title: A protein phosphatase is involved in the inhibition of histone deacetylation by sodium butyrate.
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.
authors.affiliation: Laboratoire de Biologie Moléculaire des Cellules Eucaryotes, I.C.G.M-EA 1501, Université Paris V, Faculté de Médecine, France.
authors.forename: L
authors.initials: L
authors.lastname: Cuisset
authors.forename: L
authors.initials: L
authors.lastname: Tichonicky
authors.forename: M
authors.initials: M
authors.lastname: Delpech
mesh_terms: D000123:Acetyltransferases / Q000187:drug effects*; D002087:Butyrates / Q000494:pharmacology*; D020148:Butyric Acid; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases / Q000187:drug effects*; D006657:Histones / Q000378:metabolism*; D008387:Marine Toxins; D019319:Okadaic Acid / Q000494:pharmacology; D010080:Oxazoles / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000187:drug effects*; D029701:Saccharomyces cerevisiae Proteins
chemical_list: D002087:Butyrates; D006657:Histones; D008387:Marine Toxins; D010080:Oxazoles; D029701:Saccharomyces cerevisiae Proteins; D020148:Butyric Acid; D019319:Okadaic Acid; C059041:calyculin A; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D010749:Phosphoprotein Phosphatases; D006655:Histone Deacetylases