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[Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus].
Biofizika 2012 Nov-Dec; 57(6):982-7B

Abstract

Seasonal changes of the isoform composition of myosin heavy chains in skeletal muscles (m. triceps, m. longissimus dorsi, m. soleus, m. gastrocnemius, m. vastus lateralis) of hibernating ground squirrels Spermophilus undulatus were studied. Functional properties of myosin (the actin-activated ATPase activity and its Ca(2+)-sensitivity in vitro) were also examined. It was observed that the content of slow myosin heavy chain I isoform increased and the content of fast IIx/d isoform decreased in muscles of torpid ground squirrels and animals which are active in autumn and winter. In muscles of these animals the content of N2A-titin isorfom decreased although the relative content of NT-titin isoform, observed in striated muscles of mammals in our previous experimental works, increased. Actin-activated ATPase activity and Ca(2+)-sensitivity of myosin isolated from skeletal muscles of torpid and interbout ground squirrels were found to reduce. The changes observed are discussed in the context of adaptation of skeletal muscles of ground squirrels to hibernation conditions.

Authors

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Pub Type(s)

English Abstract
Journal Article

Language

rus

PubMed ID

23272578

Citation

Lazareva, M V., et al. "[Seasonal Changes in the Isoform Composition of the Myosin Heavy Chains in Skeletal Muscles of Hibernating Ground Squirrels Spermophilus Undulatus]." Biofizika, vol. 57, no. 6, 2012, pp. 982-7.
Lazareva MV, Trapeznikova KO, Vikhliantsev IM, et al. [Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus]. Biofizika. 2012;57(6):982-7.
Lazareva, M. V., Trapeznikova, K. O., Vikhliantsev, I. M., Bobylev, A. G., Klimov, A. A., & Podlubnaia, Z. A. (2012). [Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus]. Biofizika, 57(6), pp. 982-7.
Lazareva MV, et al. [Seasonal Changes in the Isoform Composition of the Myosin Heavy Chains in Skeletal Muscles of Hibernating Ground Squirrels Spermophilus Undulatus]. Biofizika. 2012;57(6):982-7. PubMed PMID: 23272578.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus]. AU - Lazareva,M V, AU - Trapeznikova,K O, AU - Vikhliantsev,I M, AU - Bobylev,A G, AU - Klimov,A A, AU - Podlubnaia,Z A, PY - 2013/1/1/entrez PY - 2013/1/1/pubmed PY - 2013/2/16/medline SP - 982 EP - 7 JF - Biofizika JO - Biofizika VL - 57 IS - 6 N2 - Seasonal changes of the isoform composition of myosin heavy chains in skeletal muscles (m. triceps, m. longissimus dorsi, m. soleus, m. gastrocnemius, m. vastus lateralis) of hibernating ground squirrels Spermophilus undulatus were studied. Functional properties of myosin (the actin-activated ATPase activity and its Ca(2+)-sensitivity in vitro) were also examined. It was observed that the content of slow myosin heavy chain I isoform increased and the content of fast IIx/d isoform decreased in muscles of torpid ground squirrels and animals which are active in autumn and winter. In muscles of these animals the content of N2A-titin isorfom decreased although the relative content of NT-titin isoform, observed in striated muscles of mammals in our previous experimental works, increased. Actin-activated ATPase activity and Ca(2+)-sensitivity of myosin isolated from skeletal muscles of torpid and interbout ground squirrels were found to reduce. The changes observed are discussed in the context of adaptation of skeletal muscles of ground squirrels to hibernation conditions. SN - 0006-3029 UR - https://www.unboundmedicine.com/medline/citation/23272578/[Seasonal_changes_in_the_isoform_composition_of_the_myosin_heavy_chains_in_skeletal_muscles_of_hibernating_ground_squirrels_Spermophilus_undulatus]_ DB - PRIME DP - Unbound Medicine ER -