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热休克蛋白:凋亡性细胞死亡的内源性调节因子。

Heat shock proteins: endogenous modulators of apoptotic cell death.

作者信息

Didelot C, Schmitt E, Brunet M, Maingret L, Parcellier A, Garrido C

机构信息

Faculty of Medicine and Pharmacy, INSERM U-517, Dijon, France.

出版信息

Handb Exp Pharmacol. 2006(172):171-98. doi: 10.1007/3-540-29717-0_8.

Abstract

The highly conserved heat shock proteins (Hsps) accumulate in cells exposed to heat and a variety of other stressful stimuli. Hsps, that function mainly as molecular chaperones, allow cells to adapt to gradual changes in their environment and to survive in otherwise lethal conditions. The events of cell stress and cell death are linked and Hsps induced in response to stress appear to function at key regulatory points in the control of apoptosis. Hsps include anti-apoptotic and pro-apoptotic proteins that interact with a variety of cellular proteins involved in apoptosis. Their expression level can determine the fate of the cell in response to a death stimulus, and apoptosis-inhibitory Hsps, in particular Hsp27 and Hsp70, may participate in carcinogenesis. This review summarizes the apoptosis-regulatory function of Hsps.

摘要

高度保守的热休克蛋白(Hsps)在暴露于热及多种其他应激刺激的细胞中积累。Hsps主要作为分子伴侣发挥作用,使细胞能够适应环境的逐渐变化并在其他致命条件下存活。细胞应激和细胞死亡事件相互关联,应激诱导产生的Hsps似乎在细胞凋亡控制的关键调节点发挥作用。Hsps包括与多种参与细胞凋亡的细胞蛋白相互作用的抗凋亡和促凋亡蛋白。它们的表达水平可决定细胞对死亡刺激的反应命运,尤其是Hsp27和Hsp70等凋亡抑制性Hsps可能参与致癌过程。本综述总结了Hsps的细胞凋亡调节功能。

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