Competitive inhibitory effect of microsomal N-hydroxylase, a possible explanation for the in vivo in inhibition of 2-acetylaminofluorene carcinogenicity by 3-methylcholanthrene.

Razzouk, C.;Agazzi-Léonard, E;Batardy-Grégoire, M;Mercier, Michel;Roberfroid, Marcel;et.al.
(1980) Toxicology Letters — Vol. 5, n° 1, p. 61-67 (1980)

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  • Razzouk, C.
    Author
  • Agazzi-Léonard, E
    Author
  • Batardy-Grégoire, M
    Author
  • Mercier, MichelUCLouvain
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  • Roberfroid, MarcelUCLouvain
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Abstract
The kinetic properties of the N-hydroxylation of 2-acetylaminofluorene (2-AAF) are studied with microsomal preparations of livers from both control and 3-methylcholanthrene (3-MC)-pretreated rats and hamsters. The level of basal enzymatic activity is higher in hamster than in rat liver; 3-MC induces the activity in both animals. When added in vitro to incubation mixture, 3-MC competitively inhibits the N-hydroxylase activity. When fed to rats simultaneously with 2-AAF, 3-MC suppresses the carcinogenicity of the acetylated arylamine by inhibiting the first step in its activation pathway. Hamster tissues are not protected by this pretreatment because the level of N-hydroxylase activity is too high.
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Razzouk, C., Agazzi-Léonard, E., Batardy-Grégoire, M., Mercier, M., Poncelet, F., & Roberfroid, M. (1980). Competitive inhibitory effect of microsomal N-hydroxylase, a possible explanation for the in vivo in inhibition of 2-acetylaminofluorene carcinogenicity by 3-methylcholanthrene. Toxicology Letters, 5(1), 61-67. https://hdl.handle.net/2078.5/83596 (Original work published 1980)