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. 2019 Sep 20;10:1221. doi: 10.3389/fphys.2019.01221

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Copyright © 2019 Ulanova, Gritsyna, Salmov, Lomonosova, Belova, Nemirovskaya, Shenkman and Vikhlyantsev.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Levels of intact titin-1 (T1) and proteolytic fragments (T2) in the soleus muscle of rats. (A) SDS-PAGE analysis of titin expression in the soleus muscle of rats. MyHC – myosin heavy chains. T2 (m.w. ∼2000–2100 kDa) are proteolytic fragments of titin. NT and N2A are isoforms of intact titin-1 (T1, m.w. ∼3400–3700 kDa in skeletal muscles). High molecular weight titin isoforms (denoted as NT-titin) were found in striated muscles of mammals (Vikhlyantsev and Podlubnaya, 2017). Plots of densitometric quantification of the T1 content (B) and T2 content (C) relative to MyHC content (n = 5). ^∗P < 0.05 as compared to control group. Values are means ± SD.