Proteostasis of Heat Shock Protein HSP90 in Skeletal Muscles of the Long-Tailed Ground Squirrel during Hibernation

IF 4.033 Q4 Biochemistry, Genetics and Molecular Biology Biophysics Pub Date : 2024-03-07 DOI:10.1134/s000635092305010x
Yu. V. Gritsyna, S. S. Popova, G. Z. Mikhailova, L. G. Bobyleva, S. N. Udaltsov, O. S. Morenkov, N. M. Zakharova, I. M. Vikhlyantsev
{"title":"Proteostasis of Heat Shock Protein HSP90 in Skeletal Muscles of the Long-Tailed Ground Squirrel during Hibernation","authors":"Yu. V. Gritsyna, S. S. Popova, G. Z. Mikhailova, L. G. Bobyleva, S. N. Udaltsov, O. S. Morenkov, N. M. Zakharova, I. M. Vikhlyantsev","doi":"10.1134/s000635092305010x","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Changes in the content of heat shock protein 90 (HSP90) in m. soleus (contains mainly fibers expressing the “slow” isoform I MyHC) and m. gastrocnemius (contains mainly fibers expressing the “fast” isoforms II MyHC) of a true hibernant, the long-tailed ground squirrel (<i>Urocitellus undulatus</i>), during different periods of the annual cycle, summer activity (seasonal control), hypothermia/winter torpor, and winter (interbout) activity, were studied. It was found that despite the development of atrophic changes that were more pronounced in the “fast” m. gastrocnemius, the content of HSP90 in both muscles did not change throughout the hibernation period. The role of HSP90 in maintaining the stability of the titin giant sarcomeric protein molecules during the periods of the animal’s entry into and exit from hypothermia, when the activity of calpain proteases increased due to the increased content of Ca<sup>2+</sup> in the cytosol of muscle cells, as well as during hypothermia, when the activity of calpains most likely was not completely inhibited, was discussed. During the winter/interbout activity, when there was an increased titin turnover in the striated ground squirrel muscles, a constant content of HSP90 was apparently necessary for the correct folding of newly synthesized titin molecules and their embedding into sarcomeres, as well as for the removal of improperly folded and old titin molecules/fragments, as well as other proteins. Thus, HSP90 proteostasis in skeletal muscles of the long-tailed ground squirrel could contribute to maintaining a stable level of titin and, possibly, other sarcomeric proteins during hibernation, which, in turn, would contribute to maintaining a highly ordered sarcomeric structure and the necessary level of contractile muscle activity in different phases of the hibernation–wakefulness cycle.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":null,"pages":null},"PeriodicalIF":4.0330,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics","FirstCategoryId":"4","ListUrlMain":"https://doi.org/10.1134/s000635092305010x","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0

Abstract

Changes in the content of heat shock protein 90 (HSP90) in m. soleus (contains mainly fibers expressing the “slow” isoform I MyHC) and m. gastrocnemius (contains mainly fibers expressing the “fast” isoforms II MyHC) of a true hibernant, the long-tailed ground squirrel (Urocitellus undulatus), during different periods of the annual cycle, summer activity (seasonal control), hypothermia/winter torpor, and winter (interbout) activity, were studied. It was found that despite the development of atrophic changes that were more pronounced in the “fast” m. gastrocnemius, the content of HSP90 in both muscles did not change throughout the hibernation period. The role of HSP90 in maintaining the stability of the titin giant sarcomeric protein molecules during the periods of the animal’s entry into and exit from hypothermia, when the activity of calpain proteases increased due to the increased content of Ca2+ in the cytosol of muscle cells, as well as during hypothermia, when the activity of calpains most likely was not completely inhibited, was discussed. During the winter/interbout activity, when there was an increased titin turnover in the striated ground squirrel muscles, a constant content of HSP90 was apparently necessary for the correct folding of newly synthesized titin molecules and their embedding into sarcomeres, as well as for the removal of improperly folded and old titin molecules/fragments, as well as other proteins. Thus, HSP90 proteostasis in skeletal muscles of the long-tailed ground squirrel could contribute to maintaining a stable level of titin and, possibly, other sarcomeric proteins during hibernation, which, in turn, would contribute to maintaining a highly ordered sarcomeric structure and the necessary level of contractile muscle activity in different phases of the hibernation–wakefulness cycle.

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
冬眠期间长尾地松鼠骨骼肌中热休克蛋白 HSP90 的蛋白稳态
摘要真正冬眠的长尾地松鼠(Urocitellus undulatus)的比目鱼肌(主要含有表达 "慢 "异构体I MyHC的纤维)和腓肠肌(主要含有表达 "快 "异构体II MyHC的纤维)中热休克蛋白90(HSP90)含量的变化。研究了真正冬眠的长尾地松鼠(Urocitellus undulatus)在年周期的不同时期(夏季活动(季节控制)、低温/冬季冬眠和冬季(间歇期)活动)中比目鱼肌(主要含有表达 "慢 "异构体 I MyHC 的纤维)和腓肠肌(主要含有表达 "快 "异构体 II MyHC 的纤维)中热休克蛋白 90(HSP90)含量的变化。研究发现,尽管腓肠肌的萎缩性变化在 "快速 "腓肠肌中更为明显,但两块肌肉中的 HSP90 含量在整个冬眠期都没有变化。在动物进入低体温期和脱离低体温期,钙蛋白酶的活性会因肌肉细胞胞质中 Ca2+ 含量的增加而增加,而在低体温期,钙蛋白酶的活性很可能没有被完全抑制,因此讨论了 HSP90 在维持 titin 巨型肉瘤蛋白分子稳定性方面的作用。在冬季/冬季活动期间,横纹肌中的钛蛋白更替增加,HSP90的恒定含量显然是新合成的钛蛋白分子正确折叠和嵌入肌节,以及清除折叠不当和老化的钛蛋白分子/碎片及其他蛋白质所必需的。因此,长尾地松鼠骨骼肌中的HSP90蛋白稳态可能有助于在冬眠期间维持稳定水平的钛蛋白以及其他肉瘤蛋白,这反过来又有助于在冬眠-觉醒周期的不同阶段维持高度有序的肉瘤结构和必要水平的收缩肌活动。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Biophysics
Biophysics Biochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍: Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.
期刊最新文献
Chlorophyllin Inhibits Lipid Peroxidation Triggered by the Fenton Reaction Secondary Metabolites and Amino Acids in the Neocortex of the Long-Tailed Ground Squirrel Urocitellus undulatus at Different Stages of Hibernation Superoxide Generating Activity of Nicotinamide Coenzymes Annotation of a New Low-Threshold Potential-Dependent Calcium Channel of Trichoplax adhaerens (Phylum Placozoa) Spatial Structure of the Casoxin C Molecule
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1