High impact information on PRDX5

• Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence [1].
• The immunostimulatory dinitrohalobenzene compound 1-chloro-2, 4-dinitrobenzene (DNCB) irreversibly inhibits mammalian thioredoxin reductase (TrxR) in the presence of NADPH, inducing an NADPH oxidase activity in the modified enzyme (Arnér, E. S. J., Björnstedt, M., and Holmgren, A. (1995) J. Biol. Chem. 270, 3479-3482) [2].
• Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue [2].
• Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction [3].
• The work reported here used an NADPH-coupled assay with thioredoxin reductase to show that reduced thioredoxin at micromolar concentrations is also an effective sulfur-acceptor substrate for rhodanese under conditions where millimolar concentrations of lipoate or dithiothreitol would be required [4].

Biological context of PRDX5

• The thioredoxin/thioredoxin reductase system has been studied as regenerative machinery for proteins inactivated by oxidative stress in vitro and in cultured endothelial cells [5].

Anatomical context of PRDX5

• The inhibition of thioredoxin reductase activity by 13-cis-retinoic acid resulted in a decrease in the regeneration of glyceraldehyde-3-phosphate dehydrogenase in the H2O2-treated endothelial cells [5].

Associations of PRDX5 with chemical compounds

• Bovine thioredoxin reductase, together with NADPH, could replace GSH [6].
• In the presence of purified bovine liver thioredoxin reductase, homogeneous bovine liver thioredoxin failed to reduce DHA to ascorbic acid as measured by NADPH oxidation [7].
• Reduction of the two active-site disulfides in PDI by NADPH and bovine thioredoxin reductase was not reversible by addition of excess NADP+, consistent with a redox potential (E0') above -200 mV [8].
• Se's ability to control cellular oxidative state through its incorporation into selenoproteins such as thioredoxin reductase (TrxR) may explain previous studies that connect Se status to tumor angiogenesis [9].
• Under the same conditions, intracellular AA was oxidized when cell monolayers were treated with 1,3-bis(2-Chloroethyl)-1-nitrosourea (BCNU), an inhibitor of glutathione reductase and thioredoxin reductase [10].

Other interactions of PRDX5

• PRDX1 and PRDX5 transcripts were detected throughout development [11].

References