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BioMed Research International
Volume 2015, Article ID 104735, 13 pages
Research Article

Isoform Composition and Gene Expression of Thick and Thin Filament Proteins in Striated Muscles of Mice after 30-Day Space Flight

1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya Street 3, Pushchino 142290, Russia
2Pushchino State Institute of Natural Science, Nauki Street 3, Pushchino 142290, Russia
3Dagestan State University, Gadzhieva Street 43a, Makhachkala, Republic of Dagestan 367000, Russia
4Institute of Cell Biophysics, Russian Academy of Sciences, Institutskaya Street 3, Pushchino 142290, Russia
5SRC, Institute for Biomedical Problems, Russian Academy of Sciences, Khoroshevskoye Street 76A, Moscow 123007, Russia

Received 14 August 2014; Revised 11 December 2014; Accepted 20 December 2014

Academic Editor: Peter Krustrup

Copyright © 2015 Anna Ulanova 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.


Changes in isoform composition, gene expression of titin and nebulin, and isoform composition of myosin heavy chains as well as changes in titin phosphorylation level in skeletal (m. gastrocnemius, m. tibialis anterior, and m. psoas) and cardiac muscles of mice were studied after a 30-day-long space flight onboard the Russian spacecraft “BION-M” number 1. A muscle fibre-type shift from slow-to-fast and a decrease in the content of titin and nebulin in the skeletal muscles of animals from “Flight” group was found. Using Pro-Q Diamond staining, an ~3-fold increase in the phosphorylation level of titin in m. gastrocnemius of mice from the “Flight” group was detected. The content of titin and its phosphorylation level in the cardiac muscle of mice from “Flight” and “Control” groups did not differ; nevertheless an increase (2.2 times) in titin gene expression in the myocardium of flight animals was found. The observed changes are discussed in the context of their role in the contractile activity of striated muscles of mice under conditions of weightlessness.