Activation and deactivation of aflatoxin B1 in isolated rat hepatocytes.

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.

authors

Ch'ih JJ,Lin T,Devlin TM

doi

10.1016/0006-291x(83)91201-9

subject

Has Abstract

pub_date

1983-01-27 00:00:00

pages

668-74

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)91201-9

journal_volume

110

pub_type

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