DNA binding of N-hydroxy-Trp-P-2 and N-hydroxy-Glu-P-1 by acetyl-CoA dependent enzyme in mammalian liver cytosol

3-Hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole and 2-hydroxyamino-6-methyldipyrido[1,2-a:3',2'-d]imidazole, active metabolites of protein pyrolysate carcinogens, were further activated to DNA-binding species by an acetyl-CoA dependent enzyme in hepatic cytosol. This activity was supported...

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Bibliographic Details
Published inCarcinogenesis (New York) Vol. 6; no. 2; p. 305
Main Authors Shinohara, A, Saito, K, Yamazoe, Y, Kamataki, T, Kato, R
Format Journal Article
LanguageEnglish
Published England 01.02.1985
Subjects
Acetyl Coenzyme A - pharmacology
Acetylation
Animals
Carbolines - metabolism
Cytosol - enzymology
DNA - metabolism
Imidazoles - metabolism
In Vitro Techniques
Indoles - metabolism
Liver - enzymology
Mice
Mutagens - metabolism
Rabbits
Rats
Species Specificity
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Summary:3-Hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole and 2-hydroxyamino-6-methyldipyrido[1,2-a:3',2'-d]imidazole, active metabolites of protein pyrolysate carcinogens, were further activated to DNA-binding species by an acetyl-CoA dependent enzyme in hepatic cytosol. This activity was supported also by N-hydroxy-2-acetylaminofluorene instead of acetyl-CoA, and it was inhibited by iodoacetamide and 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2) but not by diethyl-p-nitrophenylphosphate. The activity was observed in the cytosols of rats, mice and rapid acetylator rabbits, which possessed N-acetylation activity of 2-aminofluorene and Trp-P-2. On the other hand, the activity could not be detected in the cytosols of a dog and a slow acetylator rabbit.
ISSN:0143-3334
DOI:10.1093/carcin/6.2.305