FEBS Letters | |
Oxidation of nuclear thioredoxin during oxidative stress | |
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
【 预 览 】
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RO201912020312972ZK.pdf | 183KB | download |