TAILIEUCHUNG - Báo cáo khoa học: ATP-binding domain of heat shock protein 70 is essential for its effects on the inhibition of the release of the second mitochondria-derived activator of caspase and apoptosis in C2C12 cells

Hydrogen peroxide (H2O2) is a well known oxidative stress inducer causing apoptosis of many cells. Previously, we have shown that heat shock pre-treatment blocked the release of the second mitochondria-derived activator of caspase (Smac) to the cytosol and inhibited apoptosis of C2C12 myo-blast cells in response to H2O2. | ATP-binding domain of heat shock protein 70 is essential for its effects on the inhibition of the release of the second mitochondria-derived activator of caspase and apoptosis in C2C12 cells Bimei Jiang1 Kangkai Wang1 Pengfei Liang2 Weimin Xiao1 Haiyun Wang1 and Xianzhong Xiao1 1 Department of Pathophysiology Xiangya Schoolof Medicine CentralSouth University Changsha Hunan China 2 Department of Burns and plastic surgery Xiangya Hospital CentralSouth University Changsha Hunan China Keywords apoptosis heat shock protein 70 hydrogen peroxide mitochondria Smac Correspondence X. Xiao Department of Pathophysiology Xiangya School of Medicine Central South University Changsha Hunan 410008 China Fax Tel 86 731 2355019 E-mail xianzhongxiao@ Received 8 December 2008 revised 14 February 2009 accepted 2 March 2009 doi Hydrogen peroxide H2O2 is a well known oxidative stress inducer causing apoptosis of many cells. Previously we have shown that heat shock pretreatment blocked the release of the second mitochondria-derived activator of caspase Smac to the cytosol and inhibited apoptosis of C2C12 myoblast cells in response to H2O2. The present study aimed to elucidate the underlying mechanism by over-expressing a major stress-inducible protein heat shock protein HSP 70 and characterizing the resulting cellular changes. We demonstrate that HSP70 over-expression markedly inhibited the release of Smac and prevented the activation of caspases-9 and -3 and apoptosis in C2C12 cells under H2O2 treatment. However no direct interaction between HSP70 and Smac was observed by co-immunoprecipitation. Mutational analysis demonstrated that the ATP-binding domain of HSP70 rather than the peptide-binding domain was essential for these observed HSP functions. Taken together our results provide evidence supporting the role of HSP70 in the protection of C2C12 cells from H2O2-induced and Smac-promoted apoptosis by preventing the release of Smac from mitochondria

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