Activation of arylamines to mutagenic product(s) by two in vitro plant systems

Activation of arylamines to mutagenic product(s) by two in vitro plant systems

Plant activation of three isomers of phenylenediamine, o-, m- and p-phenylenediamine, has been studied. Two in vitro plant systems have been used: Persea americana S117 with mixed-function oxidase (MFO) and peroxidase activities, and Zea mays S9 which contains only peroxidase activity. As genetic en...

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Bibliographic Details
Published in:Mutation research Vol. 394; no. 1; pp. 45 - 51
Main Authors: Chiapella, Carles, Moreno, José Antonio, Radovan, Rodrigo D, Gaubert, Nathalie, Llagostera, Montserrat
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 27-11-1997
Subjects:
2-Aminofluorene
Animals
Biotransformation
Isomerism
Mixed-function oxidase
Mutagens - metabolism
o, m, p-Phenylenediamine
Peroxidase
Persea americana S117
Phenylenediamines - chemistry
Phenylenediamines - pharmacokinetics
Plant activation
Plants - metabolism
Rats
Zea mays S9
Zea mays S9
2-Aminofluorene
Plant activation
Persea americana S117
Peroxidase
Mixed-function oxidase
o, m, p-Phenylenediamine
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Summary:Plant activation of three isomers of phenylenediamine, o-, m- and p-phenylenediamine, has been studied. Two in vitro plant systems have been used: Persea americana S117 with mixed-function oxidase (MFO) and peroxidase activities, and Zea mays S9 which contains only peroxidase activity. As genetic endpoint, the classical Salmonella tester strains, TA98 and TA100, their derivatives with high O-acetyltransferase levels (YG1024 and YG1029, respectively) and TA98/1,8-DNP 6, deficient in this enzyme, have been assayed. Of the three isomers studied, only m-PDA was activated to mutagenic product(s) by both plant systems. This activation required the bacterial O-acetyltransferase activity to give frameshift mutagenic product(s), detected in TA98 and YG1024 strains. In all the assays the P. americana system was more potent than the Z. mays system in activating m-PDA. A slight increase of the number of YG1029 revertants was detected when m-PDA was activated by P. americana, suggesting that this compound can be also converted into ultimate mutagenic product(s) that induce base-pair substitutions. m-PDA activation by Z. mays was dependent on the peroxidase activity of this system, but the activation produced by P. americana was totally dependent on MFOs, because a total inhibition of the mutagenic response was found when these activities were inhibited. In addition, the P. americana system was more potent in generating proximal mutagenic forms from m-PDA than S9 from non-induced rat liver, although S9 from Aroclor 1254-induced Sprague-Dawley male rats was the most potent system in the m-PDA activation. These results indicate that the P. americana system can be useful in determining the role of mixed-function oxidases in plant activation of xenobiotics.
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ISSN:1383-5718
0027-5107
1879-3592
DOI:10.1016/S1383-5718(97)00122-8