Thioredoxin redox regulation

In 1986, the antioxidant effects of thioredoxin reductase were studied by Schallreuter et al. [81]. It has been shown that thioredoxin reductase was contained in the plasma membrane surface of human keratinocytes where it provided skin protection against free radical mediated damage. Later on, the reductive activity of Trx/thioredoxin reductase system has been shown for the reduction of ascorbyl radical to ascorbate [82], the redox regulation of NFkB factor [83], and in the regulation of nitric oxide-nitric oxide synthase activities [84,85],... 

Nikitovic, D., Holmgren, A., S-Nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide,/. Biol. Chem. 27 (1996),... 

Fig. 7.4 Reactions associated with the thioredoxin system. Thioredoxin is a redox-regulating protein with a redox-active disulfide/dithiol within the conserved active site sequence -Cys-Gly-pro-Cys-. Thioredoxin reductase, a 55 kDa flavoprotein that catalyzes the NADPH-dependent reduction of thioredoxin (1) and thioredoxin oxidase (2), a flavin-dependent sulfhydry 1 oxidase that catalyzes the oxidative protein folding with the generation of disulfides...

Kondo, N., Nakamura, H., Masutani, H., and Yodoi, 1. 2006. Redox regulation of human thioredoxin network. Antioxid. Redox Signal. 8 1881-1890. 

Nimata, M., Kishimito, C., Shioji, K., Ishizaki, K., Kitaguchi, S., Hashimoto, T., Nagata, N., and Kawai, C. 2003. Upregulation of redox-regulating protein, thioredoxin, in endomyocardial biopsy samples of patients with myocarditis and cardiomyopathies. Mol. Cell. Biochem. 248 193-196. 

T. Okamoto and T. Tetsuko, Rore of thioredoxine in the redox regulation of gene expression in inmfammatory diseases. In P.G. Winyard, D.R. Blake, and C.H. Evans (eds.). Free Radicals and Inflammation, Birkhauser, Basel, Boston, Berlin, 1998, pp. 119-132. 

Kim YC, Yamaguchi Y, Kondo N, Masutani H, Yodoi J (2003) Thioredoxin-dependent redox regulation of the antioxidant responsive element (ARE) in electrophile response. Oncogene 22 1860-1865... 

Lindahl, M. and Kieselbach, T. (2009) Disulphide proteomes and interactions with thioredoxin on the track towards understanding redox regulation in chloroplasts and cyanobacteria. J. Proteomics, 72 (3), 416-438. 

NF-kB inhibition. Aqueous extract of mainstream smoke (smoke-bubbled phosphate-buffered saline), in Swiss 3T3 cells, decreased DNA binding of NF-kB during the first 2 hours of exposure and increased more than twofold over controls after 4-6 hours of exposure. There was lack of phosphorylation and degradation of iKB-a and a significant increase in thioredoxin reductase mRNA after 2-6 hours of exposure. Results indicated that the activity of NF-kB in smoke-treated cells was subject mainly to a redox-controlled mechanism dependent on the availability of reduced thioredoxin rather than being controlled by its normal regulator, iKB-a " ". 

Das, D.K. 2004. Thioredoxin regulation of ischemic preconditioning. Antioxid. Redox Signal. 6 405-412. 

In 1996, Tamura and Stadtman showed that thioredoxin reductase from mammalia-in contrast to the bacterial homologs-is a selenoprotein, and that selenocysteine is the penultimate C-terminal amino acid residue. Selenium-containing isoenzymes, which are tissue specific, have later on been characterized biochemically, or the existence of such isoforms was suggested by in-sihco methods. The substrate of thioredoxin reductase is thioredoxin, which is the key regulator of the redox status within cells. Thioredoxin catalyzes thiol-disulfide exchange reactions in proteins and peptides it is involved as redox mediator in the... 

One possibihty for minimizing oxidized protein damage is the thiol repair (Fig. 3). This repair system requires either glutathione or the thioredoxin system. The thioredoxin/thioredoxin reductase repair system [10] is able to reduce disulfide bonds. It can dethiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells. Thioredoxin is a smaU ubiquitous protein that contains a pair of cysteines that undergo reversible oxidation and are re-reduced by the enzyme thioredoxine reductase. The thioredoxin reductase transfers electrons from NADPH to thioredoxin via a flavin. 

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