Species differences in the N-acetylation by liver cytosol of mutagenic heterocyclic aromatic amines in protein pyrolysates

• Published in: Carcinogenesis (New York) 1984-05, Vol.5 (5), p.683-686
• Main Authors: Shinohara, Atsuko, Yamazoe, Yasushi, Saito, Kazuki, Kamataki, Tetsuya, Kato, Ryuichi
• Format: Article
• Language: English
• Subjects: Acetylation; Animals; Biological and medical sciences; Carbolines - metabolism; Chemical mutagenesis; Cricetinae; Cytosol - metabolism; Female; Heterocyclic Compounds - metabolism; Hot Temperature; Indoles - metabolism; Kinetics; Liver - metabolism; Male; Medical sciences; Mesocricetus; Mice; Mice, Inbred Strains; Mutagens - metabolism; Proteins; Rabbits; Rats; Rats, Inbred Strains; Species Specificity; Toxicology
• ISSN: 0143-3334; 1460-2180
• DOI: 10.1093/carcin/5.5.683

The N-acetylation of 3-amino-1-methyl-5H-pyrido(4,3-b)-indole (Trp-P-2) and other heterocyctic aromatic amine pro-mutagens isolated originally from protein pyrolysates was investigated using liver cytosols from various animal species and acetyl-CoA as an acetyl donor. Marked species differences in the enzymatic N-acetylation activity of these heterocydk amines were observed. The N-acetylation activity also varied among the substrates used. The N-acetylation of these heterocydk amines by hepatic cytosols from all animal species used was much less than that of the non-heterocydic aromatic amine carcinogen, 2-aminofluorene (2-AF): the N-acetylation of Trp-P-2 was more than one hundred times less than that of 2-AF. These results suggested that the metabolic activation pathway of these mutagenic heterocydk amines is different from that of 2−AF. The hamster but not rat cytosol showed the ability to utilize N-hydroxy−2-acetyl-aminofluorene and 2-acetylaminofluorene as acetyl donor in the N-acetylation of Trp-P-2.