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Biochem Biophys Res Commun. 2006 Apr 21;342(4):1168-73. Epub 2006 Feb 23.

Histone deacetylase inhibitor apicidin induces cyclin E expression through Sp1 sites.

Author information

1
College of Pharmacy, Sungkyunkwan University, Suwon 440-746, Republic of Korea.

Abstract

We show that a histone deacetylase (HDAC) inhibitor apicidin increases the transcriptional activity of cyclin E gene, which results in accumulation of cyclin E mRNA and protein in a time- and dose-dependent manner. Interestingly, apicidin induction of cyclin E gene is found to be mediated by Sp1- rather than E2F-binding sites in the cyclin E promoter, as evidenced by the fact that specific inhibition of Sp1 leads to a decrease in apicidin activation of cyclin E promoter activity and protein expression, but mutation of E2F-binding sites of cyclin E promoter region fails to inhibit the ability of apicidin to activate cyclin E transcription. In addition, this transcriptional activation of cyclin E by apicidin is associated with histone hyperacetylation of cyclin E promoter region containing Sp1-binding sites. Our results demonstrate that regulation of histone modification by an HDAC inhibitor apicidin contributes to induction of cyclin E expression and this effect is Sp1-dependent.

PMID:
16516150
DOI:
10.1016/j.bbrc.2006.02.081
[Indexed for MEDLINE]

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