scholarly journals Effects of Kampo Extracts on Drug Metabolism in Rat Liver Microsomes: Rhei Rhizoma Extract and Glycyrrhizae Radix Extract Inhibit Drug Oxidation

2002 ◽  
Vol 89 (2) ◽  
pp. 164-170 ◽  
Author(s):  
Atsushi Hasegawa ◽  
Yoko Kawaguchi ◽  
Hiromitsu Nakasa ◽  
Hiroyoshi Nakamura ◽  
Shigeru Ohmori ◽  
...  
Keyword(s):  
Drug Metabolism ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Glycyrrhizae Radix ◽  
Rhei Rhizoma ◽  
Drug Oxidation ◽  
Kampo Extracts

The effects of primaquine stereoisomers and metabolites on drug metabolism in the isolated perfused rat liver and in vitro rat liver microsomes

1985 ◽  
Vol 34 (3) ◽  
pp. 331-336 ◽  
Author(s):  
George W. Mihaly ◽  
Stephen A. Ward ◽  
Deborah D. Nicholl ◽  
Geoffrey Edwards ◽  
Alasdair M. Breckenridge
Keyword(s):  
Drug Metabolism ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Isolated Perfused Rat Liver ◽  
Rat Liver Microsomes ◽  
Perfused Rat Liver

Interaction of famotidine with rat liver microsomes, a study showing less inhibition of drug metabolism than with cimetidine

1986 ◽  
Vol 18 (7) ◽  
pp. 629-638 ◽  
Author(s):  
Yasuharu Imai ◽  
Masami Inada ◽  
Shinji Tamura ◽  
Shuzo Noda ◽  
Sumio Kawata ◽  
...  
Keyword(s):  
Drug Metabolism ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes

Cytochromes P450 Involved in Cyclophosphamide, Paclitaxel and Docetaxel Metabolism in Rats

2000 ◽  
Vol 65 (7) ◽  
pp. 1183-1190 ◽  
Author(s):  
Lucie Bořek-Dohalská ◽  
Ivan Gut ◽  
Pavel Souček ◽  
Zdeněk Roth ◽  
Petr Hodek
Keyword(s):  
Drug Metabolism ◽  
Anticancer Drugs ◽  
Rat Liver ◽  
Indirect Method ◽  
Cytochromes P450 ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Fast Estimation ◽  
Cyp Enzymes ◽  
Model Drug

We investigated involvement of cytochromes P450 (CYPs) of rat liver microsomes in metabolism of two anticancer drugs, paclitaxel (PCT) and docetaxel (DTX), by an indirect method. This method is based on the presumption that the compound competitively inhibiting oxidation of the CYP-selective substrate should also be a substrate for the CYP enzyme. The validity of this approach was confirmed using the model drug, cyclophosphamide (CPA). Indeed, CPA competitively inhibited oxidation of substrates specific for CYP2B1 and CYP3A1/2, enzymes previously reported to be capable of metabolizing CPA. Using this method, we identified CYP enzymes participating in PCT and DTX metabolism. The CYP2D1/2/3 and CYP3A1/2 are enzymes oxidizing PCT while CYP3A1/2 and CYP2E1 are responsible for metabolism of DTX. Here, we report a suitable method serving for easy and fast estimation of CYP enzymes involved in drug metabolism.

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