Publication: Emetine Regulates the Alternative Splicing of Bcl-x through a Protein Phosphatase 1-Dependent Mechanism
Issued Date
2007-12-26
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ISSN
10745521
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2-s2.0-37149011077
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Mahidol University
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SCOPUS
Bibliographic Citation
Chemistry and Biology. Vol.14, No.12 (2007), 1386-1392
Suggested Citation
Kritsanapol Boon-Unge, Qingming Yu, Tie Zou, An Zhou, Piyarat Govitrapong, Jianhua Zhou Emetine Regulates the Alternative Splicing of Bcl-x through a Protein Phosphatase 1-Dependent Mechanism. Chemistry and Biology. Vol.14, No.12 (2007), 1386-1392. doi:10.1016/j.chembiol.2007.11.004 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/24325
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Title
Emetine Regulates the Alternative Splicing of Bcl-x through a Protein Phosphatase 1-Dependent Mechanism
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Abstract
Exon 2 of the Bcl-x gene undergoes alternative splicing in which the Bcl-xS splice variant promotes apoptosis in contrast to the anti-apoptotic splice variant Bcl-xL. In this study, the regulation of the alternative splicing of pre-mRNA of Bcl-x was examined in response to emetine. Treatment of different types of cancer cells with emetine dihydrochloride downregulated the level of Bcl-xL mRNA with a concomitant increase in the mRNA level of Bcl-xS in a dose- and time-dependent manner. Pretreatment with calyculin A, an inhibitor of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), blocked emetine-induced alternative splicing in contrast to okadaic acid, a specific inhibitor of PP2A in cells, demonstrating a PP1-mediated mechanism. Our finding on the regulation of RNA splicing of members of the Bcl-2 family in response to emetine presents a potential target for cancer treatment. © 2007 Elsevier Ltd. All rights reserved.