Species differences in the N-acetylation by liver cytosol of mutagenic heterocyclic aromatic amines in protein pyrolysates.
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.
D000107:Acetylation; D000818:Animals; D002243:Carbolines / Q000378:metabolism*; D006224:Cricetinae; D003600:Cytosol / Q000378:metabolism; D005260:Female; D006571:Heterocyclic Compounds / Q000378:metabolism*; D006358:Hot Temperature; D007211:Indoles / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D008647:Mesocricetus; D051379:Mice; D008815:Mice, Inbred Strains; D009153:Mutagens / Q000378:metabolism*; D011506:Proteins; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D013045:Species Specificity
D002243:Carbolines; D006571:Heterocyclic Compounds; D007211:Indoles; D009153:Mutagens; D011506:Proteins; C019133:3-amino-1-methyl-5H-pyrido(4,3-b)indole