热休克蛋白 70 介导的 Bcl-2 稳定性增加对氧化应激诱导的细胞凋亡的保护作用。
Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress.
机构信息
Department of Pathophysiology, Xiangya School of Medicine, Central South University, Changsha, Hunan, People's Republic of China.
出版信息
Cell Stress Chaperones. 2011 Mar;16(2):143-52. doi: 10.1007/s12192-010-0226-6. Epub 2010 Oct 3.
Abstract
We have previously shown that heat shock protein 70 (HSP70) markedly inhibits H(2)O(2)-induced apoptosis in mouse C2C12 myogenic cells by reducing the release of Smac. However, the molecular mechanism by which HSP70 interferes with Smac release during oxidative stress-induced apoptosis is not understood. In the current study, we showed that HSP70 increased the stability of Bcl-2 during oxidative stress. An antisense phosphorothioate oligonucleotide against Bcl-2 caused selective inhibition of Bcl-2 protein expression induced by HSP70 and significantly attenuated HSP70-mediated cell protection against H(2)O(2)-induced release of Smac and apoptosis. Taken together, our results indicate that there are important relationships among HSP70, Bcl-2, release of Smac, and induction of apoptosis by oxidative stress.
摘要
我们之前已经表明，热休克蛋白 70（HSP70）通过减少 Smac 的释放，显著抑制 H(2)O(2)-诱导的小鼠 C2C12 成肌细胞凋亡。然而，HSP70 在氧化应激诱导的细胞凋亡过程中干扰 Smac 释放的分子机制尚不清楚。在本研究中，我们表明 HSP70 在氧化应激过程中增加了 Bcl-2 的稳定性。针对 Bcl-2 的反义硫代磷酸寡核苷酸选择性地抑制了 HSP70 诱导的 Bcl-2 蛋白表达，并显著减弱了 HSP70 介导的对 H(2)O(2)-诱导的 Smac 释放和凋亡的细胞保护作用。总之，我们的结果表明，HSP70、Bcl-2、Smac 的释放和氧化应激诱导的凋亡之间存在重要关系。
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