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Effect of Interchain Disulfide Crosslinking in the Tropomyosin Molecule on Actin-Myosin Interaction in the Atrial Myocardium

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Bulletin of Experimental Biology and Medicine Aims and scope

Tropomyosin (Tpm) is one of the main regulatory proteins in the myocardium. In some heart pathologies, interchain disulfide crosslinking in the Tpm molecule occurs. In the ventricle, this change in the structural properties of the Tpm molecule affects calcium regulation of the actin-myosin interaction. Using an in vitro motility assay, we found that Tpm crosslinking does not affect the actin-myosin interaction in the atria. We assume that the intramolecular crosslinking of Tpm in the atrium does not play such a crucial role in the pathogenesis of heart failure as it plays in the heart ventricles.

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Authors and Affiliations

  1. Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia

    D. V. Shchepkin, A. M. Matyushenko, S. Y. Bershitsky & G. V. Kopylova

  2. A. N. Bakh Institute of Biochemistry, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia

    A. M. Matyushenko

Authors
  1. D. V. Shchepkin
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  2. A. M. Matyushenko
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  3. S. Y. Bershitsky
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  4. G. V. Kopylova
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Corresponding author

Correspondence to G. V. Kopylova.

Additional information

Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 167, No. 1, pp. 72-75, January, 2019

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Shchepkin, D.V., Matyushenko, A.M., Bershitsky, S.Y. et al. Effect of Interchain Disulfide Crosslinking in the Tropomyosin Molecule on Actin-Myosin Interaction in the Atrial Myocardium. Bull Exp Biol Med 167, 65–68 (2019). https://doi.org/10.1007/s10517-019-04462-8

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  • DOI: https://doi.org/10.1007/s10517-019-04462-8

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