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Stable Level of Giant Sarcomeric Cytoskeletal Proteins in Striated Muscles of the Edible Dormouse Glis glis during Hibernation

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Abstract

The changes in the content of the giant sarcomeric cytoskeletal proteins titin (3000–3700 kDa) and nebulin (770 kDa) in skeletal muscles (m. soleus, m. gastrocnemius), and titin in the left ventricular myocardium, as well as of the submembrane cytoskeletal protein dystrophin (427 kDa) in m. soleus and m. extensor digitorum longus (EDL), have been studied in the edible dormouse Glis glis during hibernation. The animals were divided into two experimental groups: “Summer activity” and “Hypothermia”. It was found that the development of atrophic changes in the skeletal muscles of hibernating animals is accompanied by a decrease in the dystrophin content. Specifically, the fluorescence intensity in skeletal muscle cross sections labeled with primary antibodies to dystrophin and Alexa Fluor® 488 conjugated secondary antibodies decreased in animals of the “Hypothermia” group by 2.7 times (p < 0.05) and 2.0 times (p < 0.05) in m. soleus and m. EDL, respectively. SDS electrophoresis of proteins in agarose-strengthened macroporous 2.2%-polyacrylamide gel revealed an insignificant decrease (by 15%, p ≤ 0.01) in the titin content compared to the myosin heavy chain content in m. gastrocnemius of animals of the “Hypothermia” group. The titin content in m. soleus and cardiac muscle, as well as the nebulin content in m. soleus and m. gastrocnemius, did not decrease during hibernation. These results are consistent with our previous data for other hibernators: long-tailed ground squirrel, brown and Himalayan black bears. It can be assumed that during evolution, hibernating animals developed the molecular mechanisms responsible for maintaining a stable level of giant sarcomeric cytoskeletal proteins during hibernation.

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Abbreviations

Т1:

intact titin, a full-length molecules that span the distance from the M-line to Z-disk in a sarcomere of the vertebrate striated muscle

Т2:

proteolytic titin fragments oriented along myosin filaments in the sarcomeric M-line region and A-band

MHC:

myosin heavy chains that form a myosin filament

CSA:

cross-sectional area

m. EDL :

musculus extensor digitorum longus

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Funding

This work was implemented using the equipment of the Center for Collective Use (CCU) at the FRC Kazan Scientific Center, CCU “Structural and Functional Studies of Biosystems” at the Institute of Theoretical and Experimental Biophysics (Pushchino), and CCU (EM Sector) at the Institute of Cell Biophysics (Pushchino) (all refer to Russian Academy of Sciences). The studies were supported by the Russian Foundation for Basic Research; grant Nos. 14-04-92116, 17-00-00243, 20-04-00204.

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Authors and Affiliations

  1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia

    S. S. Popova, D. A. Yurshenas, G. Z. Mikhailova, L. G. Bobyleva, N. N. Salmov & I. M. Vikhlyantsev

  2. Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center, Russian Academy of Sciences, Kazan, Russia

    O. V. Tyapkina & L. F. Nurullin

  3. Kazan State Medical University, Kazan, Russia

    O. V. Tyapkina & L. F. Nurullin

  4. Kazan Federal University, Institute of Fundamental Medicine and Biology, Kazan, Russia

    G. R. Gazizova, I. R. Nigmetzyanov & O. A. Gusev

  5. Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Russia

    N. M. Zakharova

Authors
  1. S. S. Popova
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  2. D. A. Yurshenas
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  3. G. Z. Mikhailova
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  4. L. G. Bobyleva
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  5. N. N. Salmov
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  6. O. V. Tyapkina
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  11. N. M. Zakharova
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  12. I. M. Vikhlyantsev
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Contributions

Concept and design: I.M.V., N.M.Z., O.A.G.; data acquisition and processing: S.S.P., D.A.Yu., L.G.B., N.N.S., O.V.T., L.F.N., G.R.G., I.R.N.; data analysis and interpretation: I.M.V., N.M.Z., O.A.G., O.V.T., G.Z.M.; manuscript writing: I.M.V., O.V.T., G.Z.M.

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Correspondence to I. M. Vikhlyantsev.

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CONFLICT OF INTEREST

The authors declare that they have no evident of potential conflict of interest related to the publication of this article.

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Translated by A. Polyanovsky

Russian Text © The Author(s), 2021, published in Rossiiskii Fiziologicheskii Zhurnal imeni I.M. Sechenova, 2021, Vol. 107, Nos. 6–7, pp. 828–841https://doi.org/10.31857/S0869813921060108.

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Popova, S.S., Yurshenas, D.A., Mikhailova, G.Z. et al. Stable Level of Giant Sarcomeric Cytoskeletal Proteins in Striated Muscles of the Edible Dormouse Glis glis during Hibernation. J Evol Biochem Phys 57, 886–895 (2021). https://doi.org/10.1134/S0022093021040128

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