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 Blood, 15 November 2006, Vol. 108, No. 10, pp. 3590-3599.
Prepublished online as a Blood First Edition Paper on August 8, 2006; DOI 10.1182/blood-2006-01-023713.

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RED CELLS

Mechanism for fetal hemoglobin induction by histone deacetylase inhibitors involves {gamma}-globin activation by CREB1 and ATF-2

Jose Sangerman, Moo Seung Lee, Xiao Yao, Eugene Oteng, Cheng-Hui Hsiao, Wei Li, Sima Zein, Solomon F. Ofori-Acquah, and Betty S. Pace

From the Department of Pediatrics, Yale University, New Haven, CT; the Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson; and the Department of Cell Biology and Neuroscience, University of South Alabama, Mobile.

The histone deacetylase inhibitors (HDA-CIs) butyrate and trichostatin A activate {gamma}-globin expression via a p38 mitogen-activating protein kinase (MAPK)-dependent mechanism. We hypothesized that down-stream effectors of p38 MAPK, namely activating transcription factor-2 (ATF-2) and cyclic AMP response element (CRE) binding protein (CREB), are intimately involved in fetal hemoglobin induction by these agents. In this study, we observed increased ATF-2 and CREB1 phosphorylation mediated by the HDACIs in K562 cells, in conjunction with histone H4 hyperacetylation. Moreover, enhanced DNA-protein interactions occurred in the CRE in the G{gamma}-globin promoter (G-CRE) in vitro after drug treatments; subsequent chromatin immunoprecipitation assay confirmed ATF-2 and CREB1 binding to the G-CRE in vivo. Enforced expression of ATF-2 and CREB produced G{gamma}-promoter trans-activation which was abolished by a 2-base pair mutation in the putative G-CRE. The data presented herein demonstrate that {gamma}-gene induction by butyrate and trichostatin A involves ATF-2 and CREB1 activation via p38 MAPK signaling.


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