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@ARTICLE{Stiborov:128387,
author = {M. Stiborová and K. Levová and F. Bárta and M. Šulc and
E. Frei$^*$ and V. M. Arlt and H. Schmeiser$^*$},
title = {{T}he influence of dicoumarol on the bioactivation of the
carcinogen aristolochic acid {I} in rats.},
journal = {Mutagenesis},
volume = {29},
number = {3},
issn = {1464-3804},
address = {Oxford},
publisher = {Oxford Univ. Press},
reportid = {DKFZ-2017-04404},
pages = {189 - 200},
year = {2014},
abstract = {Aristolochic acid I (AAI) is the major toxic component of
the plant extract AA, which leads to the development of
nephropathy and urothelial cancer in human. Individual
susceptibility to AAI-induced disease might reflect
variability in enzymes that metabolise AAI. In vitroquinone
oxidoreductase (NQO1) is the most potent enzyme that
activates AAI by catalyzing formation of AAI-DNA adducts,
which are found in kidneys of patients exposed to AAI.
Inhibition of renal NQO1 activity by dicoumarol has been
shown in mice. Here, we studied the influence of dicoumarol
on metabolic activation of AAI in Wistar rats in vivo. In
contrast to previous in vitro findings, dicoumarol did not
inhibit AAI-DNA adduct formation in rats. Compared with rats
treated with AAI alone, 11- and 5.4-fold higher AAI-DNA
adduct levels were detected in liver and kidney,
respectively, of rats pretreated with dicoumarol prior to
exposure to AAI. Cytosols and microsomes isolated from liver
and kidney of these rats were analysed for activity and
protein levels of enzymes known to be involved in AAI
metabolism. The combination of dicoumarol with AAI induced
NQO1 protein level and activity in both organs. This was
paralleled by an increase in AAI-DNA adduct levels found in
ex vivo incubations with cytosols from rats pretreated with
dicoumarol compared to cytosols from untreated rats.
Microsomal ex vivo incubations showed a lower AAI
detoxication to its oxidative metabolite,
8-hydroxyaristolochic acid (AAIa), although cytochrome P450
(CYP) 1A was practically unchanged. Because of these
unexpected results, we examined CYP2C activity in microsomes
and found that treatment of rats with dicoumarol alone and
in combination with AAI inhibited CYP2C6/11 in liver.
Therefore, these results indicate that CYP2C enzymes might
contribute to AAI detoxication.},
keywords = {Aristolochic Acids (NLM Chemicals) / Carcinogens (NLM
Chemicals) / Cytochromes (NLM Chemicals) / DNA Adducts (NLM
Chemicals) / Mutagens (NLM Chemicals) / Dicumarol (NLM
Chemicals) / aristolochic acid I (NLM Chemicals) / Cyp1a2
protein, rat (NLM Chemicals) / Cytochrome P-450 CYP1A1 (NLM
Chemicals) / Cytochrome P-450 CYP1A2 (NLM Chemicals) /
NAD(P)H Dehydrogenase (Quinone) (NLM Chemicals) / NQO1
protein, rat (NLM Chemicals)},
cin = {G110 / C016 / E030},
ddc = {570},
cid = {I:(DE-He78)G110-20160331 / I:(DE-He78)C016-20160331 /
I:(DE-He78)E030-20160331},
pnm = {315 - Imaging and radiooncology (POF3-315)},
pid = {G:(DE-HGF)POF3-315},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:24598128},
doi = {10.1093/mutage/geu004},
url = {https://inrepo02.dkfz.de/record/128387},
}