Abstract
Bik, a BH3-only protein, was identified to induce cells apoptosis. In this study, we reported that Bik exclusively localized to endoplasmic reticulum rather than mitochondria. The apoptosis induced by Bik was inhibited in Hep3B cells, when TM domain of Bik was truncated. The ectopic overexpression of Bik protein caused the rapid and sustained elevation of the intracellular cytosolic Ca2+, which originated from the ER Ca2+ stores releasing. The Hep3B cells apoptosis induced by Bik was not prevented by establishing the clamped cytosolic Ca2+ condition, or by buffering of the extracellular Ca2+ with EGTA, suggesting that the depletion of ER Ca2+ stores rather than the elevation of cytosolic Ca2+ or the extracellular Ca2+ entry contributed to Bik-induced Hep3B cells apoptosis.
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Abbreviations
- ER:
-
Endoplasmic reticulum
- TG:
-
Thapsigargin
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Acknowledgments
This work was supported by The National Key Program for Basic Research of China (2004CB518804), The Science and Technology Commission of Shanghai (01JC14025, 04JC14041 and 07JC14034) and The Basic Medicine Research Foundation of Shanghai Renji Hospital (ZD0702).
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The authors Xiaoping Zhao and Li Wang contributed equally to this work.
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Zhao, X., Wang, L., Sun, Y. et al. The endoplasmic reticulum (ER)-target protein Bik induces Hep3B cells apoptosis by the depletion of the ER Ca2+ stores. Mol Cell Biochem 312, 33–38 (2008). https://doi.org/10.1007/s11010-008-9718-4
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DOI: https://doi.org/10.1007/s11010-008-9718-4