Binding of α-tocopherylquinone, an oxidized form of α-tocopherol, to glutathione-S-transferase in the liver cytosol

Makoto Arita, Yuji Sato, Hiroyuki Arai, Keizo Inoue

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

α-Tocopherol (vitamin E) is an important fat-soluble antioxidant in biological systems and, as a result of scavenging reactive oxygen, it is converted to α-tocopherylquinone. α-Tocopherol binds to α-tocopherol transfer protein (αTTP) in the liver cytosol, whereas α-tocopherylquinone does not. We found that α-tocopherylquinone binds to a liver protein with a molecular mass of about 40 kDa that is distinct from αTTP. This α-tocopherylquinone binding protein was purified further by multiple-step column chromatography. Sodium dodecylsulfate-polyacrylamide gel electrophoresis of the final preparation yielded a single band with an apparent molecular mass of 25 kDa, which microsequencing revealed was identical to glutathione-S-transferase (GST). The GST activity was inhibited in the presence of α-tocopherylquinone, as it is by other non-substrate ligands for GST, confirming that GST and α-tocopherylquinone interact directly. α-Tocopherylquinone binds to GST and may be transported to the site of metabolism or excreted in the bile as other non-substra.

Original languageEnglish
Pages (from-to)424-426
Number of pages3
JournalFEBS Letters
Volume436
Issue number3
DOIs
Publication statusPublished - 1998 Oct 9

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Keywords

  • Antioxidant
  • Binding protein
  • Glutathione-S-transferase
  • Rat liver
  • α-Tocopherol
  • α-Tocopherylquinone

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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