[Changes in the isoform composition of the cytoskeletal protein titn--adaptation process in hibernation].
Changes in the isoform composition of the elastic protein titin from skeletal and cardiac muscles of hibernating ground squirrels were revealed for the first time. It was shown that, upon hibernation, the molecular mass of titin decreases and its functional properties change as compared with the active state of the animal. The physiological significance of the changes in titin isoform composition for the inhibition of muscle contractile activity upon hibernation is discussed in connection with similar changes during some cardiomyopathies.
Vikhliantsev
I M
IM
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
makarenko
I V
IV
Khalina
Ia N
IaN
Malyshev
S L
SL
Podlubnaia
Z A
ZA
D000818:Animals; D064211:Connectin; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000502:physiology; D006605:Hibernation / Q000502:physiology*; D009124:Muscle Proteins / Q000737:chemistry* / Q000502:physiology; D018482:Muscle, Skeletal / Q000737:chemistry; D009206:Myocardium / Q000737:chemistry; D020033:Protein Isoforms / Q000737:chemistry* / Q000502:physiology; D011494:Protein Kinases / Q000737:chemistry* / Q000502:physiology; D012589:Sciuridae / Q000502:physiology*
D064211:Connectin; D003598:Cytoskeletal Proteins; D009124:Muscle Proteins; D020033:Protein Isoforms; D011494:Protein Kinases