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Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 659869, 11 pages
http://dx.doi.org/10.1155/2012/659869
Research Article

Structure and Functional Characteristics of Rat’s Left Ventricle Cardiomyocytes under Antiorthostatic Suspension of Various Duration and Subsequent Reloading

State Scientific Center of Russian Federation, Institute of Biomedical Problems of Russian Academy of Sciences, 76-a, Khoroshevskoyoe Shosse, Moscow 123007, Russia

Received 5 March 2012; Revised 17 May 2012; Accepted 1 June 2012

Academic Editor: Michael Kalafatis

Copyright © 2012 I. V. Ogneva et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The goal of the research was to identify the structural and functional characteristics of the rat's left ventricle under antiorthostatic suspension within 1, 3, 7 and 14 days, and subsequent 3 and 7-day reloading after a 14-day suspension. The transversal stiffness of the cardiomyocyte has been determined by the atomic force microscopy, cell respiration—by polarography and proteins content—by Western blotting. Stiffness of the cortical cytoskeleton increases as soon as one day after the suspension and increases up to the 14th day, and starts decreasing during reloading, reaching the control level after 7 days. The stiffness of the contractile apparatus and the intensity of cell respiration also increases. The content of non-muscle isoforms of actin in the cytoplasmic fraction of proteins does not change during the whole experiment, as does not the beta-actin content in the membrane fraction. The content of gamma-actin in the membrane fraction correlates with the change in the transversal stiffness of the cortical cytoskeleton. Increased content of alpha-actinin-1 and alpha-actinin-4 in the membrane fraction of proteins during the suspension is consistent with increased gamma-actin content there. The opposite direction of change of alpha-actinin-1 and alpha-actinin-4 content suggests their involvement into the signal pathways.