Prostaglandin H synthase-dependent epoxidation of aflatoxin B1.
This report demonstrates that aflatoxin B1 (AFB1) is cooxidized by prostaglandin H (PGH) synthase to form 2,3-dihydro-2,3-epoxy-aflatoxin B1 oxide. Using ram seminal vesicle microsomes as a source of PGH synthase, our results demonstrate that AFB1 is converted to a mutagen during arachidonate turnover that we identify as the epoxide by isolating adducts formed to DNA. The efficiency of AFB1 epoxidation by PGH synthase is assessed and compared with mixed-function oxidase-dependent metabolic activation of this compound.
D016604:Aflatoxin B1; D000348:Aflatoxins / Q000378:metabolism*; D000818:Animals; D001711:Biotransformation; D002273:Carcinogens / Q000378:metabolism*; D004852:Epoxy Compounds / Q000378:metabolism*; D004988:Ethers, Cyclic / Q000378:metabolism*; D008297:Male; D009153:Mutagens / Q000378:metabolism; D011451:Prostaglandin-Endoperoxide Synthases / Q000502:physiology*; D012756:Sheep
D000348:Aflatoxins; D002273:Carcinogens; D004852:Epoxy Compounds; D004988:Ethers, Cyclic; D009153:Mutagens; D016604:Aflatoxin B1; D011451:Prostaglandin-Endoperoxide Synthases