Skip to main content
SpringerLink
Log in

Myosin types in human skeletal muscle fibers

  • Published:
Histochemistry Aims and scope Submit manuscript

Summary

By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.

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

  • Arkansas, V., Engel, W.K.: Distinct subtypes of type I fibers of human skeletal muscle. Neurology 25, 879–887 (1975)

    Google Scholar 

  • Bergström, J.: Muscle electrolytes in man determined by neuron activation analysis on needle biopsy specimens. A study on normal subjects, kidney patients with chronic diarrhea. Scand. J. Clin. Lab. Invest. Suppl. 68, 1–110 (1962)

    Google Scholar 

  • Brevet, A., Whalen, R.G.: Comparative structural analysis of myosin after limited tryptic hydrolysis by use of two-dimensional gel electrophoresis. Biochimie 60, 459–466 (1978)

    Google Scholar 

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

    Google Scholar 

  • Brooke, M.H., Kaiser, K.K.: The use and abuse of muscle histochemistry. Ann. N.Y. Acad. Sci. 228, 121–144 (1974)

    Google Scholar 

  • Bruggmann, S., Jenny, E.: The immunological specificity of myosins from cross-striated muscles as revealed by quantitative microcomplement fixation and enzyme inhibition by antisera. Biochim. Biophys. Acta 412, 39–50 (1975)

    Google Scholar 

  • Celio, M.R., Lutz, H., Binz, H., Fey, H.: Protein A in immunoperoxidase techniques. J. Histochem. Cytochem. 27, 691–698 (1979)

    Google Scholar 

  • Colling-Saltin, A.S.: Enzyme histochemistry on skeletal muscle of the human foetus. N. Neurol. Sci. 39, 169–185 (1978)

    Google Scholar 

  • Dalla-Libera, L., Margreth, A., Mussini, I., Cerri, C., Scarlato, G.: Myosin polymorphism in human skeletal muscles. Muscle and Nerve 1, 280–291 (1978)

    Google Scholar 

  • Dhoot, G.K., Perry, S.V.: Distribution of polymorphic forms of troponin components and tropomyosin in skeletal muscle. Nature 278, 714–718 (1979)

    Google Scholar 

  • Dubois-d'Alcq, M., McFarland, H., McFarlin, D.: Protein A-peroxidase: A valuable tool for the localization of antigens. J. Histochem. Cytochem. 25, 1201–1206 (1977)

    Google Scholar 

  • Dubowitz, V., Brooke, M.H.: In: Muscle biopsy — A modern approach. Vol. 2, pp. 98–102. London: Saunders 1973

    Google Scholar 

  • Edgerton, V.R., Simpson, D.R.: The intermediate muscle fiber of rats and guinea pigs. J. Histochem. Cytochem. 17, 828–838 (1969)

    Google Scholar 

  • Engvall, E., Perlmann, P.: Enzyme-linked immunosorbent assay, ELISA; III. Quantitation of specific antibodies by enzyme-labelled anti-immunoglobulin in antigen-coated tubes. Immunology 109, 129–135 (1972)

    Google Scholar 

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

    Google Scholar 

  • Farkas-Bargeton, E., Diebler, M.F., Arsénio-Nunes, M.L., Wehrlé, R., Rosenberg, B.: Etude de la maturation histochimique, quantitative et ultrastructurale du muscle foetal humain. J. Neurol. Sci. 31, 245–259 (1977)

    Google Scholar 

  • Garnett, R.A.F., O'Donovan, M.J., Stephens, J.A., Taylor, A.: Motor unit organization of human medial gastrocnemius. J. Physiol. 287, 33–43 (1978)

    Google Scholar 

  • Gauthier, G., Lowey, S.: Polymorphism of myosin among skeletal muscle fiber types. J. Cell Biol. 74, 760–779 (1977)

    Google Scholar 

  • Gauthier, G., Lowey, S., Hobbs, A.W.: Fast and slow myosin in developing muscle fibers. Nature 274, 25–29 (1978)

    Google Scholar 

  • Gauthier, G., Lowey, S.: Distribution of myosin isoenzymes among skeletal muscle fiber types. J. Cell Biol. 81, 10–25 (1979)

    Google Scholar 

  • Gröschel-Stewart, U., Meschede, D., Lehr, I.: Histochemical and immunochemical studies on mamalian striated muscle fibers. Histochemie 33, 79–85 (1973)

    Google Scholar 

  • Hoh, J.F.Y., Yeoh, G.P.S.: Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles. Nature 280, 321–322 (1979)

    Google Scholar 

  • Jansson, E.: Type II fibers in human skeletal muscle: Biochemical characteristics and distribution. Acta Physiol. Scand. 95, 47 (1975)

    Google Scholar 

  • Jansson, E., Kaijser, L.: Muscle adaptation to extreme endurance training in man. Acta Physiol. Scand. 100, 315–324 (1977)

    Google Scholar 

  • Jansson, E., Sjödin, B., Tesch, P.: Changes in muscle fiber type distribution in man after physical training. A sign of fiber type transformation? Acta Physiol. Scand. 104, 235–237 (1978)

    Google Scholar 

  • Johnson, M.A., Polgar, J., Weightman, D., Appleton, D.: Data on the distribution of fiber types in thirty-six human muscles. An autopsy study. J. Neurol. Sci. 18, 111–129 (1973)

    Google Scholar 

  • Kundrat, E., Pepe, F.: The M band. Studies with fluorescent antibody staining. J. Cell Biol. 48, 340–347 (1971)

    Google Scholar 

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

    Google Scholar 

  • Lutz, H., Ermini, M., Jenny, E., Bruggmann, S., Joris, F., Weber, E.: The size of the fiber populations in rabbit skeletal muscles as revealed by indirect immunofluorescence with anti-myosin sera. Histochemistry 57, 223–235 (1978)

    Google Scholar 

  • Lutz, H., Weber, H., Billeter, R., Jenny, E.: Fast and slow myosin within single skeletal muscle fibers of adult rabbits. Nature 281, 142–144 (1979)

    Google Scholar 

  • Meijer, A.E.F.H., Elias, E.A.: The value of enzyme histochemical techniques in classifying fiber types of human skeletal muscle. 1. Adult skeletal muscles with no apparent disease of the neuromuscular system. Histochemistry 48, 257–267 (1976)

    Google Scholar 

  • Pette, D., Schnez, U.: Coexistence of fast and slow type myosin light chains in single muscle fibers during transformation as induced by long-term stimulation. FEBS Lett, 83, 128–130 (1977)

    Google Scholar 

  • Pette, D., Henriksson, J., Emmerich, M.: Myofibrillar protein patterns of single fibers from human muscle. FEBS Lett. 103, 152–155 (1979)

    Google Scholar 

  • Portmann, A.J., Levison, S.A., Dandliker, W.B.: Equilibrium binding studies on antifluorescein antibody during various stages of the immune response. Immunochemistry 12, 461–466 (1975)

    Google Scholar 

  • Richards, E.G., Chung, C.-S., Menzel, D.B., Olcott, H.S.: Chromatography of myosin on diethylaminoethyl-Sephadex A-50. Biochemistry 6, 528–540 (1967)

    Google Scholar 

  • Rowlerson, A.: Fluorescent-labelled antibody to fast and slow muscle myosin in the study of mammalian muscle fiber specialization. J. Physiol. 282, 29P-30P (1978)

    Google Scholar 

  • Rubinstein, N., Mabuchi, K., Pepe, F., Salmons, S., Gergely, J., Sreter, F.: Use of type specific antimyosins to demonstrate the transformation of individual fibers in chronically stimulated rabbit fast muscles. J. Cell Biol. 79, 252–261 (1978)

    Google Scholar 

  • Schaub, M.C., Perry, S.V.: The regulatory proteins of the myofibril. Characterization and properties of the inhibitory factor (Troponin B). Biochem. J. 123, 367–377 (1971)

    Google Scholar 

  • Schaub, M.C., Watterson, J.G., Waser, P.G.: Conformational differences in myosin. IV. Radioactive labelling of specific thiol groups as influenced by ligand binding. Hoppe-Seyler's Z. Physiol. Chem. 356, 325–339 (1975)

    Google Scholar 

  • Spamer, C., Pette, D.: Activities of malate dehydrogenase, 3-hydroxyacyl-CoA-dehydrogenase and fructose-1,6-diphosphatase with regard to metabolic subpopulations of fast- and slow-twitch fibers in rabbit muscles. Histochemistry 60, 9–19 (1979)

    Google Scholar 

  • Sreter, F.A., Åström, K.-E., Romanul, F.C.A., Young, R.R., Jones, H.R. Jr.: Characteristics of myosin in nemaline myopathy. J. Neurol. Sci. 27, 99–116 (1976)

    Google Scholar 

  • Weber, H., Schaub, M.C., Römer, W., Lutz, H., Jenny, E., in preparation

  • Whalen, R.G., Butler-Browne, G.S., Gros, F.: Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cells. J. Mol. Biol. 126, 415–431 (1978)

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Pharmacology and Biochemistry, University of Zürich, Winterthurerstr. 260, CH-8057, Zürich

    R. Billeter, H. Weber, H. Lutz & E. Jenny

  2. Research Institute, Swiss School of Physical Education and Sports, CH-2532, Magglingen

    H. Howald

  3. Institute of Cell Biology, Swiss Federal Institute of Technology, CH-8093, Zürich, Switzerland

    H. M. Eppenberger

Authors
  1. R. Billeter
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. H. Weber
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. H. Lutz
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. H. Howald
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. H. M. Eppenberger
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. E. Jenny
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Billeter, R., Weber, H., Lutz, H. et al. Myosin types in human skeletal muscle fibers. Histochemistry 65, 249–259 (1980). https://doi.org/10.1007/BF00493174

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00493174

Keywords

Search

Navigation