Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11, 2627–2633 (1972)

    Google Scholar 

  • Pette, D., Müller, W., Leisner, E., Vrbová, G.: Time dependent effects on contractile properties, fibre population, myosin light chains and enzymes of energy metabolism in intermittently and continuously stimulated fast twitch muscles of the rabbit. Pflügers Arch. 364, 103–112 (1976)

    Google Scholar 

  • Pette, D., Spamer, C.: Typing of single muscle fibres according to their myosin light chain and enzyme activity patterns. Proc. 5th Intern. Congr. Histochem. Cytochem. p. 274, Bukarest 1976

  • Potter, J.D.: The content of troponin, tropomyosin, actin, and moysin in rabbit skeletal muscle myofibrils. Arch. Biochem. Biophys. 167, 436–441 (1974)

    Google Scholar 

  • Romanul, F.C.A.: Enzymes in muscle. I. Histochemical studies of enzymes in individual muscle fibers. Arch. Neurol. 11, 355–369 (1964)

    Google Scholar 

  • Samaha, F.J., Guth, L., Albers, R.W.: Differences between slow and fast muscle myosin. Adenosine triphosphatase activity and release of associated proteins by p-chloromercuriphenyl-sulfonate. J. Biol. Chem. 245, 219–224 (1970)

    Google Scholar 

  • Sarkar, S., Sréter, F.A., Gergely, J.: Light chains of myosins from white, red, and cardiac muscles. Proc. Nat. Acad. Sci. USA 68, 946–950 (1971)

    Google Scholar 

  • Spamer, C., Pette, D.: Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle. Histochemistry 52, 201–216 (1977)

    Google Scholar 

  • Sréter, F.A., Seidel, J.C., Gergely, J.: Studies on myosin from red and white skeletal muscles of the rabbit. J. Biol. Chem. 241, 5772–5776 (1966)

    Google Scholar 

  • Weeds, A.G., Hall, R., Spurway, N.C.S.: Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle. FEBS Lett. 49, 320–324 (1975)

    Google Scholar 

  • Weeds, A.G., Pope, B.: Chemical studies on light chains from cardiac and skeletal muscle myosins. Nature (Lond.) 234, 85–88 (1971)

    Google Scholar 

  • Weeds, A.G., Trentham, D.R., Kean, C.J., Buller, A.J.: Myosin from cross-reinnervated cat muscles. Nature (Lond.) 247, 135–139 (1974)

    Google Scholar 

  • Widmalm, S.E., Magnusson, B.C., Heyden, G.: Enzyme histochemical studies on ATPase activities in longitudinal sections of striated muscle tissue in the rat. Histochem. J. 5, 265–269 (1973)

    Google Scholar 

  • Yellin, H.: Differences in histochemical attributes between diaphragm and hindleg muscles of the rat. Anat. Rec. 173, 333–339 (1972)

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Fachbereich Biologie, Universität Konstanz, Postfach 7733, D-7750, Konstanz, Federal Republic of Germany

    Dirk Pette & Ursula Schnez

Authors
  1. Dirk Pette
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ursula Schnez
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Dedicated to the memory of Ernest Gutmann who has contributed so much to our knowledge on differentiation of muscle and who died on August 6, 1977

Rights and permissions

Reprints and permissions

About this article

Cite this article

Pette, D., Schnez, U. Myosin light chain patterns of individual fast and slow-twitch fibres of rabbit muscles. Histochemistry 54, 97–107 (1977). https://doi.org/10.1007/BF00489668

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00489668

Keywords

Search

Navigation