In VivoPhenobarbital Treatment Increases Protein Binding to a Putative AP-1 Site in the CYP2B2 Promoter
| Autor: | Robert A. Blouin, Amy L. Roe, Georgette Howard |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Male
HMG-box Biophysics Plasma protein binding Biology Biochemistry Rats Sprague-Dawley chemistry.chemical_compound Cytochrome P-450 Enzyme System Animals Nuclear protein Binding site Promoter Regions Genetic Molecular Biology Binding Sites Oligonucleotide Binding protein Nuclear Proteins Cell Biology Molecular biology Rats Transcription Factor AP-1 DNA binding site Oligodeoxyribonucleotides chemistry Phenobarbital Steroid Hydroxylases Aryl Hydrocarbon Hydroxylases DNA Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 228:110-114 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1996.1624 |
| Popis: | Phenobarbital (PB) is a potent inducer of cytochrome P450 enzymes, particularly CYP2B1/2B2. Although the mechanism(s) of PB induction of CYP2B1/2B2 is not fully understood, current research is focusing on the role PB may play in altering the binding of nuclear proteins to critical DNA response elements in the 5'-flanking region of these genes. In this study, rat liver nuclear proteins were analyzed for DNA binding ability using both a general consensus and a CYP2B2 sequence-specific AP-1 oligonucleotide. We demonstrate that in vivo PB treatment enhances protein binding activity to the consensus AP-1 oligonucleotide. Likewise, a putative AP-1 site, identified at -1441 in the CYP2B2 5'-flanking region, also formed a sequence specific DNA/protein complex which was enhanced after PB exposure. These data may support a role of AP-1 in the PB induction mechanism of CYP2B1/2B2. |
| Databáze: | OpenAIRE |
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