Abstract
Oxidative stress evokes various cellular responses including alteration of gene expression to preserve cellular homeostasis (1,2). Thioredoxin (TRX) is a small ubiquitous protein with protein thiol-reducing activity and has been shown to function as a cellular antioxidant buffering system in response to oxidative stress and play essential roles in maintenance of cellular function (3,4). Recently, a growing number of evidence has shown that TRX plays crucial roles in redox regulation of gene expression via either direct or indirect interaction with various transcription factors including NF-κB (5), AP-1 (6), and PEBP2 (7). Alteration in expression and/or subcellular localization of TRX has been indicated to be involved in such redox-dependent control of the transcription factors (8,9), however, precise mechanisms remain unknown.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsSpringer Nature is developing a new tool to find and evaluate Protocols. Learn more
References
Yu, B. P. (1994) Cellular defenses against damage from reactive oxygen species. Physiol. Rev. 74, 139–162.
Demple, B. and Amabile-Cuevas, C. F. (1991) Redox redux: the control of oxidative stress responses. Cell 67, 837–839.
Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3, 239–243.
Holmgren, A. (1985) Thioredoxin. Annu. Rev. Biochem. 54, 237–271.
Schenk, H., Klein, M., Erdbrugger, W., Droge, W., and Schulze-Osthoff, K. (1994) Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-ΚB and AP-1. Proc. Natl. Acad. Sci. USA 91, 1672–1676.
Meyer, M., Schreck, R., and Baeuerle, P. A. (1993) H2O2 and antioxidants have opposite effects on activation of NF-ΚB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J. 12, 2005–2015.
Akamatsu, Y., Ohno, T., Hirota, K., Kagoshima, H., Yodoi, J., and Shigesada, K. (1997) Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues. J. Biol. Chem. 272, 14497–14500.
Makino, Y., Yoshikawa, N., Okamoto, K., Hiorota, K., Yodoi, J., Makino, I., and Tanaka, H. (1999) Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem. 274, 3182–3188.
Hirota, K., Murata, M., Sachi, Y., Nakmura, H., Takeuchi, J., Mori, K., and Yodoi, J. (1999) Distinct roles of thioredoxin in the cytoplasm and in the nucleus. J. Biol. Chem. 274, 27891–27897.
Evans, R. M. (1988) The steroid and thyroid hormone receptor superfamily. Science 240, 889–895.
Beato, M., Herrlich, P., and Schutz, G. (1995) Steroid receptors: many actors in search of a plot. Cell 83, 851–857.
Picard, D. and Ymamoto, K. R. (1987) Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6, 3333–3340.
Simons, S. S.Jr. and Pratt, W. B. (1995) Glucocorticoid receptor thiols and steroid-binding activity. Methods Enzymol. 251, 406–422.
Bodwell, J. E., Holbrook, N. J., and Munck, A. (1984) Sulfhydryl-modifying reagents reversibly inhibit binding of glucocorticoid-receptor complexes to DNA-cellulose. Biochemistry 23, 1392–1398.
Okamoto, K., Tanaka, H., Ogawa, H., Makino, Y., Eguchi, H., Hayashi, S., et al. (1999) Redox-dependent regulation of nuclear import of the glucocoritcoid receptor. J. Biol. Chem. 274, 10363–10371.
Makino Y., Tanaka, H., Dahlman-Wright, K., and Makino, I. (1996) Modulation of glucocorticoid-inducible gene expression by metal ions. Mol. Pharmacol. 49, 612–620.
Makino, Y., Okamoto, K., Yoshikawa, N., Aoshima, M., Hirota, K., Yodoi, J., et al. (1996) Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defence system. J. Clin. Invest. 98, 2469–2477.
Hayashi, S., Hajiro-Nakanishi, K., Makino, Y., Eguchi, H., and Tanaka, H. (1997) Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator. Nucleic Acids Res. 25, 4035–4040.
Taniguchi, Y., Taniguchi-Ueda, Y., Mori, K., and Yodoi, J. (1996) A novel promoter sequence is involved in stress-induced expression of the adult T-cell leukemiaderived factor (ADF)/human thioredoxin (TRX) gene. Nucleic Acids Res. 24, 2746–2752.
Sachi, Y., Hirota, K., Masutani, H., Toda, K., Okamoto, T., Takigawa, M., and Yodoi, J. (1995) Induction of ADF/TRX by oxidative stress in keratinocytes and lymphoid cells. Immunol. Lett. 44, 189–193.
Wakasugi, N., Tagaya, Y., Wakasugi, H., Mitsui, A., Maeda, M., Yodoi, J., and Tursz, T. (1990) Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotrophic virus type I-and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2. Proc. Natl. Acad. Sci. USA 87, 8282–8286.
Sasada, T., Iwata, S., Sato, N., Kitaoka, Y., Hirota, K., Nakamura, K., et al. (1996) Redox control of resistence to cis-diamminedichloroplatinum (II) (CDDP). Protective effect of human thioredoxin against CDDP-induced cytotoxicity. J. Clin. Invest. 97, 2268–2276.
Hirota, K., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., and Yodoi, J. (1997) AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc. Natl. Acad. Sci. USA 94, 3633–3638.
Nakamura, H., Nakamura, H., and Yodi, J. (1997) Redox regulation of cellular activation. Annu. Rev. Immunol. 15, 351–369.
Schenk, H., Vogt, M., Droge, W., and Schulze-Osthoff, K. (1996) Thioredoxin as a potent costimulus of cytokine expression. J. Immunol. 156, 765–771.
Yokomizo, A., Ono, M., Nanri, H., Makino, Y., Ohga, T., Wada, M., et al. (1995) Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide. Cancer Res. 55, 4293–4296.
Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J., and Taketo, M. (1996) Early embryonic lethality by targeted disruption of the mouse thioredoxin gene. Dev. Biol. 178, 179–185.
Qin, J., Clore, G. M., Kennedy, W. M. P., Huth, J. R., and Gronenborn, A. M. (1995) Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFкB. Structure 3, 289–297.
Matthews, J. R., Wakasugi, N., Virelizer, J.-L., Yodoi, J., and Hay, R. T. (1992) Thioredoxin regulates the DNA binding activity of NF-кB by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res. 20, 3821–3830.
Tagaya, Y., Wakasugi, H., Masutani, H., Nakamura, H., Iwata, S., Mitsui, A., et al. (1990) Role of ATL-derived factor (ADF) in the normal and abnormal cellular activation: involvement of dithiol related reduction. Mol. Immunol. 27, 1279–1289.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Humana Press Inc.
About this protocol
Cite this protocol
Makino, Y., Okamoto, K., Tanaka, H. (2002). Thioredoxin and Redox Regulation of the Nuclear Receptor. In: Armstrong, D. (eds) Oxidants and Antioxidants. Methods in Molecular Biology™, vol 196. Humana Press. https://doi.org/10.1385/1-59259-274-0:171
Download citation
DOI: https://doi.org/10.1385/1-59259-274-0:171
Publisher Name: Humana Press
Print ISBN: 978-0-89603-851-6
Online ISBN: 978-1-59259-274-6
eBook Packages: Springer Protocols