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Interaction of acrylonitrile with the liver mixed function oxidases
Archives of Toxicology. Supplement. = Archiv Fur Toxikologie. Supplement
|January 1, 1984
Summary
Acrylonitrile inhibits liver enzymes like benzo(a)pyrene hydroxylase, but not aniline hydroxylase. This suggests cyanide, released during metabolism, mediates the inhibitory effect on liver microsomes.
Area of Science:
- Biochemistry
- Toxicology
- Drug Metabolism
Background:
- Liver mixed-function oxidases are crucial for metabolizing xenobiotics.
- Acrylonitrile is an industrial chemical with potential toxicological effects.
- Cytochrome P-450 enzymes are key players in the mixed-function oxidase system.
Purpose of the Study:
- To investigate the impact of acrylonitrile on specific liver microsomal enzymes.
- To elucidate the mechanism underlying acrylonitrile's effect on liver hydroxylation activities.
Main Methods:
- Assessing the activity of benzo(a)pyrene hydroxylase, epoxide hydrase, and aniline hydroxylase in liver microsomes.
- Incubating liver microsomes with acrylonitrile to observe enzyme activity changes.
Main Results:
- Acrylonitrile significantly inhibited benzo(a)pyrene hydroxylase and epoxide hydrase activity.
- Aniline hydroxylase activity remained unaffected by acrylonitrile exposure.
- These results indicate a selective inhibitory effect on specific liver enzymes.
Conclusions:
- The findings exclude a direct inhibitory effect of acrylonitrile on cytochrome P-450.
- The study proposes that cyanide, a metabolite of acrylonitrile, mediates the observed enzyme inhibition.
- This highlights the role of metabolic products in the toxicity of acrylonitrile.