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Carcinogenic pollutants o-nitroanisole and o-anisidine are substrates and inducers of cytochromes P450
H. Rýdlová, M. Miksanová, H. Ryslavá, M. Stiborová
Jazyk angličtina Země Česko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2001
Free Medical Journals
od 1998
ROAD: Directory of Open Access Scholarly Resources
od 2001
PubMed
16601807
DOI
10.5507/bp.2005.077
Knihovny.cz E-zdroje
- MeSH
- aniliny farmakokinetika farmakologie MeSH
- anisoly farmakokinetika farmakologie MeSH
- enzymová indukce MeSH
- karcinogeny farmakokinetika farmakologie MeSH
- králíci MeSH
- krysa rodu rattus MeSH
- látky znečišťující životní prostředí farmakokinetika farmakologie MeSH
- mikrozomy enzymologie MeSH
- potkani Wistar MeSH
- systém (enzymů) cytochromů P-450 biosyntéza MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- krysa rodu rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
2-Methoxyaniline (o-anisidine) and 2-methoxynitrobenzene (o-nitroanisole) are important pollutants and potent carcinogens for rodents. o-Anisidine is oxidized by microsomes of rats and rabbits to N-(2-methoxyphenyl)hydroxylamine that is also formed as the reduction metabolite of o-nitroanisole. o-Anisidine is a promiscuity substrate of rat and rabbit cytochrome P450 (CYP) enzymes, because CYPs of 1A, 2B, 2E and 3A subfamilies oxidize o-anisidine. Using purified CYP enzymes, reconstituted with NADPH: CYP reductase, rabbit CYP2E1 was the most efficient enzyme oxidizing o-anisidine, but the ability of CYP1A1, 1A2, 2B2, 2B4 and 3A6 to participate in o-anisidine oxidation was also proved. Utilizing Western blotting and consecutive immunoquantification employing chicken polyclonal anti bodies raised against various CYPs, the effect of o-anisidine and o-nitroanisole on the expression of the CYP enzymes was investigated. The expression of CYP1A1/2 was found to be strongly induced in rats treated with either compounds. In addition, 7-ethoxyresorufin O-deethylation, a marker activity for both CYP1A1 and 1A2, was significantly increased in rats treated with either carcinogen. The data demonstrate the participation of different rat and rabbit CYP enzymes in o-anisidine oxidation and indicate that both experimental animal species might serve as suitable models to mimic the o-anisidine oxidation in human. Furthermore, by induction of rat hepatic and renal CYP1A1/2, both o-nitroanisole and o-anisidine influence their carcinogenic effects, modifying their detoxification and/or activation pathways.
Citace poskytuje Crossref.org
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