Effect of the histone deacetylase inhibitor trichostatin A on the responsiveness of rat hepatocytes to dioxin

Biochemical Pharmacology
L XuM F Ruh

Abstract

Since histone acetylation has been implicated in the facilitation of specific gene transcription, we investigated the effect of increasing histone acetylation through inhibition of histone deacetylase on 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) induction of P4501A activity in cultured rat hepatocytes. Inhibition of histone deacetylation was accomplished with addition of trichostatin A (TSA) to the incubation medium, and P4501A activity was measured spectrofluorometrically by determination of the rate of resorufin formation by ethoxyresorufin-O-deethylase (EROD). While TSA alone (5-200 ng/mL) had no effect on EROD activity, TSA potentiated the effect of various concentrations (10(-12) to 10(-10) M) of TCDD. Addition of 200 ng TSA/mL with TCDD resulted in an increased EROD activity of approximately 200% compared with TCDD alone. When TSA was removed from the cells after various incubation times (2, 6, 24 hr) by successive washings with TSA-free medium, it was determined that TSA was required for 24 hr in order to potentiate the effects of a 48-hr incubation with TCDD. In addition to measurement of EROD activity, P4501A1 and 1A2 microsomal protein were determined by western immunoblotting analysis. While neither P4501A1 nor 1A2 ...Continue Reading

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Citations

Feb 10, 2000·Archives of Biochemistry and Biophysics·P M GarrisonM S Denison
Aug 21, 2007·Biochimica Et Biophysica Acta·Michael SchnekenburgerAlvaro Puga
Aug 25, 2004·Biochemical and Biophysical Research Communications·Frédérique FalloneBruno Lacarelle
Jan 21, 2017·BioMed Research International·Rebeca Santes-PalaciosJesús Javier Espinosa-Aguirre

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