About: Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases     Goto   Sponge   NotDistinct   Permalink

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  • Ingestion of aristolochic acid (AA) is associated with development of urothelial tumors linked with aristolochic acid nephropathy, and is implicated in the development of Balkan endemic nephropathy-associated urothelial tumors. Aristolochic acid I (AAI), the major toxic component of AA, is more toxic than its demethoxylated derivate AAII. A different enzymatic conversion of both carcinogens might be one of the reasons explaining this feature. Therefore, the present study has been designed to compare efficiency of human NAD(P)H:quinone oxidoreductase (NQO1) and phase II enzymes such as sulfotransferases (SULTs) and N,O-acetyltransferases (NATs) to activate AAI and AAII in vitro. In addition, to investigate the molecular mechanisms of AAI and AAII reduction by human NQO1, molecular modeling was used to compare interactions of AAI and AAII with the active site of this enzyme.
  • Ingestion of aristolochic acid (AA) is associated with development of urothelial tumors linked with aristolochic acid nephropathy, and is implicated in the development of Balkan endemic nephropathy-associated urothelial tumors. Aristolochic acid I (AAI), the major toxic component of AA, is more toxic than its demethoxylated derivate AAII. A different enzymatic conversion of both carcinogens might be one of the reasons explaining this feature. Therefore, the present study has been designed to compare efficiency of human NAD(P)H:quinone oxidoreductase (NQO1) and phase II enzymes such as sulfotransferases (SULTs) and N,O-acetyltransferases (NATs) to activate AAI and AAII in vitro. In addition, to investigate the molecular mechanisms of AAI and AAII reduction by human NQO1, molecular modeling was used to compare interactions of AAI and AAII with the active site of this enzyme. (en)
Title
  • Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases
  • Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases (en)
skos:prefLabel
  • Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases
  • Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases (en)
skos:notation
  • RIV/00216208:11310/11:10107363!RIV12-GA0-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0505), P(GA203/09/0812), P(GA303/09/0472), Z(MSM0021620808)
http://linked.open...iv/cisloPeriodika
  • Suppl. 1
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 191061
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/11:10107363
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • molecular modeling; DNA adducts; acetyltransferase; sulfotransferase; NAD(P)H:quinone oxidoreductase; aristolochic acid (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • SE - Švédské království
http://linked.open...ontrolniKodProRIV
  • [42029E6842B9]
http://linked.open...i/riv/nazevZdroje
  • Neuroendocrinology Letters
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 32
http://linked.open...iv/tvurceVysledku
  • Arlt, Volker M.
  • Frei, Eva
  • Hudeček, Jiří
  • Kubíčková, Božena
  • Martínek, Václav
  • Schmeiser, Heinz H.
  • Stiborová, Marie
http://linked.open...n/vavai/riv/zamer
issn
  • 0172-780X
number of pages
http://localhost/t...ganizacniJednotka
  • 11310
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