Oxidation of nuclear thioredoxin during oxidative stress

FEBS Lett. 2003 May 22;543(1-3):144-7. doi: 10.1016/s0014-5793(03)00430-7.

Abstract

Thioredoxin 1 (Trx1) is a key redox control system within the nucleus, yet little is known about the sensitivity of nuclear Trx1 to oxidative stress. The present study compared oxidant-induced changes in the redox states of nuclear Trx1, cytoplasmic Trx1, and cellular glutathione (GSH). Nuclear Trx1 was more reducing than cytoplasmic Trx1 and cellular GSH in proliferating cells. tert-Butylhydroperoxide caused an increase in the total amount of nuclear Trx1, but this was accompanied by a 60 mV oxidation. Thus, the increase in nuclear Trx1 levels did not correspond to an increase in the overall reducing capacity of Trx1 in the nucleus.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Active Transport, Cell Nucleus
  • Cell Line
  • Cell Nucleus / chemistry
  • Cell Nucleus / metabolism
  • Cytosol / chemistry
  • Glutathione / chemistry
  • Glutathione Disulfide / chemistry
  • Humans
  • Kinetics
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Oxidation-Reduction
  • Oxidative Stress*
  • Thioredoxins / chemistry*
  • Thioredoxins / metabolism
  • tert-Butylhydroperoxide / pharmacology

Substances

  • Membrane Proteins
  • Nuclear Proteins
  • TXN protein, human
  • Thioredoxins
  • tert-Butylhydroperoxide
  • Glutathione
  • Glutathione Disulfide