The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Oxidation of Aflatoxin B1 by Bacterial Recombinant Human Cytochrome P450 Enzymes
Abstract
Human cytochromes P450 (P450) 1A2 and P450 3A4 were expressed in Escherichia coli, purified, and used in reconstituted oxidation systems. The optimal system for P450 3A4 included a mixture of phospholipids, sodium cholate, cytochrome b5, GSH, and MgCl2. Relatively high catalytic activities were obtained with such a system for aflatoxin (AF) B1 3 alpha-hydroxylation and 8,9-epoxidation. P450 3A4 was more active than P450 1A2 in forming genotoxic AFB1 oxidation products. Analysis of the AFB1 products indicated that P450 3A4 formed AFQ1 and the exo-8,9-epoxide; P450 1A2 formed AFM1, a small amount of AFQ1, and both the exo- and endo-8,9-epoxides. The endo epoxide is essentially nongenotoxic in the umu test, as found previously in bacterial mutagenicity assays [Iyer, R. S., Coles, B. F., Raney, K. D., Thier, R., Guengerich, F. P., and Harris, T. M. (1994) J. Am. Chem. Soc. 116, 1603-1609]. 7,8-Benzoflavone (alpha-naphthoflavone, alpha NF) stimulated AFB1 (exo) 8,9-epoxidation and inhibited 3 alpha-hydroxylation in human liver microsomes and a reconstituted P450 3A4 system but was a potent inhibitor of all reactions catalyzed by P450 1A2. Plots of AFB1 3 alpha-hydroxylation and 8,9-epoxidation vs AFB1 concentration were sigmoidal in both human liver microsomes and the reconstituted P450 3A4 system. The results are consistent with the view that P450 3A4 is a major human liver P450 enzyme involved in AFB1 activation, although the in vivo situation may be more complex due to the presence of the enzyme in the gastrointestinal tract.
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Cites
Expression of Bovine 17α-Hydroxylase Cytochrome P-450 cDNA in Nonsteroidogenic (COS 1) Cells
Zuber, M. X., Simpson, E. R., & Waterman, M. R. (1986) · Science · doi:10.1126/science.3535074 · Cited by 388
Cited by
Rushing, B. R., & Selim, M. I. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.11.047 · Cited by 989
IN VITRO AND IN VIVO DRUG INTERACTIONS INVOLVING HUMAN CYP3A
Thummel, K. E., & Wilkinson, G. R. (1998) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.38.1.389 · Cited by 831
Aflatoxin: a 50-year odyssey of mechanistic and translational toxicology
Kensler, T. W., Roebuck, B. D., Wogan, G. N., & Groopman, J. D. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfq283 · Cited by 703
Activation and detoxication of aflatoxin B1
Guengerich, F. P., Johnson, W. W., Shimada, T., Ueng, Y.-F., Yamazaki, H., & Langouët, S. (1998) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(97)00289-3 · Cited by 344
Self-citationContributions of Human Enzymes in Carcinogen Metabolism
Rendic, S., & Guengerich, F. P. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300132k · Cited by 279
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Metadata
- Authors
- Ueng, Y.-F., Shimada, T., Yamazaki, H., & Guengerich, F. P.
- Venue
- Chemical Research in Toxicology
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-03
- Volume
- 8
- Issue
- 2
- Pages
- 218-225
- ISSN
- 0893-228X (ISSN-L)
- 1520-5010
- OpenAlex
- W2036504837
- Cited by
- 216
- References
- 1
- FWCI
- 12.76
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ueng, Y.-F., Shimada, T., Yamazaki, H., & Guengerich, F. P. (1995). Oxidation of Aflatoxin B1 by Bacterial Recombinant Human Cytochrome P450 Enzymes. Chemical Research in Toxicology. https://doi.org/10.1021/tx00044a006
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