[Adaptive behavior of titin isoforms from skeletal and cardiac muscles of ground squirrels (Citellus undulatus) during hibernation].
By the use of modified SDS electrophoresis in agarose-strengthened 2% polyacrylamide gels, the adaptive behavior of titin isoforms in skeletal and cardiac muscles of ground squirrels (Citellus undulatus) during hibernation was studied. The presence of two titin isoforms (short and long) with molecular weights approximately 3700 and approximately 3800 kDa in m. soleus, approximately 3400 and approximately 3600 kDa in m. psoas, approximately 3000 and approximately 3400 kDa in the left ventricle of myocardium was found. It was found that the content of the short titin isoform in the above muscles of hibernating and arousing ground squirrels is considerably lower than that of the long titin isoform. The preservation of the long titin isoform in skeletal and cardiac muscles of hibernating and arousing ground squirrels can be regarded as an evolutionarily determined adaptive mechanism favoring the survival of animal under extreme conditions without pathological consequences.
Vikhliantsev
I M
IM
Podlubnaia
Z A
ZA
D000818:Animals; D064211:Connectin; D004591:Electrophoresis, Polyacrylamide Gel; D006605:Hibernation; D009124:Muscle Proteins / Q000378:metabolism / Q000502:physiology*; D018482:Muscle, Skeletal / Q000378:metabolism / Q000502:physiology*; D009206:Myocardium / Q000378:metabolism*; D020033:Protein Isoforms / Q000378:metabolism / Q000502:physiology*; D011494:Protein Kinases / Q000378:metabolism / Q000502:physiology*; D012589:Sciuridae / Q000502:physiology*
D064211:Connectin; D009124:Muscle Proteins; D020033:Protein Isoforms; D011494:Protein Kinases