Activation and deactivation of aflatoxin B1 in isolated rat hepatocytes

Biochemical and Biophysical Research Communications
J J Ch'ihT M Devlin

Abstract

Isolated rat hepatocytes took up [3H]-aflatoxin B1 during incubation with fifty percent of the aflatoxin B1 covalantly bound to cellular macromolecules. The amount of bound-aflatoxin B1 was proportional to the medium concentration of aflatoxin B1. The specific radioactivity (pmole/mg) of aflatoxin B1 found in the DNA fraction was 20 fold greater than that associated with protein. Metyrapone (0.75 mM) inhibited significantly the uptake and binding whereas 1,2-epoxy-3,3,3-trichloropropane (0.5 mM) enhanced 2-3 fold both the uptake and binding. Glutathione (0.25 mM) reduced these processes. Results indicate that a transformation of aflatoxin B1 is catalyzed by cytochrome P-450 mixed function oxidase and aflatoxin B1-2,3-epoxide so formed is primarily deactivated by epoxide hydrolase. In the isolated hepatocyte depletion of the epoxide by glutathione apparently has an insignificant role in aflatoxin detoxication.

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Citations

May 1, 1984·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·M Y Fukayama, D P Hsieh
Dec 1, 1986·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·D H MonroeD L Eaton
Jul 24, 1998·Mutation Research·F P GuengerichS Langouët
Dec 1, 1988·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·D J McCormickD McKillop
Aug 15, 1991·Biochemical and Biophysical Research Communications·J J Ch'ihT M Devlin
Jul 18, 1984·Biochemical and Biophysical Research Communications·J J Ch'ih, T M Devlin

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