Abstract
The ability of prostaglandin synthetase (PGS) to cooxidize benzo(a)pyrene, benzo(a)anthracene, chrysene, and several of their dihydrodiol derivatives to mutagenic products was tested with Salmonella typhimurium strains TA98 and TA100. The microsomal fraction of ram seminal vesicles, a known source of PGS, in the presence of the PGS substrate arachidonic acid, metabolized benzo(a)pyrene-7,8-dihydrodiol, benzo(a)anthracene-3,4-dihydrodiol, and chrysene-1,2-dihydrodiol to mutagenic products. This activity was inhibited by the PGS inhibitor indomethacin. Unlike the PGS system, however, a cytochrome P-450-reduced nicotinamide adenine dinucleotide phosphatedependent system, present in an Aroclor 1254-induced rat liver 9000 × g supernatant fraction, also activated the parent compounds [benzo(a)pyrene, benzo(a)anthracene, chrysene] and several other benzo(a)anthracene dihydrodiols (the 1,2-dihydrodiol, the 8,9-dihydrodiol, and the 10,11-dihydrodiol). The chrysene trans-3,4, trans-5,6, and cis-5,6 diols were not activated to mutagens by either system. Thus, the PGS system appears to be more selective than does the cytochrome P-450 system in the activation of polycyclic aromatic hydrocarbons to mutagenic products, activating only those dihydrodiols with adjacent double bonds in the bay region from which the bayregion diol-epoxides are formed.
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