The thioredoxin antioxidant system.

  title={The thioredoxin antioxidant system.},
  author={Jun Lu and Arne Holmgren},
  journal={Free radical biology \& medicine},

Thioredoxin and glutaredoxin systems under oxidative and nitrosative stress

This study highlighted the importance of the structural cysteines in human Trx1 and provided a potential rational design of new anticancer agents and characterized Grxs as S-denitrosylases catalyzing the reversible S-nitrosylation.

The Thioredoxin System of Mammalian Cells and Its Modulators

The Trx/TrxR system has been used as a target to treat cancer through the thiol–disulfide exchange reaction mechanism that results in the reduction of a wide range of target proteins and the generation of oxidized Trx.

Modulation of thiol-dependent redox system by metal ions via thioredoxin and glutaredoxin systems.

Results demonstrate that metal ions are major players in regulating the Trx and Grx systems-mediated cellular redox processes and thus, provide an opportunity to understand the functions of metal ions in thiol metabolism dysfunction-related diseases.

Redox Signaling Mediated by Thioredoxin and Glutathione Systems in the Central Nervous System.

This review focuses on how ROS/RNS are produced and mediate signaling in CNS and how Trx and GSH systems regulate redox signaling by catalyzing reversible thiol modifications, and the effects of certain small molecules that target thiol-based signaling pathways in the CNS.

Characterization of the thioredoxin system in Methanosarcina mazei

This thesis research concerns the thioredoxin system of the late evolving members of the group which are exposed to oxygen more frequently than the deeply rooted members ofThe group, and have several Trxs and TrxRs.

Glutathione-dependent thioredoxin reduction and lipoamide system support in-vitro mammalian ribonucleotide reductase catalysis: a possible antioxidant redundancy

It is concluded that GSH-mediated Trx reduction and LAM systems support basal level R NR activity in vitro; in absence of TrxR and complete redoxin systems respectively and hypothesize that potential redundancy between the various antioxidant systems might synergize in sustaining RNR activity.

Characterization of thioredoxin related protein of 14 kDa and its role in redox signaling

It is demonstrated that the Trx system, including both Trx1 and TRP14, impacts the oxidation of specific PTPs and can thereby modulate PDGF signaling, which reinforces the notion that TrxR1-dependent pathways are not only mediated via its wellknown substrate TrX1.

Thioredoxin system in cell death progression.

This work focuses on the research progress that is involved in the regulation of apoptosis by Trx systems, and proposes some useful principles to understand the reaction mechanism of the TrxR inhibition by these compounds.

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.

The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae*

Intriguingly cells lacking GLR1 encoding the GSSG reductase in S. cerevisiae accumulated increased levels of GSH via a mechanism independent of the GSH biosynthetic pathway, and purified thioredoxins can reduce G SSG to GSH in the presence ofThioredoxin reduct enzyme and NADPH in a reconstituted in vitro system.

Glutathione and Glutaredoxin Act as a Backup of Human Thioredoxin Reductase 1 to Reduce Thioredoxin 1 Preventing Cell Death by Aurothioglucose*

The glutaredoxin system and glutathione have a backup role to keep Trx1 reduced in cells with loss of TrxR1 activity, and this work demonstrated the critical role of the thioredoxin redox state in cell survival and a new role of glutATHione.

The thioredoxin system in retroviral infection and apoptosis

Thioredoxin binding protein-2/vitamin D3 upregulated protein 1 is a growth suppressor and its expression is suppressed in HTLV-I-transformed cells.

Antioxidant function of thioredoxin and glutaredoxin systems.

  • A. Holmgren
  • Biology, Chemistry
    Antioxidants & redox signaling
  • 2000
Results show that selenium is essential for the activity of thioredoxin reductase, explaining why this trace element is required for cell proliferation by effects on thiOREDoxin-dependent control of the intracellular redox state, ribonucleotide reduct enzyme production of deoxyribonucleotides, or activation of transcription factors.

Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3*

It is shown that the mitochondrial 2-Cys peroxiredoxin (Prx3) is not only substrate for thioredoxin 2 (Trx2), but can also be reduced by glutaredoxin 2

Thioredoxin-dependent peroxide reductase from yeast.