Abstract
Female rats were treated with phenobarbital, dexamethasone, 3-methylcholanthrene, clofibrate, or isoniazid to induce different hepatic cytochromes P-450. The profile of hydroxylated metabolites of estradiol (E2) formed by liver microsomes was then determined using a new HPLC method for the separation of hydroxylated estrogen metabolites. Inhibition of liver microsomal E2 metabolism by monoclonal antibodies raised against specific cytochrome P-450 isozymes was also evaluated. Treatment of immature or adult female rats with phenobarbital caused a 3-fold increase in the 2-hydroxylation of E2 and a more than 5-fold increase in liver microsomal hydroxylation of E2 at the 4-, 6 alpha, 6 beta-, and 14 alpha-positions. Monoclonal antibody directed toward CYP2B1/2B2 completely inhibited the 6 alpha- and 6 beta-hydroxylation of E2 and partially inhibited the 2-hydroxylation of E2 by liver microsomes from phenobarbital-treated adult female rats. Antibodies directed toward CYP3A1/3A2 completely inhibited the 4- and 14 alpha-hydroxylation of E2 by these liver microsomes. Treatment of immature or adult female rats with dexamethasone resulted in a 2- to 3-fold increase in the microsomal 2-hydroxylation of E2 and a several-fold increase in the...Continue Reading
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