Contractile Protein Isoforms

  • Ute Gröschel-Stewart
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


All active cell movement originates in the interaction of only a few different classes of protein molecules. The major representatives are Actin and Tropomyosin, which can assemble into long and thin filamentous polymers, and Myosin, which can also aggregate to form thick filaments. They are found in varying proportions, in the three major categories: namely striated muscle, smooth muscle and non-muscle (or cytoplasmic) contractile system. Biochemical and ultrastructural studies have shown that the proteins from the different contractile systems have many characteristic features in common, and yet measurable differences have been found between them. Contractile proteins are present in numerous Isoforms, which can confer different regulatory and contractile properties to different types of muscle cells. As a consequence the three major categories can be subdivided further in the adult vertebrate systems; and, in addition, some of the components may be present as developmental stage specific (embryonic or neonatal) isoforms. The most frequently used methods, present and past, for the distinction of contractile protein isoforms, include:
  1. 1.

    Measurement of mechanical properties of isolated organs, organ strips and “skinned” muscle fibers.

  2. 2.

    Myosin ATPase activity in vitro and in situ (histochemistry).

  3. 3.

    Electrophoretic analysis of muscle proteins and extracts in the native state, in the denatured state, either alone or in combination with isoelectric focussing.

  4. 4.

    Peptide mapping, sequence analysis.

  5. 5.

    Immunological assays with antisera ± specific for isoforms.

  6. 6.

    Recombinant DNA techniques.



Myosin Heavy Chain Smooth Muscle Myosin Striate Muscle Myosin Contractile System Myosin ATPase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


I. Overviews

  1. -.
    Groschel-Stewart, U. (1980) Intl. Rev. Cytology 65, 194–254.Google Scholar
  2. -.
    Gröschel-Stewart, U. & Drenckhahn, D. (1982) Collagen Rel. Res. 2, 381–463.CrossRefGoogle Scholar
  3. -.
    Hightower, R.C. and Meagher, R.B. (1986) Genetics 114, 315–332.PubMedGoogle Scholar
  4. -.
    Perry, S.V. (1985) J. exp. Biol. 115, 31–42.PubMedGoogle Scholar
  5. -.
    Swynghedauw, B. (1986) Physiol. Rev. 66, 710–771.PubMedGoogle Scholar
  6. -.
    Whalen, R.G. (1985) J. exp. Biol. 115, 43–53.PubMedGoogle Scholar

II. Original Papers

  1. -.
    Bárány, M. (1967) J. Gen. Physiol. 50 197–218.PubMedCrossRefGoogle Scholar
  2. -.
    Gröschel-Stewart, U., Rahousky, C. Franke, R., Peleg, I., Kahane, I., Eldor, A., Mühlrad, A. (1985) Cell Tissue Res. 241, 399–403.PubMedCrossRefGoogle Scholar
  3. -.
    Gumming, G., Ponte, P., Blau, H., Kedes, L. (1983) Molec. Cell Biol. 3, 1985–1995.Google Scholar
  4. -.
    Mahdavi, V., Chambers, A.P., Nadal-Ginard, B. (1984) Proc. Natl. Acad. Sci. USA 81, 2626–2630.PubMedCrossRefGoogle Scholar
  5. -.
    Rooner, A.S., Thompson, M.M., Murphy, R.A. (1986) Am. J. Physiology.Google Scholar
  6. -.
    Ruiz-Opazo, N., Weinberger, J., Nadal-Ginard, B. (1985) Nature 315, 67–70.PubMedCrossRefGoogle Scholar
  7. -.
    Sanders, C., Burtnick, L.D., Smillie, L.B. (1986) J. Biol. Chem. 261, 12774–12778.PubMedGoogle Scholar
  8. -.
    Strehler, E.E., Strehler-Page, M.-A., Perriard, J.-C., Periasamy, M., Nadal-Ginard, B. (1986) J. Mol. Biol. 190, 291–317.PubMedCrossRefGoogle Scholar
  9. -.
    Vandekerckhove, J., Weber, K. (1979) Differentiation 14, 123–133.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Ute Gröschel-Stewart
    • 1
  1. 1.Institute of ZoologyTechnical University DarmstadtDarmstadtGermany

Personalised recommendations