title: Structure of cortical cytoskeleton in fibers of mouse muscle cells after being exposed to a 30-day space flight on board the BION-M1 biosatellite.
abstract: The aim of the work was to analyze changes in the organization of the cortical cytoskeleton in fibers of the mouse soleus muscle, tibialis anterior muscle and left ventricular cardiomyocytes after completion of a 30-day space flight on board the BION-M1 biosatellite (Russia, 2013). The transversal stiffness of the cortical cytoskeleton of the cardiomyocytes and fibers of the skeletal muscles did not differ significantly within the study groups compared with the vivarium control group. The content of beta- and gamma-actin in the membranous fraction of proteins in the left ventricular cardiomyocytes did not differ significantly within all study groups and correlated with the transversal stiffness. A similar situation was revealed in fibers of the soleus muscle and tibialis anterior muscle. At the same time, the content of beta-actin in the cytoplasmic fraction of proteins was found to be decreased in all types of studied tissues compared with the control levels in the postflight group, with lowered beta-actin gene expression rates in the postflight group. After completion of the space flight, the content of alpha-actinin-4 was found to be reduced in the membranous fraction of proteins from the mouse cardiomyocytes, while its content in the cytoplasmic fraction of proteins did not change significantly. Furthermore, gene expression rates of this protein were decreased at the time of dissection (it was started after 13 h after landing). At the same time, the content of alpha-actinin-1 decreased in the membranous fraction and increased in the cytoplasmic fraction of proteins from the soleus muscle fibers.
authors.affiliation: Department of Molecular and Cell Biomedicine, State Scientific Center of Russian Federation, Institute of Biomedical Problems of the Russian Academy of Sciences, Moscow, Russia; I.M. Sechenov First Moscow State Medical University, Moscow, Russia; and iogneva@yandex.ru.
authors.forename: I V
authors.initials: IV
authors.lastname: Ogneva
authors.affiliation: Department of Molecular and Cell Biomedicine, State Scientific Center of Russian Federation, Institute of Biomedical Problems of the Russian Academy of Sciences, Moscow, Russia; Moscow Institute of Physics and Technology (State University), Moscow, Russia.
authors.forename: M V
authors.initials: MV
authors.lastname: Maximova
authors.affiliation: Department of Molecular and Cell Biomedicine, State Scientific Center of Russian Federation, Institute of Biomedical Problems of the Russian Academy of Sciences, Moscow, Russia;
authors.forename: I M
authors.initials: IM
authors.lastname: Larina
mesh_terms: D000199:Actins / Q000502:physiology*; D000222:Adaptation, Physiological / Q000502:physiology*; D000818:Animals; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D055119:Elastic Modulus / Q000502:physiology; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D051379:Mice; D008810:Mice, Inbred C57BL; D018485:Muscle Fibers, Skeletal / Q000166:cytology / Q000502:physiology*; D032383:Myocytes, Cardiac / Q000166:cytology / Q000502:physiology*; D013026:Space Flight; D018531:Spacecraft; D014893:Weightlessness
chemical_list: D000199:Actins
keywords: actin-binding proteins; cell stiffness; mechanoreception; microgravity; nonmuscle actin