Background: Thioredoxins ("TRX") are ubiquitous 12-kDa oxidoreductase enzyme containing a dithiol-disulfide active site facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. When thioredoxin levels are elevated there is increased cell growth and resistance to the normal mechanism of programmed cell death. An increase in thioredoxin levels seen in many human primary ...

Thioredoxin (Trx) is an oxidoreductase with important physiological function. Imbalances in the NADPH/thioredoxin reductase/thioredoxin system are associated with a number of pathologies, particularly cancer, and a number of clinical trials for thioredoxin and thioredoxin reductase inhibitors have been carried out or are underway. Due to the emerging role and importance of oxidoreductases for h...

COMMENTARY Correction for “Mitochondrial metabolism is regulated by thioredoxin,” by Ian Max Møller, which appeared in issue 11, March 17, 2015, of Proc Natl Acad Sci USA (112:3180–3181; first published March 9, 2015; 10.1073/pnas.1502425112). The authors note that on page 3181, left column, second full paragraph, line 14, “thioredoxin reductase using NADPH” should instead appear as “ferredoxin...

Chloroplast-free mutant cells C-2A ' of the green algae Scenedesmus obliquus lack thioredoxin / , which functions in the light activation of chloroplast enzymes, but do con­ tain the regular thioredoxins I and II. When dark-grown algae are transferred to light, thioredoxin / activity appears rapidly and increases in parallel with photosynthetic ac­ tivities; however it precedes chlorophyll bios...

The presence of thioredoxin was demonstrated in 20 strains of cyanobacteria as well as in one phototrophic bacterium Rhodopseudomonas sulfidophila and in Thiobacillus denitrificans. Thioredoxin activity was not found in Cyanophora paradoxa and in Porphyridium cruentum using the thioredoxin-dependent PAPS-sulfotransferase activity from Synechococcus 6301 as assay system.

The thioredoxin and glutathione systems play a central role in thiol-disulfide redox homeostasis in many organisms by providing electrons to essential enzymes, and defence against oxidative stress. These systems have recently been characterized in platyhelminth parasites, and the emerging biochemical scenario is the existence of linked processes with the enzyme thioredoxin glutathione reductase...

BACKGROUND Exacerbations of chronic obstructive pulmonary disease (COPD) are characterized by acute enhancement of airway neutrophilic inflammation under oxidative stress and can be involved in emphysema progression. However, pharmacotherapy against the neutrophilic inflammation and emphysema progression associated with exacerbation has not been established. Thioredoxin-1 has anti-oxidative and...

BACKGROUND Acute lung injury (ALI) and its extreme manifestation the acute respiratory distress syndrome (ARDS) complicate a wide variety of serious medical and surgical conditions. Thioredoxin is a small ubiquitous thiol protein with redox/inflammation modulatory properties relevant to the pathogenesis of ALI. We therefore investigated whether thioredoxin is raised extracellulary in patients w...

Stimulation of target gene transcription by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. LexA/p53 fusion proteins were used to study the basis for thioredoxin reductase dependence. A fusion protein containing all 393 of the residues of p53 efficiently and specifically stimulated transcription of a LexOP-LacZ reporter gene in wild-type yeast but w...