Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers
Language English Country Ireland Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15766589
DOI
10.1016/j.canlet.2004.07.036
PII: S0304-3835(04)00617-2
Knihovny.cz E-resources
- MeSH
- Cytochrome P-450 CYP1A1 biosynthesis pharmacology MeSH
- Immunoblotting MeSH
- Microsomes, Liver MeSH
- Liver drug effects enzymology MeSH
- Carcinogens metabolism MeSH
- Humans MeSH
- Liver Neoplasms chemically induced physiopathology MeSH
- Naphthols metabolism MeSH
- Oxidation-Reduction MeSH
- Gene Expression Profiling MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 1-phenylazo-2-naphthol MeSH Browser
- Cytochrome P-450 CYP1A1 MeSH
- Carcinogens MeSH
- Naphthols MeSH
Cytochrome P450 1A1 (CYP1A1) is one of the most important enzymes implicated in the metabolic activation of carcinogens. To date, there is still conflicting evidence for the expression of enzymatically functional CYP1A1 in human liver. In the present work, we clearly demonstrate that CYP1A1 capable of metabolizing a carcinogen 1-phenylazo-2-naphthol (Sudan I) is expressed in livers of eight American Caucasian donors. Using two independent methods (immunoblotting and N-terminal sequencing), CYP1A1 protein was detected and quantified in all human hepatic microsomes tested in the study. Its levels, ranging from 0.97 to 3.0 pmol/mg protein, correlated with activities catalyzed by this enzyme [7-ethoxyresorufin O-deethylation (EROD) and oxidation of Sudan I], indicating the presence of enzymatically active CYP1A1. Even though levels of CYP1A1 expression are low, <0.7% of total hepatic CYP, the CYP1A1 contribution to oxidation of carcinogenic Sudan I in the test set of human liver microsomes ranges from 12 to 30%.
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