Characterization of benzo[a]pyrene metabolism and related cytochrome P-450 isozymes in Syrian hamster livers.

Cytochrome P-450 monooxygenases of golden Syrian hamsters were characterized with respect to benzo[a]pyrene metabolism. Male hamsters were treated with phenobarbital, 3-methylcholanthrene, dexamethasone, benzoflavone, or ethanol, and the activity of aryl hydrocarbon hydroxylase and benzo[a]pyrene activation was determined by mutagenicity testing in hepatic microsomes. Aryl hydrocarbon hydroxylase activity was induced markedly by treatment with phenobarbital but not with 3-methylcholanthrene, nor with other chemicals. The degree of benzo[a]pyrene activation on mutagenicity testing was significantly elevated by treatment with 3-methylcholanthrene and phenobarbital but was reduced with dexamethasone. Immunoinhibition of these activities and Western blotting of hepatic microsomes using antibodies against cytochrome P-450 isozymes suggested that the isozymes responsible for benzo[a]pyrene metabolism in Syrian hamsters belong to the CYP1A, CYP2A, and CYP3A families, a result that differs from observations in rats.