Role of `classical nitroreductase` and O-acetyltransferase in the mutagenicity of plant activated aromatic amines

Journal Article · Wed Oct 01 04:00:00 EDT 1997 · Environmental and Molecular Mutagenesis

OSTI ID:530845

Ju, Y H; Plewa, M J ^[1]

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1. Univ. of Illinois, Urbana, IL (United States)

Benzidine and 4-aminobiphenyl (4-ABP) are activated by intact plant cells and cell free TX1MX into mutagenic metabolites that induce frameshift and base pair substitution mutations in Salmonella typhimurium strains. The plant activation of these agents in plant peroxidase-mediated and bacterial O-acetyltransferase (OAT) dependent. This study was conducted to determine if the plant-activation of benzidine and 4-ABP follows the prostaglandin H synthase-mediated activation pathway in mammals. TX1MX-activated benzidine and 4-ABP were 1-50 {mu}M and 0.1-mM, respectively. The plant activation of benzidine and 4-ABP required a critical level of bacterial nitroreductase as well as OAT to metabolize the plant-activated products. In S. typhimurium strains that over express OAT, nitroreductase was required to metabolize these plant-activated aromatic amines into mutagens. Plant-activated benzidine and 4-ABP induced higher frameshift and base pair substitution mutations in OAT over expressing strains, YG1024 and YG1029 which have a single copy of the nitroreductase gene. The data indicate that the plant-activated benzidine and 4-ABP products have an absolute requirement for O-acetyltransferase in order to be mutagenic in S. typhimurium.

• OSTI ID: 530845
• Report Number(s): CONF-9704100--; CNN: Grant R-823184
• Journal Information: Environmental and Molecular Mutagenesis, Journal Name: Environmental and Molecular Mutagenesis Journal Issue: Suppl.28 Vol. 29; ISSN 0893-6692; ISSN EMMUEG
• Country of Publication: United States
• Language: English

Related Subjects

56 BIOLOGY AND MEDICINE
APPLIED STUDIES
AMINES
BENZIDINE
BIOLOGICAL PATHWAYS
GENETIC EFFECTS
MUTATIONS
SALMONELLA TYPHIMURIUM