Abstract
The ventricles and atria of the mammalian heart have differences in structure and function at different levels of organization. However, the current data on mechanical function of the heart chambers at different levels are contradictory and demand a detailed study. We compared mechanical characteristics of actin–myosin interaction by an in vitro motility assay and structural characteristics of contractile and regulatory proteins by one-dimensional denaturating polyacrylamide gel electrophoresis (SDS-PAGE) in atria, septum, right, and left ventricles. The sliding velocity of the reconstituted thin filaments over atrial myosin was significantly higher compared to other myocardium regions. No differences were observed in sliding velocity of atrial, septal, and ventricular native thin filaments over the myosin from the same myocardium region of the same rats. At the same time, the sliding velocity of the atrial native thin filament over porcine myosin was lower than that of the ventricular and septal native thin filament.
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This work was implemented using the equipment of the Shared Research Center of Scientific Equipment of Institute of Immunology and Physiology within the Governmental assignment to the Institute of Immunology and Physiology of the Russian Academy of Sciences; theme reg. no. 122022200089-4.
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Idea and design of the experiment: L.V.N. and O.P.G.; data collection and processing: O.P.G., V.O.V., I.K.P., and S.R.N.; manuscript writing and editing: O.P.G. and L.V.N.
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Translated by A. Polyanovsky
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The online version contains supplementary material available at https://doi.org/10.1134/S0022093022070110.
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Gerzen, O.P., Votinova, V.O., Potoskueva, I.K. et al. Characteristics of Actin—Myosin Interaction in Different Regions of Rat Heart. J Evol Biochem Phys 58 (Suppl 1), S98–S106 (2022). https://doi.org/10.1134/S0022093022070110
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DOI: https://doi.org/10.1134/S0022093022070110