TAILIEUCHUNG - Báo cáo khoa học: The transcription factor ZBP-89 suppresses p16 expression through a histone modification mechanism to affect cell senescence

The transcription factor ZBP-89 has been implicated in the induction of growth arrest and apoptosis. In this article, we demonstrate that ZBP-89 was able to restrain senescence in NCI-H460 human lung cancer cells, through epigenetically regulating p16 INK4a expression. | ỊFEBS Journal The transcription factor ZBP-89 suppresses p16 expression through a histone modification mechanism to affect cell senescence Yunpeng Feng Xiuli Wang Liang Xu Hong Pan Shan Zhu Qian Liang Baiqu Huang and Jun Lu Institute of Genetics and Cytology Northeast Normal university and the Key Laboratory of Molecular Epigenetics of Ministry of Education MOE Northeast NormalUniversity Changchun China Keywords histone deacetylase 3 HDAC3 histone deacetylase 4 HDAC4 p16 senescence ZBP-89 Correspondence J. Lu Institute of Genetics and Cytology and the Key Laboratory of Molecular Epigenetics of MOE Northeast Normal University 5268 Renmin Street Changchun 130024 China Fax 86 431 85099768 Tel 86 431 85099798 E-mail luj809@ These authors contributed equally to this work Received 1 April2009 revised 29 May 2009 accepted 3 June 2009 doi The transcription factor ZBP-89 has been implicated in the induction of growth arrest and apoptosis. In this article we demonstrate that ZBP-89 was able to restrain senescence in NCI-H460 human lung cancer cells through epigenetically regulating p16INK4a expression. Specifically our results indicate that knockdown of ZBP-89 by RNA interference stimulated cellular senescence in NCI-H460 cells as judged by the senescence-associated b-galactosidase activity assay and senescence-associated heterochromatin foci assay and this process could be reversed by RNA interference-mediated p16INK4a silencing. We also show that histone deacetylase HDAC 3 and HDAC4 inhibited p16INK4a promoter activity in a dose-dependent manner. Furthermore chromatin immunoprecipitation assays verified that HDAC3 was recruited to the p16INK4a promoter by ZBP-89 through an epigenetic mechanism involving histone acetylation modification. Moreover immunofluorescence and coimmunoprecipitation assays revealed that ZBP-89 and HDAC3 formed a complex. These data suggest that ZBP-89 and HDAC3 but not HDAC4 can work coordinately to .

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