The Human Carcinogen Aristolochic Acid I Is Activated to Form DNA Adducts by Human NAD(P)H:quinone Oxidoreductase Without the Contribution of Acetyltransferases or Sulfotransferases
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10100373" target="_blank" >RIV/00216208:11310/11:10100373 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11130/11:7041
Result on the web
<a href="http://dx.doi.org/10.1002/em.20642" target="_blank" >http://dx.doi.org/10.1002/em.20642</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/em.20642" target="_blank" >10.1002/em.20642</a>
Alternative languages
Result language
angličtina
Original language name
The Human Carcinogen Aristolochic Acid I Is Activated to Form DNA Adducts by Human NAD(P)H:quinone Oxidoreductase Without the Contribution of Acetyltransferases or Sulfotransferases
Original language description
Ingestion of aristolochic acid (AA) is associated with development of urothelial tumors linked with AA nephropathy and is implicated in the development of Balkan endemic nephropathy-associated urothelial tumors. We investigated the efficiency of human NAD(P)H:quinone oxidoreductase (NQO1) to activate aristolochic acid I (AAI) and used in silico docking, using soft-soft (flexible) docking procedure, to study the interactions of AAI with the active site of human NQO1. AAI binds to the active site of NQO1indicating that the binding orientation allows for direct hydride transfer (i.e., two electron reductions) to the nitro group of AAI. NQO1 activated AAI, generating DNA adduct patterns reproducing those found in urothelial tissues from humans exposed toAA. Because reduced aromatic nitro-compounds are often further activated by sulfotransferases (SULTs) or N,O-acetlytransferases (NATs), their roles in AAI activation were investigated. Our results indicate that phase II reactions do not p
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Environmental and Molecular Mutagenesis
ISSN
0893-6692
e-ISSN
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Volume of the periodical
52
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
448-459
UT code for WoS article
000293250700003
EID of the result in the Scopus database
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