%0 Journal Article %1 Hu.200710 %A Hu, Ying %A Urig, Sabine %A Koncarevic, Sasa %A Wu, Xinjiang %A Fischer, Marina %A Rahlfs, Stefan %A Mersch-Sundermann, Volker %A Becker, Katja %D 2007/10// %J Biol Chem %K 2'-disulfonic_Acid 4-Acetamido-4'-isothiocyanatostilbene-2 Allyl_Compounds Anticarcinogenic_Agents Cell_Cycle Cell_Line Cell_Proliferation Disulfides Dose-Response_Relationship Drug Glutathione Glutathione_Transferase Humans IFZ Oxidation-Reduction Sulfur_Compounds Thioredoxin-Disulfide_Reductase Thioredoxins Tumor Up-Regulation glutathione_peroxidase isothiocyanates %N 10 %P 1069-1081 %T Glutathione- and thioredoxin-related enzymes are modulated by sulfur-containing chemopreventive agents %V 388 %X We studied the effects of sulfur-containing chemopreventive agents, including allyl sulfides and isothiocyanates, on human redox networks. Isothiocyanates inhibited isolated redox-active enzymes in a time- and dose-dependent manner. As shown for the most active compound, benzyl isothiocyanate (BITC), on thioredoxin reductase, the inhibition has an initial competitive part (Ki=6.1+/-1.0 microM) followed by a time-dependent irreversible inhibition (k2=72.8+/-25.5 M(-1) s(-1)). Also, glutathione reductase and glutathione S-transferase were irreversibly modified by BITC. Sulforaphane led to irreversible inhibition of the studied redox enzymes, but with 5-10 times lower k2 values. In contrast, allyl sulfides had only moderate effects on the tested enzymes. However, diallyl disulfide was found to react directly with reduced glutathione (k2=100 M(-2) s(-1)). This reaction might contribute to enhanced oxidative stress and the induction of the selenoprotein glutathione peroxidase as determined

@article{Hu.200710, abstract = {We studied the effects of sulfur-containing chemopreventive agents, including allyl sulfides and isothiocyanates, on human redox networks. Isothiocyanates inhibited isolated redox-active enzymes in a time- and dose-dependent manner. As shown for the most active compound, benzyl isothiocyanate (BITC), on thioredoxin reductase, the inhibition has an initial competitive part (Ki=6.1+/-1.0 microM) followed by a time-dependent irreversible inhibition (k2=72.8+/-25.5 M(-1) s(-1)). Also, glutathione reductase and glutathione S-transferase were irreversibly modified by BITC. Sulforaphane led to irreversible inhibition of the studied redox enzymes, but with 5-10 times lower k2 values. In contrast, allyl sulfides had only moderate effects on the tested enzymes. However, diallyl disulfide was found to react directly with reduced glutathione (k2=100 M(-2) s(-1)). This reaction might contribute to enhanced oxidative stress and the induction of the selenoprotein glutathione peroxidase as determined }, added-at = {2008-10-14T16:07:18.000+0200}, author = {Hu, Ying and Urig, Sabine and Koncarevic, Sasa and Wu, Xinjiang and Fischer, Marina and Rahlfs, Stefan and Mersch-Sundermann, Volker and Becker, Katja}, biburl = {https://www.bibsonomy.org/bibtex/208e03de016eac0326ebb47c3922bbc3d/nutribiochem}, interhash = {5cc54ebfcc4e6e07c7650f4055370545}, intrahash = {08e03de016eac0326ebb47c3922bbc3d}, journal = {Biol Chem}, keywords = {2'-disulfonic_Acid 4-Acetamido-4'-isothiocyanatostilbene-2 Allyl_Compounds Anticarcinogenic_Agents Cell_Cycle Cell_Line Cell_Proliferation Disulfides Dose-Response_Relationship Drug Glutathione Glutathione_Transferase Humans IFZ Oxidation-Reduction Sulfur_Compounds Thioredoxin-Disulfide_Reductase Thioredoxins Tumor Up-Regulation glutathione_peroxidase isothiocyanates}, number = 10, pages = {1069-1081}, timestamp = {2008-10-14T16:08:41.000+0200}, title = {Glutathione- and thioredoxin-related enzymes are modulated by sulfur-containing chemopreventive agents}, volume = 388, year = {2007/10//} }