Protective effects of five allium derived organosulfur compounds against mutation and oxidation

Food Chem. 2016 Apr 15;197(Pt A):829-35. doi: 10.1016/j.foodchem.2015.11.064. Epub 2015 Nov 14.

Abstract

In this study, we examined the ability of five allium-derived organosulfur compounds to protect cells against mutation and oxidation. The compounds tested were 1-propylmercaptan (PM), dimethyl disulfide (DMDS), diallyl disulfide (DADS), propyl disulfide (PDS), and 2,5-dimethylthiophene (DMT). Our results showed that when used at concentrations of 100-400 μmol/l, the five compounds inhibited the mutagenicity of 4-nitroquinoline-N-oxide, a direct mutagen, and benzo[a]pyrene, an indirect mutagen, toward Salmonella typhimurium TA 98 and TA 100. Furthermore, at these concentrations, all five of the compounds protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative cytotoxicity. The compounds likely enhanced cell viability by suppressing the formation of reactive oxygen species and the depletion of glutathione depletion in cells. DMT and PM inhibited mutation and oxidation to a greater extent than DMDS, DADS, and PDS. These results demonstrate for the first time that DMT and PM can contribute to the antimutagenic and the antioxidative property of Allium vegetables.

Keywords: Antioxidation; Cytotoxicity; Mutation; Organosulfur compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allium / chemistry*
  • Allyl Compounds / pharmacology*
  • Benzo(a)pyrene / toxicity
  • Cells / drug effects
  • Cells / metabolism
  • Disulfides / pharmacology*
  • Glutathione / metabolism
  • Glutathione Transferase / metabolism
  • Hep G2 Cells
  • Humans
  • Mutagens / toxicity
  • Mutation / drug effects*
  • Oxidation-Reduction / drug effects
  • Plant Extracts / pharmacology*
  • Protective Agents / pharmacology*

Substances

  • Allyl Compounds
  • Disulfides
  • Mutagens
  • Plant Extracts
  • Protective Agents
  • Benzo(a)pyrene
  • dimethyl disulfide
  • diallyl disulfide
  • Glutathione Transferase
  • Glutathione