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• W1982805924 abstract "Because both iron deficiency and iron excess are deleterious to normal cell function, the intracellular level of iron must be tightly controlled. Ferritin, an iron binding protein, regulates iron balance by storing iron in a bioavailable but nontoxic form. Ferritin protein comprises two subunits: ferritin H, which contains ferroxidase activity, and ferritin L. Here we demonstrate that ferritin H mRNA and protein are induced by histone deacetylase inhibitors (HDAC inhibitors), a promising class of anti-cancer drugs, in cultured human cancer cells. Deletion analysis and EMSA assays reveal that the induction of ferritin H occurs at a transcriptional level via Sp1 and NF-Y binding sites near the transcriptional start site of the human ferritin H promoter. Classically, HDAC inhibitors modulate gene expression by increasing histone acetylation. However, ChIP assays demonstrate that HDAC inhibitors induce ferritin H transcription by increasing NF-Y binding to the ferritin H promoter without changes in histone acetylation. These results identify ferritin H as a new target of HDAC inhibitors, and recruitment of NF-Y as a novel mechanism of action of HDAC inhibitors." @default.
• W1982805924 created "2016-06-24" @default.
• W1982805924 creator A5025620869 @default.
• W1982805924 creator A5046597133 @default.
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• W1982805924 date "2010-08-01" @default.
• W1982805924 modified "2023-10-14" @default.
• W1982805924 title "Ferritin H induction by histone deacetylase inhibitors" @default.
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• W1982805924 doi "https://doi.org/10.1016/j.bcp.2010.04.008" @default.
• W1982805924 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2913600" @default.
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