Diethyldithiocarbamate suppresses the plant activation of aromatic amines into mutagens by inhibiting tobacco cell peroxidase.

@article{Plewa1991DiethyldithiocarbamateST,
  title={Diethyldithiocarbamate suppresses the plant activation of aromatic amines into mutagens by inhibiting tobacco cell peroxidase.},
  author={Michael J. Plewa and S. Ray Smith and Elizabeth D. Wagner},
  journal={Mutation research},
  year={1991},
  volume={247 1},
  pages={
          57-64
        }
}
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TLDR
The data implicate a TX1 cell peroxidase and a FAD‐dependent monooxygenase in the plant activation of m‐phenylenediamine and an additional pathway of the plant cells in the activation of 2‐aminofluorene may involve a cytochrome P‐448‐type N‐hydroxylase.
Plant activation of m‐phenylenediamine by tobacco, cotton, and carrot cell suspension cultures
TLDR
It is concluded that m‐phenylenediamine is activated by plant cells into a mutagen that primarily induces frameshift mutations.
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In female rats, both topical application and s.c. injection for 18 months of oxidized p-PD could induce a statistically significant incidence of mammary gland tumors, and tumors of other organs including liver, kidney, adrenal gland, thyroid gland, urinary bladder and lung were occasionally observed in male rats of both groups and might be related to the p- PD treatment.
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Results suggest that 2-AF is oxidized to an electrophilic intermediate(s) by prostaglandin endoperoxide synthetase, which either binds covalently to tissue macromolecules or is further rapidly oxidizing to 2-nitrofluorene and azofluorene.
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