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http://dx.doi.org/10.5483/BMBRep.2011.44.3.176

Differentiation and upregulation of heat shock protein 70 induced by a subset of histone deacetylase inhibitors in mouse and human embryonic stem cells  

Park, Jeong-A (Department of Biochemistry, College of Natural Sciences, Chungbuk National University)
Kim, Young-Eun (Department of Biochemistry, College of Natural Sciences, Chungbuk National University)
Seok, Hyun-Jeong (Department of Biochemistry, College of Natural Sciences, Chungbuk National University)
Park, Woo-Youn (Department of Radiation Oncology, College of Medicine, Chungbuk National University)
Kwon, Hyung-Joo (Center for Medical Science Research, College of Medicine, Hallym University)
Lee, Young-Hee (Department of Biochemistry, College of Natural Sciences, Chungbuk National University)
Publication Information
BMB Reports / v.44, no.3, 2011 , pp. 176-181 More about this Journal
Abstract
Inhibiting histone deacetylase (HDAC) activity modulates the epigenetic status of cells, resulting in an alteration of gene expression and cellular function. Here, we investigated the effects of HDAC inhibitors on mouse embryonic stem (ES) cells. The HDAC inhibitors trichostatin A, suberoylanilide hydroxamic acid, sodium butyrate, and valproic acid induced early differentiation of mouse ES cells and triggered induction of heat-shock protein (HSP)70. In contrast, class III HDAC inhibitors failed to induce differentiation or HSP70 expression. Transcriptional upregulation of HSP70 was confirmed by mRNA expression analysis, an inhibitor study, and chromatin immunoprecipitation. HSP70 induction was dependent on the SAPK/JNK, p38, and PI3K/Akt pathways. Differentiation and induction of HSP70 by a subset of HDAC inhibitors was also examined in human ES cells, which suggests that the phenomenon generally occurs in ES cells. A better understanding of the effects of HDAC inhibitors may give more insight into their application in stem cell biology.
Keywords
Differentiation; Embryonic stem cells; HDAC inhibitor; HSP70;
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