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Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues.
Abstract
The organ distribution of microsomal cytochrome P 450 isoenzymes (P 450), microsomal epoxide hydrolase (EH) and cytosolic glutathione-S-transferases was investigated by immunoblotting and enzyme measurements in rats and humans. In rats, P 450 IA1 was detected only in the duodenum, and P 450 IA2 and IIC11 were detected only in the liver. The highest concentrations of P 450 IIB1/B2 were found in the lung and in the duodenum; pentoxyresorufin-O-dealkylase activity was closely correlated with the amounts of P 450 IIB1/B2 in the different organs. P 450 IIE1 was present in liver, kidney and lung, whereas EH was found in liver, intestine and kidney. In humans, P 450 IIIA4 was detected in all tissues investigated; the highest concentrations were found in liver and intestine. The P 450 IIIA4 level was closely correlated with that of erythromycin demethylase and pentoxyresorufin-O-dealkylase activities. P 450 IIC8-10, IIE1 and IID6 were expressed in liver and intestine, P 450 9 in liver and kidney and P 450 IA2 in liver. EH was identified only in liver, intestine and kidney. In both species, concentrations and total amounts of P 450 isoenzymes and EH were much lower in all extrahepatic tissues than in the liver. Conversely, glutathione-S-transferase-pi was abundant in human intestine and colon compared to liver. Glutathione-S-transferase-mu polymorphism was confirmed in all tissues investigated. This extensive study showed that the pattern of (iso) enzymes was different in all tissues studied; consequently, xenobiotic metabolism would appear to be very different in each type of tissue.
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Cited by
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Genetic contribution to variable human CYP3A-mediated metabolism
Lamba, J. K., Lin, Y. S., Schuetz, E. G., & Thummel, K. E. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00066-2 · Cited by 990
THE HUMAN INTESTINAL CYTOCHROME P450 “PIE”
Paine, M. F., Hart, H. L., Ludington, S. S., Haining, R. L., Rettie, A. E., & Zeldin, D. C. (2006) · Drug Metabolism and Disposition · doi:10.1124/dmd.105.008672 · Cited by 870
17 beta-estradiol hydroxylation catalyzed by human cytochrome P450 1B1.
Hayes, C. L., Spink, D. C., Spink, B. C., Cao, J. Q., Walker, N. J., & Sutter, T. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9776 · Cited by 632
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Metadata
- Authors
- de Waziers, I., Cugnenc, P. H., Yang, C. S., Leroux, J. P., & Beaune, P. H.
- Venue
- The Journal of Pharmacology and Experimental Therapeutics
- Publisher
- Elsevier BV
- Published
- 1990-04
- Volume
- 253
- Issue
- 1
- Pages
- 387-394
- ISSN
- 0022-3565 (ISSN-L)
- OpenAlex
- W1892194801
- Cited by
- 502
- References
- 0
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues. https://app.cochat.ai/papers/10.1016/s0022-3565(25)12474-9
- The paper
- de Waziers, I., Cugnenc, P. H., Yang, C. S., Leroux, J. P., & Beaune, P. H. (1990). Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues. The Journal of Pharmacology and Experimental Therapeutics. https://doi.org/10.1016/s0022-3565(25)12474-9
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