Document Detail


Inhibition of debrisoquin clearance in perfused rat livers and inhibition of dextromethorphan metabolism in human liver microsomes by 4-hydroxydebrisoquin or other metabolites of debrisoquin.
MedLine Citation:
PMID:  1355711     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Debrisoquin undergoes oxidative metabolism to 4-hydroxydebrisoquin, catalyzed by cytochrome CYP2D1 in rats and CYP2D6 in humans. Cytochrome CYP2D6 also plays a major role in dextromethorphan O-demethylation. In preliminary studies in perfused Lewis rat livers, we observed a difference in repeat clearance experiments using debrisoquin, but not dextromethorphan. To determine whether this change in clearance with time was due to the accumulation of 4-hydroxydebrisoquin, we sequentially used a recirculating and nonrecirculating perfusion system in the same liver perfusion experiment. We also studied the kinetics of dextromethorphan O-demethylation in microsomes prepared from human and rat livers in the presence and absence of 4-hydroxydebrisoquin. Results from the perfused rat liver experiments showed a drop in clearance from 3.27 +/- 0.57 ml/min (clearance 1) to 1.61 +/- 0.27 ml/min (clearance 2) (p less than 0.05 vs. clearance 1) during recirculation, but clearance returned to 3.21 +/- 0.46 ml/min (clearance 3, no significance vs. clearance 1) after a 30-min period of liver perfusion using a nonrecirculating system. There was significant accumulation of 4-hydroxydebrisoquin in the liver perfusate during recirculation, and concentrations fell when the nonrecirculating system was used. In microsomal studies, 4-hydroxydebrisoquin competitively inhibited dextromethorphan metabolism in human microsomes was 600 microM. These data suggest that: (a) 4-hydroxydebrisoquin and/or other metabolites of debrisoquin have an inhibitory effect on CYP2D1 and CYP2D6; (b) the active site of human CYP2D6 has different substrate specificity than the rat isozyme (CYP2D1) and/or that the pathways of metabolism of dextromethorphan are different in the Lewis rat and not primarily dependent on the activity of CYP2D1.
Authors:
S Jaruratanasirikul; A D Cooper; T F Blaschke
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Drug metabolism and disposition: the biological fate of chemicals     Volume:  20     ISSN:  0090-9556     ISO Abbreviation:  Drug Metab. Dispos.     Publication Date:    1992 May-Jun
Date Detail:
Created Date:  1992-10-15     Completed Date:  1992-10-15     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9421550     Medline TA:  Drug Metab Dispos     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  379-82     Citation Subset:  IM    
Affiliation:
Department of Medicine, Stanford University Medical Center, CA 94305-5113.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cytochrome P-450 CYP2D6
Cytochrome P-450 Enzyme System / metabolism
Debrisoquin / analogs & derivatives*,  metabolism*,  pharmacology
Dextromethorphan / metabolism*
Female
Humans
Liver / metabolism*
Methylation
Microsomes, Liver / metabolism*
Mixed Function Oxygenases / metabolism
Rats
Rats, Inbred Lew
Substrate Specificity
Grant Support
ID/Acronym/Agency:
AI27762/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
1131-64-2/Debrisoquin; 125-71-3/Dextromethorphan; 59333-79-8/4-hydroxydebrisoquin; 9035-51-2/Cytochrome P-450 Enzyme System; EC 1.-/Mixed Function Oxygenases; EC 1.14.14.1/Cytochrome P-450 CYP2D6

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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