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Regulation of CYP1A2 by histone deacetylase inhibitors in mouse hepatocytes
Author(s) -
Jin Bohwan,
Ryu DougYoung
Publication year - 2004
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20017
Subject(s) - cyp1a2 , trichostatin a , sodium butyrate , histone deacetylase , chemistry , histone deacetylase 2 , hdac11 , hdac10 , histone deacetylase inhibitor , histone , hdac1 , histone deacetylase 5 , cytochrome p450 , microbiology and biotechnology , biochemistry , biology , enzyme , gene
Abstract Cytochrome P450 1A2 (CYP1A2) is constitutively expressed in the mouse liver, but the constitutive expression progressively declines to an undetectable level in isolated hepatocytes. In this study, CYP1A2 was induced in hepatocytes exposed to the histone deacetylase inhibitors trichostatin A (TSA) and sodium butyrate (SB), but only well after constitutive CYP1A2 expression was silenced. However, cotreatment with the arylhydrocarbon receptor (AhR) ligand 2,3,7,8‐tetrachlorodibenzo‐ p ‐dioxin (TCDD) and either TSA or SB reduced the induction of CYP1A2 with the same time course as TSA or SB increased its induction. These results suggest that histone modification is involved in CYP1A2 regulation in hepatocytes through pathways that are independent of AhR. © 2004 Wiley Periodicals, Inc. J Biochem Mol Toxicol 18:131–132, 2004; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20017