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- W48381922 abstract "Benzidine is a aromatic amine bladder carcinogen in man and dog which requires endogenous metabolic activation. Dog bladder microsomes activate benzidine to bind glutathione and DNA by a peroxidatic but not a mixed-function oxidase mediated pathway. Prostaglandin H synthase was responsible for peroxidatic metabolism. This study was designed to assess benzidine metabolism in a whole cell system. Rabbit renal medullary slices (100 mg/ml) were incubated for 60 min. in Krebs-Ringer bicarbonate buffer containing 100 ..mu..M /sup 3/H-benzidine and 250 ..mu..M arachidonic acid. Arachidonic acid increased 3-(glutathione-S-yL)-benzidine, a product of peroxidatically activated benzidine, (6-fold) and /sup 3/H-benzidine binding to endogenous DNA (4-fold). Indomethacin (100 ..mu..M) completely inhibited arachidonic acid-mediated increases in conjugate formation and DNA binding. HPLC analysis of the media demonstrated benzidine (95% of total /sup 3/H), 3-(glutathion-S-yL)-benzidine (1%) and two unidentified peaks (4%). These results are consistent with the hydroperoxidase activity of prostaglandin H synthase mediating metabolic activation of benzidine to bind tissue nucleophiles in a whole cell system. Inhibition of peroxidatic activation of aromatic amines to bind DNA may prevent initiation of bladder cancer." @default.
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- W48381922 date "1986-03-01" @default.
- W48381922 modified "2023-09-24" @default.
- W48381922 title "Peroxidase-mediated binding of aromatic amine carcinogens to tissue DNA" @default.
- W48381922 hasPublicationYear "1986" @default.
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