The Effect of Sulforaphane on Glyoxalase I Expression and Activity in Peripheral Blood Mononuclear Cells

Nutrients. 2018 Nov 15;10(11):1773. doi: 10.3390/nu10111773.

Abstract

Studies demonstrate that the potential health-beneficial effect of sulforaphane (SR), a compound formed in broccoli, is the result of a number of mechanisms including upregulation of phase two detoxification enzymes. Recent studies suggest that SR increases expression/activity of glyoxalase 1 (Glo1), an enzyme involved in the degradation of methylglyoxal, is major precursor of advanced glycation end products. Those compounds are associated with diabetes complications and other age-related diseases. In this study, the effect of SR on the expression/activity of Glo1 in peripheral blood mononuclear cells (PBMCs) from 8 healthy volunteers was investigated. PBMCs were isolated and incubated with SR (2.5 μM-concentration achievable by consuming a broccoli portion) for 24 h and 48 h. Glo1 activity/expression, reduced glutathione (GSH), and glutathione-S-transferase gene expression were measured. Glo1 activity was not affected while after 48 h a slight but significant increase of its gene expression (1.03-fold) was observed. GSTP1 expression slightly increased after 24 h incubation (1.08-fold) while the expressions of isoform GSTT2 and GSTM2 were below the limit of detection. GSH sharply decreased, suggesting the formation of GSH-SR adducts that may have an impact SR availability. Those results suggest that a regular exposure to SR by broccoli consumption or SR supplements may enhance Glo1.

Keywords: glutathione; glutathione-S-transferase; glyoxalase 1; peripheral blood mononuclear cells; sulforaphane.

MeSH terms

  • Adult
  • Brassica / chemistry
  • Eating / physiology*
  • Female
  • Glutathione / metabolism
  • Glutathione Transferase / metabolism
  • Humans
  • Isothiocyanates / pharmacology*
  • Lactoylglutathione Lyase / metabolism*
  • Leukocytes, Mononuclear / metabolism*
  • Male
  • Middle Aged
  • Sulfoxides

Substances

  • Isothiocyanates
  • Sulfoxides
  • Glutathione Transferase
  • GLO1 protein, human
  • Lactoylglutathione Lyase
  • sulforaphane
  • Glutathione