Multiple pathways for the oxidative metabolism of estrogens in Syrian hamster and rabbit kidney

Journal of Biochemical Toxicology
G H DegenM Metzler

Abstract

Microsomal preparations from hamster kidney, a target tissue for the carcinogenic action of stilbene-type and steroidal estrogens, catalyze the oxidative metabolism of diethylstilbestrol (DES). The formation of the major metabolite Z,Z-dienestrol and of reactive intermediates capable of protein binding were mediated by enzyme activities requiring nicotinamide-adenine dinucleotide phosphate (reduced form-NADPH), cumene hydroperoxide, or arachidonic acid (ARA). In addition, hydroxylated DES metabolites were detected in NADPH-supplemented incubations. The NADPH-dependent oxidation of DES was inhibited by SKF 525A and metyrapone. Monooxygenase-catalyzed metabolism was apparently responsible for the majority of DES oxidation in microsomes from whole hamster kidneys in vitro and this activity is preferentially localized in the kidney cortex. However, ARA-dependent, i.e., prostaglandin H synthase (PHS) mediated oxidation of DES and of the catechol estrogen 2-hydroxyestrone was demonstrated as well in the medulla of both rabbit and hamster kidney. It is proposed that monooxygenase and PHS activities act in concert in the metabolic activation of carcinogenic estrogens. This appears to apply in particular to steroidal estrogens, since ca...Continue Reading

References

Dec 14, 1978·Biochemical and Biophysical Research Communications·M Metzler, J A McLachlan
Jun 21, 1976·Biochemical and Biophysical Research Communications·S D NelsonH A Sasame
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Jun 1, 1969·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·J J LiR L Hunter
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