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低温状态下的热休克蛋白:综述

Heat shock proteins in hypothermia: a review.

作者信息

Song Shang-Jin, Wu Guo-Cheng, Yi Li, Liu Xin, Jiang Ming-Min, Zhang Xiao-Chen, Yin Zi-Fei, Gu Wei, Ruan Yi

机构信息

School of Traditional Chinese Medicine, Naval Medical University, Shanghai, China.

Xingcheng Special Duty Sanatorium of Joint Logistics Support Force, Xingcheng, Liaoning, China.

出版信息

Front Mol Biosci. 2025 May 9;12:1564364. doi: 10.3389/fmolb.2025.1564364. eCollection 2025.

DOI:10.3389/fmolb.2025.1564364
PMID:40417060
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12098039/
Abstract

Hypothermia is a serious condition marked by a significant decrease in core body temperature, posing considerable risks to biological systems. In response to thermal stress, cells activate protective mechanisms, often synthesizing heat shock proteins (HSPs). These highly conserved proteins are crucial in cellular stress responses, primarily functioning as chaperones. HSPs facilitate correct protein folding and prevent misfolding and aggregation, thereby protecting cellular integrity during adverse conditions. This paper explains how HSPs alleviate stress responses related to low body temperature, focusing on energy metabolism, apoptosis, cellular membrane fluidity and stability, and stress signaling pathways. By enhancing cellular repair mechanisms, HSPs help maintain cellular balance and prevent further harm to the organism. Ultimately, the review emphasizes the complex relationship between cellular stress responses and HSPs in hypothermia, highlighting their potential as therapeutic targets for enhancing resistance to the harmful effects of extreme cold exposure. A deeper understanding of these mechanisms could lead to strategies that improve survival rates in hypothermic patients. It may also reveal ways to modulate HSPs' activity for enhanced cellular protection.

摘要

体温过低是一种严重的状况,其特征是核心体温显著下降,对生物系统构成相当大的风险。为应对热应激,细胞会激活保护机制,通常会合成热休克蛋白(HSPs)。这些高度保守的蛋白质在细胞应激反应中至关重要,主要起分子伴侣的作用。热休克蛋白促进蛋白质正确折叠,防止错误折叠和聚集,从而在不利条件下保护细胞完整性。本文解释了热休克蛋白如何减轻与低体温相关的应激反应,重点关注能量代谢、细胞凋亡、细胞膜流动性和稳定性以及应激信号通路。通过增强细胞修复机制,热休克蛋白有助于维持细胞平衡,防止对生物体造成进一步伤害。最终,该综述强调了低温下细胞应激反应与热休克蛋白之间的复杂关系,突出了它们作为增强对极端寒冷暴露有害影响抵抗力的治疗靶点的潜力。对这些机制的更深入理解可能会带来提高低温患者存活率的策略。它还可能揭示调节热休克蛋白活性以增强细胞保护的方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4288/12098039/b9624c7abbe3/fmolb-12-1564364-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4288/12098039/b9624c7abbe3/fmolb-12-1564364-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4288/12098039/b9624c7abbe3/fmolb-12-1564364-g001.jpg

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本文引用的文献

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Heat-shock protein 70 reduces apoptosis in the gills and hepatopancreas of Marsupenaeus japonicus under low-temperature stress.热休克蛋白70可降低低温胁迫下日本囊对虾鳃和肝胰腺中的细胞凋亡。
Int J Biol Macromol. 2025 May;307(Pt 1):141931. doi: 10.1016/j.ijbiomac.2025.141931. Epub 2025 Mar 9.
2
Electrocardiographic patterns of accidental hypothermia.意外低温的心电图模式。
Am J Emerg Med. 2025 Apr;90:210-213. doi: 10.1016/j.ajem.2025.01.079. Epub 2025 Jan 30.
3
The known unknowns of the Hsp90 chaperone.热休克蛋白90(Hsp90)分子伴侣的已知未知因素。
Elife. 2024 Dec 31;13:e102666. doi: 10.7554/eLife.102666.
4
When HSFs bring the heat-mapping the transcriptional circuitries of HSF-type regulators in .当热休克转录因子对热休克转录因子类型调节因子的转录回路进行热图绘制时。 (注:原句不完整,翻译仅供参考其大致意思,完整准确的翻译需结合完整句子)
mSphere. 2025 Jan 28;10(1):e0064423. doi: 10.1128/msphere.00644-23. Epub 2024 Dec 20.
5
Investigation of cold adaptation mechanisms by transcriptome analysis in the liver of yellowtail kingfish (Seriola aureovittata).通过转录组分析研究黄尾鰤(Seriola aureovittata)肝脏中的冷适应机制。
Comp Biochem Physiol Part D Genomics Proteomics. 2024 Dec;52:101358. doi: 10.1016/j.cbd.2024.101358. Epub 2024 Nov 10.
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Disrupting the protein-protein interaction network of Hsp72 inhibits adipogenic differentiation and lipid synthesis in adipocytes.破坏 Hsp72 的蛋白质-蛋白质相互作用网络可抑制脂肪细胞的成脂分化和脂质合成。
Cell Signal. 2024 Dec;124:111431. doi: 10.1016/j.cellsig.2024.111431. Epub 2024 Sep 21.
7
HSF1 is required for cellular adaptation to daily temperature fluctuations.HSF1 对于细胞适应每日温度波动是必需的。
Sci Rep. 2024 Sep 12;14(1):21361. doi: 10.1038/s41598-024-72415-x.
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Br J Pharmacol. 2024 Oct;181(20):3886-3907. doi: 10.1111/bph.16432. Epub 2024 Jun 16.