The thioredoxin antioxidant system.
From selenium to selenoproteins: synthesis, identity, and their role in human health.
The function of most selenoproteins is currently unknown; however, thioredoxin reductases, glutathione peroxidases and thyroid hormone deiodinases are well characterised selenobroteins involved in redox regulation of intracellular signalling, redox homeostasis and thyroid hormones metabolism.
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.
- A. Holmgren
- Biology, ChemistryJournal of Biological Chemistry
- 10 October 1979
The fast spontaneous reaction between dihydrolipoamide and thioredoxin-S2 provides a mechanism for NADH or pyruvate-dependent disulfides reduction and the implication of the dithiol-disulfide oxidoreductase activity of thiOREDoxin for the regulation of enzyme activities by thiol oxidation-reduction control is discussed.
Thioredoxin and thioredoxin reductase.
Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.
Glutaredoxins uniquely reduce mixed disulfides with glutathione via a monothiol mechanism where only an N-terminal low pKa Cys residue is required, by using their glutathionylation site.
Thioredoxin and related molecules--from biology to health and disease.
Thioredoxin and binding proteins appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis and the fundamental differences between bacterial and mammalian thiOREDoxin reductases offer new principles for treatment of infections.
The thioredoxin system in cancer.
Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis.
Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors.
- J. Ungerstedt, Y. Sowa, P. Marks
- BiologyProceedings of the National Academy of Sciences…
- 18 January 2005
It is found that the HDACi suberoylanilide hydroxamic acid (SAHA) and MS-275, a benzamide, cause an accumulation of reactive oxygen species (ROS) and caspase activation in transformed but not normal cells.
Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.
- C. Lillig, C. Berndt, A. Holmgren
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 7 June 2005
It is proposed that the iron-sulfur cluster serves as a redox sensor for the activation of Grx2 during conditions of oxidative stress when free radicals are formed and the glutathione pool becomes oxidized.