Effect of sulforaphane on glutathione-adduct formation and on glutathione_<I>S</I>_transferase-dependent detoxification of acrylamide in Caco-2 cells Export

@article{citeulike:6100240, abstract = {The toxicity of dietary acrylamide (AA) depends on its biotransformation pathways, in which phase I cytochrome P-450 enzymes transform AA into glycidamide. The phase II enzyme glutathione\_S\_transferase (GST) catalyses the conjugation of AA with glutathione (GSH). GST induction by phytochemicals like sulforaphane (SFN) plays a role in chemoprevention. Here, the effect of SFN on the detoxification of AA through GSH conjugation was studied in Caco-2 cells. GSH adducts with AA and SFN were synthesized, identified by NMR and quantified by LC-MS/MS. Caco-2 cells were treated with either 2.5 mM AA, 10 muM SFN or the combination of both for 24 h. Concentrations of GSH conjugates (GSH-AA, GSH-SFN, SFN-GSH-AA), AA and SFN were analysed by LC-MS/MS. GSH contents and GST activity were determined photometrically. GST activity was increased after treatment of the cells with SFN (38±6\%, ple0.05) or AA (25±4\%, ple0.05). GSH concentrations decreased after all treatments. Quantitative data of GSH adduct formation showed that the reaction between GSH and SFN is favoured over that between GSH and AA. The data suggest that SFN might impair the GSH-dependent detoxification of AA by SFN-GSH adduct formation and, thus, lower the GSH concentrations available for its reaction with AA.}, address = {University of Naples, Portici, Italy; Deutsche Forschungsanstalt f\"{u}r Lebensmittelchemie, Garching, Germany}, author = {Pernice, Rita and Hauder, Johanna and Koehler, Peter and Vitaglione, Paola and Fogliano, Vincenzo and Somoza, Veronika}, citeulike-article-id = {6100240}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/mnfr.200900447}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/122681035/ABSTRACT}, doi = {10.1002/mnfr.200900447}, issn = {1613-4133}, journal = {Molecular Nutrition \& Food Research}, number = {9999}, pages = {NA+}, posted-at = {2009-11-11 23:43:23}, priority = {3}, title = {Effect of sulforaphane on glutathione-adduct formation and on glutathione\_<I>S</I>\_transferase-dependent detoxification of acrylamide in Caco-2 cells}, url = {http://dx.doi.org/10.1002/mnfr.200900447}, volume = {9999}, year = {2009} }

TY - JOUR ID - citeulike:6100240 L3 - citeulike-article-id:6100240 N2 - The toxicity of dietary acrylamide (AA) depends on its biotransformation pathways, in which phase I cytochrome P-450 enzymes transform AA into glycidamide. The phase II enzyme glutathione_S_transferase (GST) catalyses the conjugation of AA with glutathione (GSH). GST induction by phytochemicals like sulforaphane (SFN) plays a role in chemoprevention. Here, the effect of SFN on the detoxification of AA through GSH conjugation was studied in Caco-2 cells. GSH adducts with AA and SFN were synthesized, identified by NMR and quantified by LC-MS/MS. Caco-2 cells were treated with either 2.5 mM AA, 10 muM SFN or the combination of both for 24 h. Concentrations of GSH conjugates (GSH-AA, GSH-SFN, SFN-GSH-AA), AA and SFN were analysed by LC-MS/MS. GSH contents and GST activity were determined photometrically. GST activity was increased after treatment of the cells with SFN (38±6%, ple0.05) or AA (25±4%, ple0.05). GSH concentrations decreased after all treatments. Quantitative data of GSH adduct formation showed that the reaction between GSH and SFN is favoured over that between GSH and AA. The data suggest that SFN might impair the GSH-dependent detoxification of AA by SFN-GSH adduct formation and, thus, lower the GSH concentrations available for its reaction with AA. IS - 9999 JF - Molecular Nutrition & Food Research SN - 1613-4133 AD - University of Naples, Portici, Italy; Deutsche Forschungsanstalt für Lebensmittelchemie, Garching, Germany TI - Effect of sulforaphane on glutathione-adduct formation and on glutathione_<I>S</I>_transferase-dependent detoxification of acrylamide in Caco-2 cells VL - 9999 SP - NA AU - Pernice, Rita AU - Hauder, Johanna AU - Koehler, Peter AU - Vitaglione, Paola AU - Fogliano, Vincenzo AU - Somoza, Veronika PY - 2009/// UR - http://dx.doi.org/10.1002/mnfr.200900447 ER -