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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)

N. N. Salmov1, I. M. Vikhlyantsev1*, A. D. Ulanova1,2, Yu. V. Gritsyna1, A. G. Bobylev1, A. P. Saveljev3, V. V. Makariushchenko3, G. Yu. Maksudov4, and Z. A. Podlubnaya1,2

1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, ul. Institutskaya 3, 142290 Pushchino, Moscow Region, Russia; fax: +7 (4967) 33-0553; E-mail: vikhlyantsev@iteb.ru

2Pushchino State Institute of Natural Sciences, pr. Nauki 3, 142290 Pushchino, Moscow Region, Russia; fax: +7 (4967) 73-2711

3Zhitkov Russian Research Institute of Game Management and Fur Farming, ul. Preobrazhenskaya 79, 610000 Kirov, Russia; fax: +7 (8332) 38-1130

4Moscow Zoo, ul. Bol’shaya Gruzinskaya 1, 123242 Moscow, Russia; fax: +7 (495) 605-1717

* To whom correspondence should be addressed.

Received September 25, 2014; Revision received December 1, 2014
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.
KEY WORDS: hibernation, brown bear, Himalayan black bear, striated muscles, thick (myosin) filaments, thin (actin) filaments, titin, nebulin, isoforms of myosin heavy chains, Pro-Q Diamond

DOI: 10.1134/S0006297915030098