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

By Bimei Jiang, Pengfei Liang, Gonghua Deng, Zizhi Tu, Meidong Liu and Xianzhong Xiao

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

Topics: Original Paper
Publisher: Springer Netherlands
OAI identifier: oai:pubmedcentral.nih.gov:3059790
Provided by: PubMed Central
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