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Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress

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Cell Stress and Chaperones Aims and scope

Abstract

We have previously shown that heat shock protein 70 (HSP70) markedly inhibits H2O2-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 H2O2-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.

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Abbreviations

HSP70:

Heat shock protein 70

H2O2 :

Hydrogen peroxide

IAPs:

Inhibitors of apoptosis proteins

Smac:

The second mitochondria-derived activator of caspases

COX II:

Cytochrome oxidase subunit II

DTT:

Dithiothreitol

DMEM:

Dulbecco’s modified Eagle’s medium

PBS:

Phospate-buffered saline

Apaf-1:

Apoptotic protease activating factor-1

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Acknowledgments

This study was supported by the grants from National Basic Research Program of China (2007CB512007) and The National Natural Science Foundation of China (30700290).

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Correspondence to Xianzhong Xiao.

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Bimei Jiang and Pengfei Liang made equal contributions to the study.

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Jiang, B., Liang, P., Deng, G. et al. Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress. Cell Stress and Chaperones 16, 143–152 (2011). https://doi.org/10.1007/s12192-010-0226-6

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  • DOI: https://doi.org/10.1007/s12192-010-0226-6

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