Abstract
Since prostaglandin H synthase (PHS) peroxidase can catalyze metabolic activation of both stilbene and steroid estrogens in vitro, it is of relevance to study this enzymatic activity in a target tissue for their carcinogenic action. Microsomal preparations from male Syrian golden hamster kidney supplemented with arachidonic acid (ARA) convert radiolabeled diethylstilbestrol (DES) to the oxidative metabolite Z, Z-dienestrol (Z,Z-DIES) and to protein-bound product(s). PHS-mediated (ARA-dependent) oxidation of DES can be clearly demonstrated in incubations with microsomes from hamster medulla/papilla, but is negligible with those from cortex. This intraorgan distribution of PHS in hamster kidney resembles that observed for rabbit kidney. The data suggest that PHS-peroxidase can contribute to the metabolic activation of carcinogenic estrogens in hamster kidney but its precise role remains to elucidated.
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