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

Bimei Jiang, Pengfei Liang, Gonghua Deng, Zizhi Tu, Meidong Liu and Xianzhong Xiao
Cell Stress & Chaperones
Vol. 16, No. 2 (MARCH 2011), pp. 143-152
Published by: Cell Stress Society International in partnership with Springer
Stable URL: http://www.jstor.org/stable/41331355
Page Count: 10
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Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress
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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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