Effect of sulforaphane on glutathione-adduct formation and on glutathione_S_transferase-dependent detoxification of acrylamide in Caco-2 cells

Rita Pernice, Johanna Hauder, Peter Koehler, Paola Vitaglione, Vincenzo Fogliano, Veronika Somoza

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

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 2.5mM AA, 10 mM SFN or the combination of both for 24h. 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 (3876%, pr0.05) or AA (2574%, pr0.05). 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.

Original languageEnglish
Pages (from-to)1540-1550
Number of pages11
JournalMolecular Nutrition and Food Research
Volume53
Issue number12
DOIs
StatePublished - Dec 2009
Externally publishedYes

Keywords

  • Acrylamide
  • Caco-2 cells
  • GSH adducts
  • Glutathione-S-transferase
  • Sulforaphane

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