title: Oxidation of nuclear thioredoxin during oxidative stress.
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.
authors.affiliation: Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, GA 30322, USA. wwatson@emory.edu
authors.forename: Walter H
authors.initials: WH
authors.lastname: Watson
authors.forename: Dean P
authors.initials: DP
authors.lastname: Jones
mesh_terms: D021581:Active Transport, Cell Nucleus; D002460:Cell Line; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D003600:Cytosol / Q000737:chemistry; D005978:Glutathione / Q000737:chemistry; D019803:Glutathione Disulfide / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism; D020122:tert-Butylhydroperoxide / Q000494:pharmacology
chemical_list: D008565:Membrane Proteins; D009687:Nuclear Proteins; C491203:TXN protein, human; D013879:Thioredoxins; D020122:tert-Butylhydroperoxide; D005978:Glutathione; D019803:Glutathione Disulfide