Changes in gene expression and titin (connectin) content in striated muscles of chronically alcoholized rats

Gritsyna, Yu. V.; Salmov, N. N.; Vikhlyantsev, I. M.; Уланова, А. Д.; Шарапов, М. Г.; Теплова, В. В.; Podlubnaya, Z. A.

doi:10.1134/s0026893313060058

Cited by 6 publications

(1 citation statement)

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“…It is known that the stay of humans and animals under conditions of gravitational unloading results in the atrophy of mainly slow fibers con taining MyHC isoform I [42,43]. The decrease in the proportion of slow MyHC isoform I was also shown in atrophied rat and human soleus muscle during the devel opment of pathological processes [44]. On the contrary, the atrophy of skeletal muscles of a hibernating long tailed ground squirrel Spermophilus undulatus is accompanied by an increase in the content of slow I and a decrease in the content of fast IIa and IIx/d isoforms of MyHCs [45].…”

Section: Study Of Seasonal Changes In Level Of Titin Phosphory Lationmentioning

confidence: 97%

Seasonal changes in isoform composition of giant proteins of thick and thin filaments and titin (connectin) phosphorylation level in striated muscles of bears (Ursidae, Mammalia)

Salmov

Vikhlyantsev

Уланова

et al. 2015

Biochemistry Moscow

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Seasonal changes in the isoform composition of thick and thin filament proteins (titin, myosin heavy chains (MyHCs), nebulin), as well as in the phosphorylation level of titin in striated muscles of brown bear (Ursus arctos) and hibernating Himalayan black bear (Ursus thibetanus ussuricus) were studied. We found that the changes that lead to skeletal muscle atrophy in bears during hibernation are not accompanied by a decrease in the content of nebulin and intact titin-1 (T1) isoforms. However, a decrease (2.1-3.4-fold) in the content of T2 fragments of titin was observed in bear skeletal muscles (m. gastrocnemius, m. longissimus dorsi, m. biceps) during hibernation. The content of the stiffer N2B titin isoform was observed to increase relative to the content of its more compliant N2BA isoform in the left ventricles of hibernating bears. At the same time, in spite of the absence of decrease in the total content of T1 in the myocardium of hibernating brown bear, the content of T2 fragments decreased ~1.6-fold. The level of titin phosphorylation only slightly increased in the cardiac muscle of hibernating brown bear. In the skeletal muscles of brown bear, the level of titin phosphorylation did not vary between seasons. However, changes in the composition of MyHCs aimed at increasing the content of slow (I) and decreasing the content of fast (IIa) isoforms of this protein during hibernation of brown bear were detected. Content of MyHCs I and IIa in the skeletal muscles of hibernating Himalayan black bear corresponded to that in the skeletal muscles of hibernating brown bear.

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