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Free radical research, v.33 no.6, 2000년, pp.851 - 855
Tanaka, Toru (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan) , Nakamura, Hajime (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan) , Nishiyama, Akira (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan) , Hosoi, Fumihito (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan) , Masutani, Hiroshi (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan) , Wada, Hiromi (Department of Thoracic Surgery, Faculty of Medicine, Kyoto University, Japan) , Yodoi, Junji (Department of Biological Responses, Institute for virus Research, Kyoto University, Japan)
Thioredoxin (TRX) is a 12 kD protein with redox-active dithiol in the active site; -Cys-Gly-Pro-Cys-. We originally cloned human TRX as adult T cell leukemia derived factor (ADF) produced by HTLV-I transformed cells. TRX and related molecules maintain a cellular reducing environment, working in concert with the glutathione system. Physiologically, TRX has cytoprotective effects against oxidative stress. TRX promotes DNA binding of transcription factors such as NF-kB, AP-1, p53, and PEBP-2. The TRX superfamily, including thioredoxin-2 (mitochondrial thioredoxin) and glutaredoxin, are involved in biologically important phenomena via the redox-regulating system. Thioredoxin-binding protein-2, which we recently identified by a yeast two-hybrid system, is a type of endogenous modulator of TRX activity. TRX is secreted from the cells and exhibits cytokine-like and chemokine-like activities. Redox regulation by TRX plays a crucial role in biological responses against oxidative stress.
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