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- W1484689544 abstract "Previous studies from our laboratories have shown that the metabolism of the cholesterol-lowering drug lovastatin by rat and human liver microsomes occurs primarily at the 6'-position, giving 6' beta-hydroxy- and 6'-exomethylene-lovastatin and that these oxidations are catalyzed by cytochrome P450-dependent monooxygenases. In the present study, the specific cytochrome P450 form involved in lovastatin oxidation was identified through immunoinhibition studies. Among several antibodies prepared against various cytochrome P450s, only anti-rat P450 3A IgG inhibited lovastatin metabolism in liver microsomes from untreated, phenobarbital-treated, and pregnenolone-16 alpha-carbonitrile-treated rats. Lovastatin metabolism at the 6'-position was markedly inhibited (6' beta-hydroxy, greater than 95%; 6'-exomethylene, 70-80%) by this antibody whereas the effect of anti-rat P450 3A on the 3-hydroxylation was variable depending on the source of the microsomes. With human liver microsomes, both anti-rat P450 3A and anti-human P450 3A inhibited lovastatin metabolism. Correlation between lovastatin oxidation and the P450 3A content in human liver microsomes (measured by immunoblot analysis) was excellent (r2 = 0.97). In addition, preincubation of human liver microsomes with troleandomycin and NADPH inhibited metabolism by 60%. These results clearly indicate that cytochrome P450 3A enzymes are primarily responsible for the metabolism of lovastatin in rat and human liver microsomes." @default.
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- W1484689544 date "1991-11-01" @default.
- W1484689544 modified "2023-09-26" @default.
- W1484689544 title "Biotransformation of lovastatin" @default.
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- W1484689544 doi "https://doi.org/10.1016/0003-9861(91)90551-s" @default.
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