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

36 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
Externally publishedYes

Fingerprint

Tocopherols
Glutathione Transferase
Liver
Cytosol
Molecular mass
Column chromatography
Proteins
Scavenging
Biological systems
tocopherylquinone
Electrophoresis
Vitamin E
Metabolism
Bile
Chromatography
Polyacrylamide Gel Electrophoresis
Carrier Proteins
Antioxidants
Sodium
Fats

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Binding of α-tocopherylquinone, an oxidized form of α-tocopherol, to glutathione-S-transferase in the liver cytosol. / Arita, Makoto; Sato, Yuji; Arai, Hiroyuki; Inoue, Keizo.

In: FEBS Letters, Vol. 436, No. 3, 09.10.1998, p. 424-426.

Research output: Contribution to journalArticle

@article{b4139673c82c46a7b7a3f7cf78fa015f,
title = "Binding of α-tocopherylquinone, an oxidized form of α-tocopherol, to glutathione-S-transferase in the liver cytosol",
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.",
keywords = "α-Tocopherol, α-Tocopherylquinone, Antioxidant, Binding protein, Glutathione-S-transferase, Rat liver",
author = "Makoto Arita and Yuji Sato and Hiroyuki Arai and Keizo Inoue",
year = "1998",
month = "10",
day = "9",
doi = "10.1016/S0014-5793(98)01176-4",
language = "English",
volume = "436",
pages = "424--426",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Binding of α-tocopherylquinone, an oxidized form of α-tocopherol, to glutathione-S-transferase in the liver cytosol

AU - Arita, Makoto

AU - Sato, Yuji

AU - Arai, Hiroyuki

AU - Inoue, Keizo

PY - 1998/10/9

Y1 - 1998/10/9

N2 - 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.

AB - 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.

KW - α-Tocopherol

KW - α-Tocopherylquinone

KW - Antioxidant

KW - Binding protein

KW - Glutathione-S-transferase

KW - Rat liver

UR - http://www.scopus.com/inward/record.url?scp=0031788232&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031788232&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(98)01176-4

DO - 10.1016/S0014-5793(98)01176-4

M3 - Article

VL - 436

SP - 424

EP - 426

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -