Effect of Myosin Heavy Chain Peptides on Contractile Activation of Skinned Cardiac Muscle Fibres

  • J. C. Rüegg
  • J. D. Strauss
  • C. Zeugner
  • I. Trayer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 332)


Peptides derived from the sequence of the S1 domain of the myosin heavy chain were tested for their effects on the regulation of cardiac contractility. Basal calcium responsiveness of the contractile apparatus in terms of isometric tension generation and ATPase was determined in chemically demembranated ventricular fibre bundles. Incubation with a series of peptides derived from the peptide sequence around SH thiol group (Cys 707) resulted in a measurable increase in isometric tension and ATPase activity at sub-maximal concentrations of calcium but not at saturating levels of calcium activity, thus demonstrating a “calcium-sensitizing” effect of these peptides. The effects of two of these peptides, S1 687–716 and S1 701–717, are demonstrated to mimic, but importantly were not additive with, the calcium sensitization induced by lowering ATP concentration to 10 μM from 10 mM. This suggests the possibility of a similar mechanism of action underlying both types of sensitization. Because these effects demonstrate tissue specificity, were sensitive with respect to potency to not only amino acid composition but also sequence, and could not be duplicated by a similarly charged, non-homologous peptide, we attribute the effects to be specific to the sequences of these peptides. These data provide further evidence that the sequence between residues 687 and 717 of the S1 domain of the myosin heavy chain influences the calcium responsiveness of the contractile apparatus.


ATPase Activity Myosin Heavy Chain Isometric Tension Contractile Apparatus North Atlantic Treaty Organization 
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  1. 1.
    Eisenberg, E. & Greene, L.E. Ann. Rev. Physiol. 42, 293–309 (1980).CrossRefGoogle Scholar
  2. 2.
    Allshire, A., Piper, M., Cuthbertson, K.S.R. & Cobbold, P.H. Biochem. J. 244, 381–385 (1987).PubMedGoogle Scholar
  3. 3.
    Ridgway, E.B., Gordon, A.M. & Martyn, D.A. Science 219, 1075–1077 (1983).PubMedCrossRefGoogle Scholar
  4. 4.
    Güth, K. & Potter J.D. J. Biol. Chem. 262, 13627–13635 (1987).PubMedGoogle Scholar
  5. 5.
    Suzuki, R., Nishi, N, Tokura, S. & Morita, F. J. Biol. Chem 262, 11410–11412 (1987).PubMedGoogle Scholar
  6. 6.
    Keane, A.M., Trayer, I.P., Levine, B.A., Zeugner, C. & Rüegg, J.C. et al. Nature 344, 265–268 (1990)PubMedCrossRefGoogle Scholar
  7. 7.
    Rüegg, J.C., Zeugner, C., Van Eyk, J., Kay, CM. & Hodges, R.S. Pflügers Arch. 414, 430–436 (1989).PubMedCrossRefGoogle Scholar
  8. 8.
    Fabiato, A. & Fabiato, F. J. Physiol. (Paris) 75, 463–505 (1979).Google Scholar
  9. 9.
    Güth, K. & Wojciechowski, R. Pflügers Arch. 407, 552–557 (1986).PubMedCrossRefGoogle Scholar
  10. 10.
    Rüegg, J.C., Zeugner, C., Van Eyk, J.E., Hodges R.S. & Trayer, I.P Peptides as Probes in Muscle Research (ed. Rüegg, J.C.), 95–110 (Springer Verlag, Heidelberg/Berlin, 1991).CrossRefGoogle Scholar
  11. 11.
    Strauss, J.D., de Lanerolle, P. & Paul, R.J. Am. J. Physiol. 262, C1437–C1445 (1992)PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • J. C. Rüegg
    • 1
  • J. D. Strauss
    • 1
  • C. Zeugner
    • 1
  • I. Trayer
    • 2
  1. 1.II. Institute of Physiology University of HeidelbergHeidelbergGermany
  2. 2.School of Biochemistry University of BirminghamEdgbastonUK

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