Thioredoxin is a critical protein that mediates the transfer of reducing equivalents in vivo and regulates redox sensitive enzymes in several cases. In addition, thioredoxin provides reducing equivalents to oxidoreductases such as peroxiredoxin. Through a dithiol-disulfide exchange reaction, the reduced form of thioredoxin preferentially interacts with the oxidized forms of targets, which are i...

Berndt C, Lillig CH, Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 292: H1227–H1236, 2007. First published December 15, 2006; doi:10.1152/ajpheart.01162.2006.—Reactive oxygen species (ROS) and the cellular thiol redox state are crucial mediators of multiple cell processes li...

Homogeneous preparations of thioredoxin-linked fructose-l,6-bisphosphatase and sedoheptulose-l,7-bisphosphatase were prepared from leaves of corn (Zea mays), a classical C4 plant. Fructose-1,6-bisphosphatase had a molecular weight of 184,000 and consisted of four apparently identical subunits of M, = 46,000. Sedoheptulose-1,7-bisphosphatase, by contrast, was composed of two identical subunits o...

Selenium participates in the antioxidant defense mainly through a class of selenoproteins, including thioredoxin reductase. Epigallocatechin-3-gallate (EGCG) is the most abundant and biologically active catechin in green tea. Depending upon the dose and biological systems, EGCG may function either as an antioxidant or as an inducer of antioxidant defense via its pro-oxidant action or other unid...

Understanding how pathogenic fungi adapt to host plant cells is of major concern to securing global food production. The hemibiotrophic rice blast fungus Magnaporthe oryzae, cause of the most serious disease of cultivated rice, colonizes leaf cells asymptomatically as a biotroph for 4-5 days in susceptible rice cultivars before entering its destructive necrotrophic phase. During the biotrophic ...

We tested the hypothesis that oxidant-injured cells upregulate thioredoxin, whereas oxidant-stressed, but not injured, cells upregulate interleukin (IL)-8 after injury. We exposed primary human tracheobronchial epithelial cells and transformed human bronchial epithelial cells (BEAS-2B S.6) to 0, 200, 400, or 600 microM H(2)O(2) for 1 h followed by an additional 7 h of incubation. Subsequently, ...

The classic function for thioredoxin is to act as a hydrogen donor for the enzyme ribonucleotide reductase, which is essential for DNA synthesis. In addition, thioredoxin participates in the regulation of different metabolic processes via thiol redox control. These kind of processes involve changes in the activity of different enzymes, receptors or transcription factors via dithiol/disulphide i...

Thioredoxins are 12-kDa proteins functional in the regulation of cellular processes throughout the animal, plant, and microbial kingdoms. Growing evidence with seeds suggests that an h-type of thioredoxin, reduced by NADPH via NADP-thioredoxin reductase, reduces disulfide bonds of target proteins and thereby acts as a wakeup call in germination. A better understanding of the role of thioredoxin...

Figure 1: Models of thioredoxin‐interacting protein action: (a) Role of thioredoxin‐interacting protein in the thioredoxin system. Thioredoxin‐interacting protein binds and inhibits the reduced form of thioredoxin, thereby functioning as a rheostat that modulates both redox status and reactive oxygen species‐mediated signaling to regulate metabolism and other cellular processes. (b) Proposed ro...

Partial purification of a thioredoxin system from Novikoff ascites hepatoma cells has been previously reported (MOORE, E. C. (1967) Biochem. Biophys. Res. Commun. 29, 264-268). Thioredoxin from the same mammalian source has now been purified to electrophoretic homogeneity by ammonium sulfate fractionation, heat treatment, DEAE-cellulose chromatography, and Sephadex chromatography. 1-Dimethylami...