Stable Level of Giant Sarcomeric Cytoskeletal Proteins in Striated Muscles of the Edible Dormouse Glis glis during Hibernation
2021
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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