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A Protein Phosphatase Is Involved in the Inhibition of Histone Deacetylation by Sodium Butyrate

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Abstract

Treatment of cells with sodium butyrate is known to increase histone acetylation by inhibiting deacetylases. Here we have observed, in cultured hepatoma cells, that the potent serine-threonine phosphatase inhibitors, okadaic acid or calyculin A, inhibited phosphatase activity and concomitantly decreased the histone acetylation classically maintained by sodium butyrate. These results suggest that a protein phosphatase may mediate the sodium butyrate effect on deacetylases. Since we have previously found that such a protein would also mediate the sodium butyrate effect on gene expression, we propose that a phosphatase activity constitutes an early and essential step in the sodium butyrate-triggered signalling pathway.

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    Correspondence should be addressed to Dr Marc Delpech, ICGM-EA 1501, CHU Cochin, 24 rue du Fg St Jacques 75014 Paris, France. Fax:33 1 44 41 24 85. E-mail:[email protected].

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