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

• Published in: Carcinogenesis (New York) Vol. 5; no. 5; p. 683
• Main Authors: Shinohara, A, Yamazoe, Y, Saito, K, Kamataki, T, Kato, R
• Format: Journal Article
• Language: English
• Published: England 01.05.1984
• Subjects: Acetylation; Animals; Carbolines - metabolism; Cricetinae; Cytosol - metabolism; Female; Heterocyclic Compounds - metabolism; Hot Temperature; Indoles - metabolism; Kinetics; Liver - metabolism; Male; Mesocricetus; Mice; Mice, Inbred Strains; Mutagens - metabolism; Proteins; Rabbits; Rats; Rats, Inbred Strains; Species Specificity
• ISSN: 0143-3334
• 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 heterocyclic aromatic amine promutagens 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 heterocyclic amines were observed. The N-acetylation activity also varied among the substrates used. The N-acetylation of these heterocyclic amines by hepatic cytosols from all animal species used was much less than that of the non-heterocyclic 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 heterocyclic amines is different from that of 2-AF. The hamster but not rat cytosol showed the ability to utilize N-hydroxy-2-acetylaminofluorene and 2-acetylaminofluorene as acetyl donor in the N-acetylation of Trp-P-2.