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[The behavior of titin and the proteins of its family from skeletal muscles of ground squirrel (Citellus undulatus) during hibernation and rats under conditions of simulated microgravity].
Biofizika 2004 Nov-Dec; 49(6):995-1002B

Abstract

By the use of SDS PAGE, the behavior of titin and MyBP-C in fast (m. psoas) as well as titin and MyBP-X in slow (m. soleus) muscles of ground squirrels (Citellus undulatus) during hibernation was compared with the behavior of titin and MyBP-X in rat m. soleus under conditions of simulated microgravity. A decrease in the amount of titin 1 and MyBP-C relative to that of myosin heavy chains by approximately 30% and approximately 40%, correspondingly, in muscles of hibernating and arousing ground squirrels was revealed in comparison with active animals. No differences in the relative amount of MyBP-X in m. soleus of hibernating, arousing and active ground squirrels were found. Under conditions of simulated microgravity, a decrease in the amount of titin 1 by approximately 2 times and MyBP-X by approximately1.5 times relative to that of myosin heavy chains in rat m. soleus was observed. By the method of SDS PAGE modified by us, an almost twofold decrease in the amount of short isovariants of the titin N2A isoform relative to that of myosin heavy chains was shown in muscles of hibernating and arousing ground squirrels, whereas no changes were found in the amount of long titin isovariants. The conditions of simulated microgravity resulted in a twofold decrease in the relative amount of both short and long titin isovariants in rat m. soleus. The results indicate that hibernating ground squirrels have an evolutionarily determined adaptive mechanism of selective degradation of fast muscle fibers and preservation or increase of slow fibers, as the most economic and energetically advantageous, with proteins typical of them. The microgravitation of nonhibernating animals (rats) leads to a non-selective degradation of MyBP-X and titin isovariants, which contributes to considerable atrophy of soleus fibers.

Authors

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Pub Type(s)

Comparative Study
English Abstract
Journal Article

Language

rus

PubMed ID

15612538

Citation

Vikhliantsev, I M., et al. "[The Behavior of Titin and the Proteins of Its Family From Skeletal Muscles of Ground Squirrel (Citellus Undulatus) During Hibernation and Rats Under Conditions of Simulated Microgravity]." Biofizika, vol. 49, no. 6, 2004, pp. 995-1002.
Vikhliantsev IM, Malyshev SL, Shenkman BS, et al. [The behavior of titin and the proteins of its family from skeletal muscles of ground squirrel (Citellus undulatus) during hibernation and rats under conditions of simulated microgravity]. Biofizika. 2004;49(6):995-1002.
Vikhliantsev, I. M., Malyshev, S. L., Shenkman, B. S., & Podlubnaia, Z. A. (2004). [The behavior of titin and the proteins of its family from skeletal muscles of ground squirrel (Citellus undulatus) during hibernation and rats under conditions of simulated microgravity]. Biofizika, 49(6), pp. 995-1002.
Vikhliantsev IM, et al. [The Behavior of Titin and the Proteins of Its Family From Skeletal Muscles of Ground Squirrel (Citellus Undulatus) During Hibernation and Rats Under Conditions of Simulated Microgravity]. Biofizika. 2004;49(6):995-1002. PubMed PMID: 15612538.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [The behavior of titin and the proteins of its family from skeletal muscles of ground squirrel (Citellus undulatus) during hibernation and rats under conditions of simulated microgravity]. AU - Vikhliantsev,I M, AU - Malyshev,S L, AU - Shenkman,B S, AU - Podlubnaia,Z A, PY - 2004/12/23/pubmed PY - 2005/5/14/medline PY - 2004/12/23/entrez SP - 995 EP - 1002 JF - Biofizika JO - Biofizika VL - 49 IS - 6 N2 - By the use of SDS PAGE, the behavior of titin and MyBP-C in fast (m. psoas) as well as titin and MyBP-X in slow (m. soleus) muscles of ground squirrels (Citellus undulatus) during hibernation was compared with the behavior of titin and MyBP-X in rat m. soleus under conditions of simulated microgravity. A decrease in the amount of titin 1 and MyBP-C relative to that of myosin heavy chains by approximately 30% and approximately 40%, correspondingly, in muscles of hibernating and arousing ground squirrels was revealed in comparison with active animals. No differences in the relative amount of MyBP-X in m. soleus of hibernating, arousing and active ground squirrels were found. Under conditions of simulated microgravity, a decrease in the amount of titin 1 by approximately 2 times and MyBP-X by approximately1.5 times relative to that of myosin heavy chains in rat m. soleus was observed. By the method of SDS PAGE modified by us, an almost twofold decrease in the amount of short isovariants of the titin N2A isoform relative to that of myosin heavy chains was shown in muscles of hibernating and arousing ground squirrels, whereas no changes were found in the amount of long titin isovariants. The conditions of simulated microgravity resulted in a twofold decrease in the relative amount of both short and long titin isovariants in rat m. soleus. The results indicate that hibernating ground squirrels have an evolutionarily determined adaptive mechanism of selective degradation of fast muscle fibers and preservation or increase of slow fibers, as the most economic and energetically advantageous, with proteins typical of them. The microgravitation of nonhibernating animals (rats) leads to a non-selective degradation of MyBP-X and titin isovariants, which contributes to considerable atrophy of soleus fibers. SN - 0006-3029 UR - https://www.unboundmedicine.com/medline/citation/15612538/[The_behavior_of_titin_and_the_proteins_of_its_family_from_skeletal_muscles_of_ground_squirrel__Citellus_undulatus__during_hibernation_and_rats_under_conditions_of_simulated_microgravity]_ DB - PRIME DP - Unbound Medicine ER -