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A more recent version of this article appeared on August 1, 2005

Papers In Press, published online ahead of print February 16, 2005
J. Lipid Res., doi:10.1194/jlr.M400424-JLR200
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Submitted on October 26, 2004
Revised on January 25, 2005
Accepted on February 2, 2005

Histone deacetylase 1: a target of 9-hydroxystearic acid in the inhibition of cell growth in human colon cancer

Natalia Calonghi, Concettina Cappadone, Eleonora Pagnotta, Carla Boga, Carlo Bertucci, Jessica Fiori, Gianluca Tasco, Rita Casadio, and Lanfranco Masotti

Biochemistry G.Moruzzi, University of Bologna, Bologna 40126

Corresponding Author: natalia.calonghi{at}unibo.it

Recent studies have shown that an endogenous lipoperoxidation product, 9-hydroxystearic acid (9-HSA), acts in colon carcinoma cells (HT29) as a growth inhibitor by inducing p21WAF1 in an immediate-early, p53 independent fashion, and that p21WAF1 is required for 9-HSA mediated growth arrest in HT29. It is therefore conceavable to hypothesize that the cytostatic effect induced by this agent can be at least partially associated to a molecular mechanism which involves histone deacetylase 1 (HDAC1) inhibition as demonstrated for sodium butyrate and other specific inhibitors, such as trichostatin A and hydroxamic acids. In the present paper we show that, after administration, 9-HSA causes an accumulation of hyperacetylated histones, and strongly inhibits the activity of HDAC1. The interaction of 9-HSA with the catalytic site of the enzyme has then been highlighted by computational modelling of the human HDAC1 using its homologue from the hyperthermophilic Aquifex aeolicus as a template. Consistently with the experimental data we find that 9-HSA can bind to the active site of the protein, showing that the inhibition of the enzyme can be explained at the molecular level by the ligand/protein interaction.


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Endogenous inhibition of histone deacetylase 1 by tumor-suppressive maspin.
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[Abstract] [Full Text] [PDF]


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