Oxidation of nuclear thioredoxin during oxidative stress

FEBS Letters

Watson, Walter H.¹  Jones, Dean P.¹ 

[1] Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, GA 30322, USA

关键词: Thioredoxin;    Redox;    Oxidative stress;    Nucleus;    Protein oxidation;    Glutathione;    Trx1;    human thioredoxin;    GSH;    glutathione;    GSSG;    glutathione disulfide;    tBH;    tert-butylhydroperoxide;    IAA;    iodoacetic acid;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(03)00430-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown