Histone modification in liver after administration of inducers of mixed function oxidase activity

Procaccini, Robert L.; Bresnick, Edward

doi:10.1016/0009-2797(75)90028-9

Cited by 11 publications

(4 citation statements)

References 22 publications

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“…PB enhances histone acetylation (Procaccini & Bresnick, 1975) and the phosphorylation of acidic proteins in nuclei (Blankenship & Bresnick, 1974). PB induction in hepatocytes was impaired when the phosphorylation status of proteins was modified (Sidhu & Omiecinski 1995;1997).…”

Section: Discussionmentioning

confidence: 99%

Upregulation of cytochromes P450 2B in rat liver by orphenadrine

Murray

Fiala-Beer

Sutton

2003

British J Pharmacology

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1 The alkylamine drug orphenadrine (ORPH) is an inducer and inhibitor of the microsomal cytochrome P450 (CYP) system in mammals. This study evaluated the selectivity of CYP induction by ORPH in rat liver. 2 Immunoblot analysis indicated that ORPH was a selective inducer of the phenobarbitone (PB)-inducible CYP2B in rat liver. CYP2B protein was increased to B14-fold of levels in untreated rat liver. By comparison PB increased CYP2B expression 40-fold. Corresponding increases in the activity of CYP2B-dependent androstenedione 16b-hydroxylation were measured in microsomes from ORPH and PB-induced rats. 3 Northern analysis indicated that CYP2B1/2 mRNA was increased in ORPH-induced rat liver. Consistent with this finding, ORPH was found to activate a PB-responsive enhancer module in constitutive androstane receptor (CAR)-transfected Hep G2 cells. 4 Other alkylamines like troleandomycin impair CYP turnover. We tested whether ORPH induction of CYP2B may include a post-translational component. In PB-pretreated animals ORPH administration delayed the loss of CYP2B after PB withdrawal, but no evidence for altered turnover was found. 5 These studies establish ORPH as a selective inducer of CYP2B in rat liver. Induction appears to be mediated pretranslationally by CAR activation of CYP2B gene transcription. Post-translational stabilisation by an ORPH metabolite does not elicit induction. Induction of CYP2B may influence pharmacokinetic interactions involving ORPH.

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Section: Discussionmentioning

confidence: 99%

Upregulation of cytochromes P450 2B in rat liver by orphenadrine

Murray

Fiala-Beer

Sutton

2003

British J Pharmacology

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“…Measurement of peak sizes was then used to determine relative stain content of each band. Alternatively, each band was excised from the gel, and the dye was removed with 2.0 ml of dimethylsulfoxide at 37°C overnight (27). Optical density readings of the extracts were made at 615 nm in a Beckman model 25 spectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

Histone modifications in simian virus 40 and in nucleoprotein complexes containing supercoiled viral DNA

Chen¹,

MacGregor²,

Goldstein³

et al. 1979

J Virol

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Simian virus (SV40) nucleoprotein complexes containing circular supercoiled viral DNA were extracted from infected cells and purified by differential centrifugation. The protein content of these complexes was compared by electrophoresis on 15% acrylamide gels with the protein content of purified SV40 virions and with histones from virus-infected cells. The electrophoretic patterns of histones from each of the sources revealed several major differences. SV40 virions contained histones H3, H2B, H2A, and H4 but not Hi. Nucleoprotein complexes and host cells contained all five major histone groups. Relative to cellular histones, virion and nucleoprotein complex histones were enriched 15 to 40% in histones H3 and H4. In addition to the major classes of histones, several subfractions of histones Hi, H3, and H4 were observed in acrylamide gels of proteins from SV40 virions and viral nucleoprotein complexes. Acetate labeling experiments indicated that each subfraction of histones H3 and H4 had a different level of acetylation. The histones from SV40 virions and nucleoprotein complexes were acetylated to significantly higher levels than those ofinfected host cells. No apparent differences in phosphorylation of the major histone groups were observed.

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“…Several lines of evidence suggest that phenobarbital treatment induces RNA synthesis. Procaccini & Bresnick (1975) observed an increase in the acetylation of histones in the liver after phenobarbital treatment, a phenomenon that has been temporally correlated with an increase in transcriptional activity (Ruiz-Carrillo et al, 1975). The administration of actinomycin D or a-amanitin before phenobarbital treatment decreases the induction of cytochrome P-450 (Nebert & Gielen, 1971;Jacob et al, 1974).…”

mentioning

confidence: 99%

The effect of phenobarbital on the transcriptional activity of liver

Hardwick

Schwalm

Richardson

1983

Biochemical Journal

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The effect of phenobarbital on the transcriptional activity of liver was studied by measuring the synthesis of RNA by suspensions of hepatocytes isolated from rats treated with phenobarbital for various time periods. The absolute rates of RNA synthesis by isolated hepatocytes were determined by measuring the incorporation of [3H]orotic acid into RNA as UMP and the specific radioactivity of the UTP pool. The specific radioactivity of the UTP extracted from hepatocytes isolated from phenobarbital-treated rats was consistently lower than that of the UTP pool of hepatocytes from untreated rats. Phenobarbital treatment increased the rate of RNA synthesis 10-fold over that observed for hepatocytes from untreated rats. The maximum rate of RNA synthesis was observed 16-18 h after phenobarbital administration. Phenobarbital treatment also affected the nuclear-cytoplasmic transport of RNA by isolated hepatocytes. Immediately after phenobarbital treatment, the transport of RNA decreased; however, 24 h after phenobarbital administration, the transport of RNA was increased 4-fold. An increase in the synthesis of RNA in vivo by liver was found 18 h after phenobarbital treatment, and the incubation of suspensions of hepatocytes with various concentrations of phenobarbital increased RNA synthesis significantly.

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Histone modification in liver after administration of inducers of mixed function oxidase activity

Cited by 11 publications

References 22 publications

Upregulation of cytochromes P450 2B in rat liver by orphenadrine

Upregulation of cytochromes P450 2B in rat liver by orphenadrine

Histone modifications in simian virus 40 and in nucleoprotein complexes containing supercoiled viral DNA

The effect of phenobarbital on the transcriptional activity of liver

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