Title : Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P-450 2C8 and P-450 3A4 in human liver microsomes.

Pub. Date : 1999 Nov

PMID : 10534310






4 Functional Relationships(s)
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1 Of fourteen cDNA-expressed human P-450 enzymes examined, CYP1A1, CYP2C8, CYP2C19, and CYP3A4 were active in catalyzing formation of a quinone-type metabolite at a concentration of 10 microM troglitazone, whereas CYP3A4 had the highest catalytic activity at 100 microM substrate. quinone cytochrome P450 family 3 subfamily A member 4 Homo sapiens
2 Of fourteen cDNA-expressed human P-450 enzymes examined, CYP1A1, CYP2C8, CYP2C19, and CYP3A4 were active in catalyzing formation of a quinone-type metabolite at a concentration of 10 microM troglitazone, whereas CYP3A4 had the highest catalytic activity at 100 microM substrate. quinone cytochrome P450 family 3 subfamily A member 4 Homo sapiens
3 The results suggest that in human liver both CYP2C8 and CYP3A4 have major roles in quinone-type metabolite formation and that the hepatic contents of these two P-450 forms determine which P-450 enzymes play major roles in individual humans. quinone cytochrome P450 family 3 subfamily A member 4 Homo sapiens
4 CYP3A4 may be expected to play a role in formation of quinone-type metabolite from troglitazone even at a low concentration in humans. quinone cytochrome P450 family 3 subfamily A member 4 Homo sapiens