PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27130146-2 2016 Inhibition of purified thioredoxin reductase (TrxR) is observed with 1 and 2 only after their enzymatic oxidation by the hydrogen peroxide/horseradish peroxidase (H2O2/HRP) system with IC50 of 2.4 and 1.2muM respectively. Hydrogen Peroxide 163-167 thioredoxin Homo sapiens 23-34 27350002-7 2016 Moreover, with H2O2, significant oxidative shifts were observed only in redox active proteins, like PRDX2, peroxiredoxin 1 (PRDX1), TXN, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Hydrogen Peroxide 15-19 thioredoxin Homo sapiens 132-135 25701705-5 2015 Using recombinant enzymes and isolated permeabilized cardiac mitochondria, we show that two normally antioxidant matrix NADPH reductases, glutathione reductase and thioredoxin reductase, generate H2O2 by leaking electrons from their reduced flavoprotein to O2 when electron flow is impaired by inhibitors or because of limited availability of their natural electron acceptors, GSSG and oxidized thioredoxin. Hydrogen Peroxide 196-200 thioredoxin Homo sapiens 164-175 26813660-2 2016 Although the thioredoxin peroxidase activity of peroxiredoxin (Prx) is important to maintain low levels of endogenous hydrogen peroxide, Prx have also been shown to promote hydrogen peroxide-mediated signalling. Hydrogen Peroxide 118-135 thioredoxin Homo sapiens 13-24 26813662-0 2016 The Roles of Peroxiredoxin and Thioredoxin in Hydrogen Peroxide Sensing and in Signal Transduction. Hydrogen Peroxide 46-63 thioredoxin Homo sapiens 31-42 25701705-5 2015 Using recombinant enzymes and isolated permeabilized cardiac mitochondria, we show that two normally antioxidant matrix NADPH reductases, glutathione reductase and thioredoxin reductase, generate H2O2 by leaking electrons from their reduced flavoprotein to O2 when electron flow is impaired by inhibitors or because of limited availability of their natural electron acceptors, GSSG and oxidized thioredoxin. Hydrogen Peroxide 196-200 thioredoxin Homo sapiens 395-406 25735211-1 2015 BACKGROUND: Thioredoxin (Trx) family proteins are crucial mediators of cell functions via regulation of the thiol redox state of various key proteins and the levels of the intracellular second messenger hydrogen peroxide. Hydrogen Peroxide 203-220 thioredoxin Homo sapiens 25-28 25451645-10 2015 The integrated Prx-TrxR model simulations well describe the NADPH and H2O2 degradation dynamics and also show that the coupling of TrxR- and Prx-dependent reduction of H2O2 allowed ultrasensitive changes in the Trx concentration in response to changes in the TrxR concentration at high Prx concentrations. Hydrogen Peroxide 70-74 thioredoxin Homo sapiens 19-22 25724691-1 2015 The glutathione peroxidase homologs (GPxs) efficiently reduce hydroperoxides using electrons from glutathione (GSH), thioredoxin (Trx), or protein disulfide isomerase (PDI). Hydrogen Peroxide 62-76 thioredoxin Homo sapiens 117-128 25724691-1 2015 The glutathione peroxidase homologs (GPxs) efficiently reduce hydroperoxides using electrons from glutathione (GSH), thioredoxin (Trx), or protein disulfide isomerase (PDI). Hydrogen Peroxide 62-76 thioredoxin Homo sapiens 130-133 25451645-0 2015 Mechanistic characterization of the thioredoxin system in the removal of hydrogen peroxide. Hydrogen Peroxide 73-90 thioredoxin Homo sapiens 36-47 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 230-247 thioredoxin Homo sapiens 4-15 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 230-247 thioredoxin Homo sapiens 74-85 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 230-247 thioredoxin Homo sapiens 87-90 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 249-253 thioredoxin Homo sapiens 4-15 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 249-253 thioredoxin Homo sapiens 74-85 25451645-1 2015 The thioredoxin system, which consists of a family of proteins, including thioredoxin (Trx), peroxiredoxin (Prx), and thioredoxin reductase (TrxR), plays a critical role in the defense against oxidative stress by removing harmful hydrogen peroxide (H2O2). Hydrogen Peroxide 249-253 thioredoxin Homo sapiens 87-90 25451645-2 2015 Specifically, Trx donates electrons to Prx to remove H2O2 and then TrxR maintains the reduced Trx concentration with NADPH as the cofactor. Hydrogen Peroxide 53-57 thioredoxin Homo sapiens 14-17 25451645-3 2015 Despite a great deal of kinetic information gathered on the removal of H2O2 by the Trx system from various sources/species, a mechanistic understanding of the associated enzymes is still not available. Hydrogen Peroxide 71-75 thioredoxin Homo sapiens 83-86 25735211-1 2015 BACKGROUND: Thioredoxin (Trx) family proteins are crucial mediators of cell functions via regulation of the thiol redox state of various key proteins and the levels of the intracellular second messenger hydrogen peroxide. Hydrogen Peroxide 203-220 thioredoxin Homo sapiens 12-23 25451645-10 2015 The integrated Prx-TrxR model simulations well describe the NADPH and H2O2 degradation dynamics and also show that the coupling of TrxR- and Prx-dependent reduction of H2O2 allowed ultrasensitive changes in the Trx concentration in response to changes in the TrxR concentration at high Prx concentrations. Hydrogen Peroxide 168-172 thioredoxin Homo sapiens 19-22 23606690-4 2013 Nasal epithelial cells (5x10(5) cells/ml) obtained from five patients were stimulated with 50 muM H2O2 in the presence of different concentrations of macrolide antibiotics for 24 h. TRX levels in culture supernatants were examined by enzyme-linked immunosorbent assay. Hydrogen Peroxide 98-102 thioredoxin Homo sapiens 182-185 26461315-5 2014 We then applied it to analyze the behavior of Prx2 and Trx under the H2O2 exposure dynamics that erythrocytes face in circulation. Hydrogen Peroxide 69-73 thioredoxin Homo sapiens 55-58 26461315-7 2014 Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter. Hydrogen Peroxide 210-214 thioredoxin Homo sapiens 152-155 26461315-8 2014 This is desirable for analogic signal transduction and allows the Prx2/Trx/TrxR system to reliably transduce changes in H2O2 supply as changes in thiol oxidation. Hydrogen Peroxide 120-124 thioredoxin Homo sapiens 71-74 24952139-8 2014 Simulations of the responses to physiological H2O2 stimuli highlight that a design combining abundant Prx2 with a low effective peroxidase activity spares NADPH while improving potential signaling properties of the Prx2/thioredoxin/thioredoxin reductase system. Hydrogen Peroxide 46-50 thioredoxin Homo sapiens 220-231 24316080-0 2013 Dissection of a redox relay: H2O2-dependent activation of the transcription factor Pap1 through the peroxidatic Tpx1-thioredoxin cycle. Hydrogen Peroxide 29-33 thioredoxin Homo sapiens 117-128 24316080-6 2013 Recycling of Tpx1 by Trx1 is required for the efficient signaling to Pap1, suggesting that the complete cycle of H2O2 scavenging by Tpx1 and further recycling of oxidized Tpx1 by Trx1 is required for full downstream activation of the redox cascade. Hydrogen Peroxide 113-117 thioredoxin Homo sapiens 21-25 24316080-6 2013 Recycling of Tpx1 by Trx1 is required for the efficient signaling to Pap1, suggesting that the complete cycle of H2O2 scavenging by Tpx1 and further recycling of oxidized Tpx1 by Trx1 is required for full downstream activation of the redox cascade. Hydrogen Peroxide 113-117 thioredoxin Homo sapiens 179-183 25350977-7 2014 In cultured human proximal tubular epithelial cells, hydrogen peroxide specifically and dose dependently increased TRX1 levels in the culture supernatant, while reducing intracellular levels. Hydrogen Peroxide 53-70 thioredoxin Homo sapiens 115-119 26461388-6 2014 Here we examine the design requirements for the Peroxiredoxin/Thioredoxin/Thioredoxin-Reductase/Protein-Dithiol System (PTTRDS) to effectively integrate H2O2 signaling and anticipatory blocking of protein dithiols as disulfides, and we compared them to the designs found in cells. Hydrogen Peroxide 153-157 thioredoxin Homo sapiens 62-73 25093297-1 2014 Peroxiredoxin 3 (Prx3) is a mitochondrial member of the antioxidant family of thioredoxin peroxidases that uses mitochondrial thioredoxin 2 as a source of reducing equivalents to scavenge hydrogen peroxide (H2O2). Hydrogen Peroxide 188-205 thioredoxin Homo sapiens 78-89 25093297-1 2014 Peroxiredoxin 3 (Prx3) is a mitochondrial member of the antioxidant family of thioredoxin peroxidases that uses mitochondrial thioredoxin 2 as a source of reducing equivalents to scavenge hydrogen peroxide (H2O2). Hydrogen Peroxide 188-205 thioredoxin Homo sapiens 126-137 25093297-1 2014 Peroxiredoxin 3 (Prx3) is a mitochondrial member of the antioxidant family of thioredoxin peroxidases that uses mitochondrial thioredoxin 2 as a source of reducing equivalents to scavenge hydrogen peroxide (H2O2). Hydrogen Peroxide 207-211 thioredoxin Homo sapiens 78-89 25093297-1 2014 Peroxiredoxin 3 (Prx3) is a mitochondrial member of the antioxidant family of thioredoxin peroxidases that uses mitochondrial thioredoxin 2 as a source of reducing equivalents to scavenge hydrogen peroxide (H2O2). Hydrogen Peroxide 207-211 thioredoxin Homo sapiens 126-137 24722990-0 2014 Nicotinamide nucleotide transhydrogenase (Nnt) links the substrate requirement in brain mitochondria for hydrogen peroxide removal to the thioredoxin/peroxiredoxin (Trx/Prx) system. Hydrogen Peroxide 105-122 thioredoxin Homo sapiens 138-149 24722990-0 2014 Nicotinamide nucleotide transhydrogenase (Nnt) links the substrate requirement in brain mitochondria for hydrogen peroxide removal to the thioredoxin/peroxiredoxin (Trx/Prx) system. Hydrogen Peroxide 105-122 thioredoxin Homo sapiens 165-168 24722990-2 2014 Mitochondria are known to be net producers of ROS, but recently we have shown that brain mitochondria can consume mitochondrial hydrogen peroxide (H2O2) in a respiration-dependent manner predominantly by the thioredoxin/peroxiredoxin system. Hydrogen Peroxide 128-145 thioredoxin Homo sapiens 208-219 24722990-2 2014 Mitochondria are known to be net producers of ROS, but recently we have shown that brain mitochondria can consume mitochondrial hydrogen peroxide (H2O2) in a respiration-dependent manner predominantly by the thioredoxin/peroxiredoxin system. Hydrogen Peroxide 147-151 thioredoxin Homo sapiens 208-219 24722990-4 2014 We hypothesized that nicotinamide nucleotide transhydrogenase (Nnt), which utilizes the proton gradient to generate NADPH from NADH and NADP(+), provides the link between mitochondrial respiration and H2O2 detoxification through the thioredoxin/peroxiredoxin system. Hydrogen Peroxide 201-205 thioredoxin Homo sapiens 233-244 24103200-10 2014 Kinetic analysis demonstrated that the reduction of H2O2 by TrxR or Trx system were enhanced by 100 or 200 muM ABX. Hydrogen Peroxide 52-56 thioredoxin Homo sapiens 60-63 24062305-6 2013 In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. Hydrogen Peroxide 130-134 thioredoxin Homo sapiens 40-44 24062305-6 2013 In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. Hydrogen Peroxide 130-134 thioredoxin Homo sapiens 77-81 23466753-7 2013 Thioredoxin modulates the expression of estrogen responsive genes through modulating the production of H2O2 in breast cancer cells. Hydrogen Peroxide 103-107 thioredoxin Homo sapiens 0-11 23676086-2 2013 MtTrxR is a promising drug target because it dominates the Trx-dependent hydroperoxide metabolism and the reduction of ribonucleotides, thus facilitating survival and proliferation of M. tuberculosis. Hydrogen Peroxide 73-86 thioredoxin Homo sapiens 2-5 23244515-7 2013 Central to redox signaling processes are the glutathione and thioredoxin systems controlling H(2)O(2) levels and, hence, the thiol/disulfide balance. Hydrogen Peroxide 93-101 thioredoxin Homo sapiens 61-72 23606690-6 2013 The addition of clarithromycin (CAM) to cell cultures caused an increase in the ability of cells to produce TRX in response to H2O2 stimulation, and the minimum concentration that caused a significant increase was 0.5 mug/ml. Hydrogen Peroxide 127-131 thioredoxin Homo sapiens 108-111 22342995-4 2012 Consistent with these observations, the apoptotic pathway activated upon H2O2 treatment relies upon Trx1 oxidation, and is mediated by the p38(MAPK)/p53 signaling axis. Hydrogen Peroxide 73-77 thioredoxin Homo sapiens 100-104 23443157-5 2013 Probuco1 is capable of antagonizing the H2O2-induced apoptosis in VSMCs, which may be related to the decrease in ASK-1 protein expression and the increase in Trx-1 protein expression. Hydrogen Peroxide 40-44 thioredoxin Homo sapiens 158-163 23519408-2 2013 Various stress stimuli such as high glucose, heat shock, UV, H2O2 and mechanical stress among others robustly induce the expression of TXNIP, resulting in the sequestration and inactivation of thioredoxin, which in turn leads to cellular oxidative stress. Hydrogen Peroxide 61-65 thioredoxin Homo sapiens 193-204 23283135-8 2013 In HK-2 cells, HSA-Trx decreased the level of reactive oxygen species induced by hydrogen peroxide, and subsequently improved cell viability. Hydrogen Peroxide 81-98 thioredoxin Homo sapiens 19-22 23088625-6 2012 The oxidation of Cys-free MRPs by hydrogen peroxide could be conveniently monitored by SDS-PAGE and was specific for Met, as evidenced by quantitative reduction of these proteins with Msrs in DTT- and thioredoxin-dependent assays. Hydrogen Peroxide 34-51 thioredoxin Homo sapiens 201-212 22148505-7 2012 Within 5 min of exposure to hydrogen peroxide, a single disulfide bond formed between C65 and C138 followed by the formation of three additional disulfide bonds within 15 min; 10 total disulfide bonds formed within 1 h. A single mixed-disulfide bond involving C99 of APE1 was observed for the reaction of oxidized APE1 with thioredoxin (TRX). Hydrogen Peroxide 28-45 thioredoxin Homo sapiens 324-335 22148505-7 2012 Within 5 min of exposure to hydrogen peroxide, a single disulfide bond formed between C65 and C138 followed by the formation of three additional disulfide bonds within 15 min; 10 total disulfide bonds formed within 1 h. A single mixed-disulfide bond involving C99 of APE1 was observed for the reaction of oxidized APE1 with thioredoxin (TRX). Hydrogen Peroxide 28-45 thioredoxin Homo sapiens 337-340 21212402-9 2011 Prolonged incubation with H(2)O(2) induced stress fiber formation, reduced Trx-1 protein levels, and increased apoptosis. Hydrogen Peroxide 26-34 thioredoxin Homo sapiens 75-80 20121341-2 2010 We introduce a network model of H(2)O(2) clearance that includes the pseudo-enzymatic oxidative turnover of protein thiols, the enzymatic actions of catalase, glutathione peroxidase, peroxiredoxin, and glutaredoxin, and the redox reactions of thioredoxin and glutathione. Hydrogen Peroxide 32-40 thioredoxin Homo sapiens 243-254 20121341-4 2010 The model correctly predicted early oxidation profiles for the glutathione and thioredoxin redox couples across a range of initial extracellular [H(2)O(2)] and highlights the importance of cytoplasmic membrane permeability to the cellular defense against exogenous sources of H(2)O(2). Hydrogen Peroxide 146-154 thioredoxin Homo sapiens 79-90 20121341-4 2010 The model correctly predicted early oxidation profiles for the glutathione and thioredoxin redox couples across a range of initial extracellular [H(2)O(2)] and highlights the importance of cytoplasmic membrane permeability to the cellular defense against exogenous sources of H(2)O(2). Hydrogen Peroxide 276-284 thioredoxin Homo sapiens 79-90 20513473-2 2010 Hydrogen peroxide, peroxynitrite, or lipid hydroperoxides are all able to oxidize cysteines to form cysteine sulfenic acids; this reactive intermediate can be directly reduced to thiol by cellular reductants such as thioredoxin or further participate in disulfide bond formation with glutathione or cysteine residues in the same or another protein. Hydrogen Peroxide 0-17 thioredoxin Homo sapiens 216-227 20306235-16 2010 Recent evidence suggests selenoprotein W and the six other small thioredoxin-like mammalian selenoproteins may serve to transduce hydrogen peroxide signals into regulatory disulfide bonds in specific target proteins. Hydrogen Peroxide 130-147 thioredoxin Homo sapiens 65-76 20494123-4 2010 The evolution of mammalian Trx system compared to its prokaryotic counterparts may be an adaptation to the use of hydrogen peroxide and nitric oxide in redox regulation and signal transduction. Hydrogen Peroxide 114-131 thioredoxin Homo sapiens 27-30 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Hydrogen Peroxide 210-224 thioredoxin Homo sapiens 4-15 20609905-5 2010 Thioredoxin couples with thioredoxin-dependent peroxidases (peroxiredoxin) to scavenge hydrogen peroxide. Hydrogen Peroxide 87-104 thioredoxin Homo sapiens 0-11 20609905-5 2010 Thioredoxin couples with thioredoxin-dependent peroxidases (peroxiredoxin) to scavenge hydrogen peroxide. Hydrogen Peroxide 87-104 thioredoxin Homo sapiens 25-36 19406206-6 2009 A selenazol drug like ebselen is a direct substrate for mammalian TrxR and dithiol Trx and ebselen selenol is readily reoxidized by hydrogen peroxide and lipid hydroperoxides, acting as an anti-oxidant and anti-inflammatory drug. Hydrogen Peroxide 132-149 thioredoxin Homo sapiens 66-69 20357934-5 2009 These NMDA receptor-dependent effects are mediated in part by a coordinated program of gene expression changes centered on the thioredoxin-peroxiredoxin system, a thiol-based enzymatic system which is an important reducer of oxidative stressors such as hydroperoxides. Hydrogen Peroxide 253-267 thioredoxin Homo sapiens 127-138 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Hydrogen Peroxide 210-224 thioredoxin Homo sapiens 25-29 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Hydrogen Peroxide 226-230 thioredoxin Homo sapiens 4-15 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Hydrogen Peroxide 226-230 thioredoxin Homo sapiens 25-29 19216714-3 2008 NADPH-dependent thioredoxin reductase, which reduces a broad range of substrates including oxidized form of thioredoxin, can also directly reduce lipid hydroperoxides, H2O2, and dehydroascorbic and lipoic acids. Hydrogen Peroxide 168-172 thioredoxin Homo sapiens 16-27 19216714-3 2008 NADPH-dependent thioredoxin reductase, which reduces a broad range of substrates including oxidized form of thioredoxin, can also directly reduce lipid hydroperoxides, H2O2, and dehydroascorbic and lipoic acids. Hydrogen Peroxide 168-172 thioredoxin Homo sapiens 108-119 17823364-5 2007 METHODS AND RESULTS: First, we investigated the localization of Trx after H2O2 and NO. Hydrogen Peroxide 74-78 thioredoxin Homo sapiens 64-67 18315495-2 2008 Among the TRX superfamily is peroxiredoxin (PRX), a family of non-heme peroxidases that catalyzes the reduction of hydroperoxides into water and alcohol. Hydrogen Peroxide 115-129 thioredoxin Homo sapiens 10-13 18410747-7 2008 Unlike mammalian thioredoxins, both proteins were able to reduce oxidised glutathione and hydrogen peroxide. Hydrogen Peroxide 90-107 thioredoxin Homo sapiens 17-29 18164270-4 2008 Increased H2O2 triggers peroxiredoxin overoxidation to a sulphinic acid; however during apoptosis peroxiredoxin 3 was captured as a disulfide, suggesting impairment of the thioredoxin system responsible for maintaining peroxiredoxin 3 in its reduced form. Hydrogen Peroxide 10-14 thioredoxin Homo sapiens 172-183 17724081-6 2007 Trx inhibited this interaction of ASK1, which was, however, enhanced by expression of TRAF2 or TRAF6 or by treatment of cells with H2O2. Hydrogen Peroxide 131-135 thioredoxin Homo sapiens 0-3 17823364-9 2007 Trx(K81/82E) abolished the antiapoptotic capacity of H2O2. Hydrogen Peroxide 53-57 thioredoxin Homo sapiens 0-3 17823364-13 2007 CONCLUSION: H2O2-induced nuclear import of Trx depends on karyopherin-alpha and NO. Hydrogen Peroxide 12-16 thioredoxin Homo sapiens 43-46 17096689-0 2006 Hydroperoxide reduction by thioredoxin-specific glutathione peroxidase isoenzymes of Arabidopsis thaliana. Hydrogen Peroxide 0-13 thioredoxin Homo sapiens 27-38 17098255-4 2007 Like other CysGPxs with thioredoxin peroxidase activity, Drosophila melanogaster (Dm)GPx oxidized by H(2)O(2) contained an intra-molecular disulfide bridge between the active-site cysteine (C45; C(P)) and C91. Hydrogen Peroxide 101-109 thioredoxin Homo sapiens 24-35 17096689-3 2006 Interestingly, these recombinant proteins were able to reduce H2O2, cumene hydroperoxide, phosphatidylcholine and linoleic acid hydroperoxides using thioredoxin but not glutathione or NADPH as an electron donor. Hydrogen Peroxide 62-66 thioredoxin Homo sapiens 149-160 15474995-5 2004 Conversely, thioredoxin overexpression blocked hydrogen peroxide-induced TEM. Hydrogen Peroxide 47-64 thioredoxin Homo sapiens 12-23 16962936-5 2006 Moreover, ERp57 reduced by the thioredoxin-reductase/thioredoxin system stimulated the binding of AP-1 to its consensus sequence on DNA, and HeLa cells stably transfected and overexpressing ERp57 were protected against hydrogen peroxide-induced cell killing. Hydrogen Peroxide 219-236 thioredoxin Homo sapiens 31-42 16263712-0 2005 Cathepsin D and H2O2 stimulate degradation of thioredoxin-1: implication for endothelial cell apoptosis. Hydrogen Peroxide 16-20 thioredoxin Homo sapiens 46-59 16263712-12 2005 Incubation with 100 microm H2O2 for 6 h decreased Trx protein levels, whereas Trx mRNA was not altered. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 50-53 16263712-13 2005 H2O2-induced Trx degradation was inhibited by pepstatin A and genetic knock down of CatD but not by other protease inhibitors. Hydrogen Peroxide 0-4 thioredoxin Homo sapiens 13-16 16263712-16 2005 Moreover, H2O2 incubation led to a translocation of Trx to the lysosomes prior to the induction of apoptosis. Hydrogen Peroxide 10-14 thioredoxin Homo sapiens 52-55 16024017-3 2005 TRX-overexpression made HT-1080 cells resistant to an oxidative stress caused by H2O2 or paraquat. Hydrogen Peroxide 81-85 thioredoxin Homo sapiens 0-3 15917183-2 2005 This novel antioxidant enzyme was shown to reduce hydroperoxides and, more recently, peroxynitrite with the use of electrons provided by a physiological thiol like thioredoxin. Hydrogen Peroxide 50-64 thioredoxin Homo sapiens 164-175 15745966-9 2005 Pretreatment with GGA and overexpression of Trx in K-1034 cells counteracted H2O2 (50 microM)-induced attenuation of cellular latex bead incorporation. Hydrogen Peroxide 77-81 thioredoxin Homo sapiens 44-47 15556622-4 2004 Here, we show that 10 and 50 microM H2O2 and short-term exposure to shear stress significantly increased Trx-1 mRNA and protein levels in endothelial cells. Hydrogen Peroxide 36-40 thioredoxin Homo sapiens 105-110 15556622-7 2004 Reduction of Trx-1 expression using an antisense oligonucleotide approach resulted in the induction of apoptosis and abolished the inhibitory effect of low doses of H2O2. Hydrogen Peroxide 165-169 thioredoxin Homo sapiens 13-18 15979675-6 2005 The thioredoxin system dependence of ebselen to catalyze reduction of other oxidized species, such as hydrogen peroxide, dehydroascorbate, and peroxynitrite, is discussed. Hydrogen Peroxide 102-119 thioredoxin Homo sapiens 4-15 15818395-4 2005 A family of thioredoxin-dependent peroxidases (peroxiredoxins) protects against apoptosis by scavenging hydrogen peroxide. Hydrogen Peroxide 104-121 thioredoxin Homo sapiens 12-23 15685369-5 2005 In addition, Trx mRNA transcription was inhibited by H2O2 (300 microM), which could be reversed by the pre-administration of DHEA in various concentrations (0.1100 nM). Hydrogen Peroxide 53-57 thioredoxin Homo sapiens 13-16 15685369-6 2005 Western blot assay confirmed that protein level of Trx could be elevated by the pre-treatment of DHEA (10100 nM) with the exposure of H2O2. Hydrogen Peroxide 134-138 thioredoxin Homo sapiens 51-54 14976238-8 2004 Additional evidence that thioredoxin serves as a donor comes from the formation of heterodimers between peroxiredoxin Q and monocysteinic mutants of spinach (Spinacia oleracea) thioredoxin m. Peroxiredoxin Q can reduce various alkyl hydroperoxides, but with a better efficiency for cumene hydroperoxide than hydrogen peroxide and tertiary butyl hydroperoxide. Hydrogen Peroxide 308-325 thioredoxin Homo sapiens 25-36 15081538-3 2004 The stable Jurkat T cell line transfected with human TRX gene (TRX-transfectant) was highly resistant to hydrogen peroxide-induced apoptosis, but not the cell line transfected with vector (mock-transfectant). Hydrogen Peroxide 105-122 thioredoxin Homo sapiens 53-56 15081538-3 2004 The stable Jurkat T cell line transfected with human TRX gene (TRX-transfectant) was highly resistant to hydrogen peroxide-induced apoptosis, but not the cell line transfected with vector (mock-transfectant). Hydrogen Peroxide 105-122 thioredoxin Homo sapiens 63-66 14713340-1 2004 Ebselen is a selanazal drug recently revealed as a highly efficient peroxiredoxin mimic catalyzing the hydroperoxide reduction by the mammalian thioredoxin system [thioredoxin (Trx), thioredoxin reductase (TrxR), and NADPH]. Hydrogen Peroxide 103-116 thioredoxin Homo sapiens 144-155 14713340-1 2004 Ebselen is a selanazal drug recently revealed as a highly efficient peroxiredoxin mimic catalyzing the hydroperoxide reduction by the mammalian thioredoxin system [thioredoxin (Trx), thioredoxin reductase (TrxR), and NADPH]. Hydrogen Peroxide 103-116 thioredoxin Homo sapiens 164-175 14688353-2 2004 We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Hydrogen Peroxide 108-112 thioredoxin Homo sapiens 41-44 15133893-0 2004 [Changes of thioredoxin mRNA level in neurons with mitochondrial dysfunction insulted by H2O2]. Hydrogen Peroxide 89-93 thioredoxin Homo sapiens 12-23 15133893-4 2004 Furthermore, the changes of thioredoxin mRNA level in both normal and abnormal cultured neurons insulted by H2O2 were analyzed by semiquantitative RT-PCR in order to explore the role of Trx, an important redox regulatory protein, in modulating the process of neuronal injury. Hydrogen Peroxide 108-112 thioredoxin Homo sapiens 28-39 15133893-5 2004 It was found that mitochondrial dysfunctional neurons could be damaged by H2O2 in a dose- and time-dependent manner and the expression of Trx decreased during certain dose (0-200 mumol/L) and time (0-4 h) of H2O2 treatment. Hydrogen Peroxide 208-212 thioredoxin Homo sapiens 138-141 14688353-2 2004 We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Hydrogen Peroxide 153-157 thioredoxin Homo sapiens 41-44 14688353-2 2004 We show here that a redox-active site in TRX is essential for its release from T lymphocytes in response to H2O2 and extracellular TRX regulates its own H2O2-induced release. Hydrogen Peroxide 153-157 thioredoxin Homo sapiens 131-134 14688353-4 2004 The level of TRX release is augmented upon the addition of H2O2, but suppressed upon the addition of N-acetylcysteine. Hydrogen Peroxide 59-63 thioredoxin Homo sapiens 13-16 14688353-5 2004 In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. Hydrogen Peroxide 205-209 thioredoxin Homo sapiens 74-77 14688353-5 2004 In the culture supernatant of a Jurkat transfectant expressing the tagged TRX-wild type (WT), the tagged TRX protein is rapidly released at 1 h and kept at a constant level until 6 h after the addition of H2O2. Hydrogen Peroxide 205-209 thioredoxin Homo sapiens 105-108 14688353-7 2004 H2O2-induced release of TRX from the transfectant is inhibited by the presence of rTRX-WT in a dose-dependent manner. Hydrogen Peroxide 0-4 thioredoxin Homo sapiens 24-27 14688353-8 2004 Preincubation of the transfectant with rTRX-WT for 1 h at 37 degrees C, but not 0 degrees C, results in a significant suppression of the TRX release, reactive oxygen species, and caspase-3 activity induced by H2O2, respectively. Hydrogen Peroxide 209-213 thioredoxin Homo sapiens 40-43 12751784-3 2003 Trypanothione is a reductant of thioredoxin and tryparedoxin, small dithiol proteins, which in turn deliver reducing equivalents for the synthesis of deoxyribonucleotides as well as for the detoxification of hydroperoxides by different peroxidases. Hydrogen Peroxide 208-222 thioredoxin Homo sapiens 32-43 12882768-9 2003 In vivo oxidative stress of HLE B3 cells resulted in a 35% upregulation of the level of Trx1 protein after 10 minutes of H(2)O(2) treatment. Hydrogen Peroxide 121-129 thioredoxin Homo sapiens 88-92 12819637-7 2003 Addition of recombinant Trx to LDMN marrow cells cultured with H(2)O(2) and rhgammaIFN partially (although not completely) reversed inhibition of CFU-E colony formation. Hydrogen Peroxide 63-71 thioredoxin Homo sapiens 24-27 12099690-6 2002 The CP-pro alpha 1(1)/TRX interaction was increased by dithiothreitol treatment, but was markedly inhibited by hydrogen peroxide or diamide treatment. Hydrogen Peroxide 111-128 thioredoxin Homo sapiens 22-25 11920685-3 2002 Oxidative stress such as hydrogen peroxide (H2O2) disrupts the ASK1-thioredoxin complex by oxidization of thioredoxin and thereby activates ASK1. Hydrogen Peroxide 25-42 thioredoxin Homo sapiens 68-79 11916965-4 2002 The reduction of H(2)O(2)-oxidized PTEN in cells appears to be mediated predominantly by thioredoxin. Hydrogen Peroxide 17-25 thioredoxin Homo sapiens 89-100 11920685-3 2002 Oxidative stress such as hydrogen peroxide (H2O2) disrupts the ASK1-thioredoxin complex by oxidization of thioredoxin and thereby activates ASK1. Hydrogen Peroxide 25-42 thioredoxin Homo sapiens 106-117 11920685-3 2002 Oxidative stress such as hydrogen peroxide (H2O2) disrupts the ASK1-thioredoxin complex by oxidization of thioredoxin and thereby activates ASK1. Hydrogen Peroxide 44-48 thioredoxin Homo sapiens 68-79 11920685-3 2002 Oxidative stress such as hydrogen peroxide (H2O2) disrupts the ASK1-thioredoxin complex by oxidization of thioredoxin and thereby activates ASK1. Hydrogen Peroxide 44-48 thioredoxin Homo sapiens 106-117 11706208-5 2001 The Prx degrades hydrogen peroxide and alkyl hydroperoxides in the presence of an exogenous proton donor that can be either thioredoxin or glutaredoxin (Grx). Hydrogen Peroxide 17-34 thioredoxin Homo sapiens 124-135 11751890-5 2002 The reduced form of Trx suppresses the serum-free-induced hydroxyl radicals, lipid peroxidation, and apoptosis, indicating that H(2)O(2) is removed by Trx peroxidase. Hydrogen Peroxide 128-136 thioredoxin Homo sapiens 20-23 11751890-5 2002 The reduced form of Trx suppresses the serum-free-induced hydroxyl radicals, lipid peroxidation, and apoptosis, indicating that H(2)O(2) is removed by Trx peroxidase. Hydrogen Peroxide 128-136 thioredoxin Homo sapiens 151-154 11469800-5 2001 The results show that an increase in TrxP-1 expression contributes to the protection against H(2)O(2) induced apoptosis caused by Trx-1, but does not protect against apoptosis induced by other agents. Hydrogen Peroxide 93-101 thioredoxin Homo sapiens 130-135 11771746-1 2001 Human peroxiredoxin (Prx) play important roles in eliminating hydrogen peroxide generated during cellular mechanisms using electrons from thioredoxin (Trx). Hydrogen Peroxide 62-79 thioredoxin Homo sapiens 138-149 11469800-0 2001 Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin. Hydrogen Peroxide 154-171 thioredoxin Homo sapiens 59-72 11497302-1 2001 The peroxiredoxins (Prx) are a family of 25 kDa peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. Hydrogen Peroxide 76-80 thioredoxin Homo sapiens 104-115 11497302-1 2001 The peroxiredoxins (Prx) are a family of 25 kDa peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. Hydrogen Peroxide 76-80 thioredoxin Homo sapiens 117-120 11771746-1 2001 Human peroxiredoxin (Prx) play important roles in eliminating hydrogen peroxide generated during cellular mechanisms using electrons from thioredoxin (Trx). Hydrogen Peroxide 62-79 thioredoxin Homo sapiens 151-154 10554525-13 1999 Recent work demonstrates that thioredoxin rapidly enters the cell nucleus upon treatment of cells with H2O2, but little is known about the compartimentalization of the respiratory burst and the intracellular localization of antioxidant enzymes during that process. Hydrogen Peroxide 103-107 thioredoxin Homo sapiens 30-41 11012661-10 2000 In contrast, thioredoxin reductases of higher eukaryotes are larger (112-130 kDa), selenium-dependent dimeric flavoproteins with a broad substrate specificity that also reduce nondisulfide substrates such as hydroperoxides, vitamin C or selenite. Hydrogen Peroxide 208-222 thioredoxin Homo sapiens 13-24 10555039-9 1999 Stimulation of synovial fibroblast-like synoviocytes with either H2O2 or TNF alpha induced an increase in the production of TRX. Hydrogen Peroxide 65-69 thioredoxin Homo sapiens 124-127 10801974-8 2000 Mechanisms of TrxR in reduction of Trx and hydroperoxides have been postulated and are compatible with known enzyme activities and the effects of inhibitors, like goldthioglucose and 1-chloro-2,4-dinitrobenzene. Hydrogen Peroxide 43-57 thioredoxin Homo sapiens 14-17 10588361-1 1999 A peroxidase from yeast that reduces H2O2 with the use of electrons provided by thioredoxin (Trx) together with homologs from a wide variety of species constitute the peroxiredoxin (Prx) family of proteins. Hydrogen Peroxide 37-41 thioredoxin Homo sapiens 80-91 10588361-1 1999 A peroxidase from yeast that reduces H2O2 with the use of electrons provided by thioredoxin (Trx) together with homologs from a wide variety of species constitute the peroxiredoxin (Prx) family of proteins. Hydrogen Peroxide 37-41 thioredoxin Homo sapiens 93-96 10588361-6 1999 All three enzymes showed similar kinetic properties: the Vmax was 6-13 micromol/min per mg at 37 degrees C, the Km for Trx was 3-6 microM, and the Km for H2O2 was < 20 microM. Hydrogen Peroxide 154-158 thioredoxin Homo sapiens 119-122 9367644-4 1997 Thioredoxin expression was augmented in a dose-dependent manner when retinal pigment epithelial cells were pretreated with 10 nm-1 microm prostaglandin E1 1 hr before the exposure to hydrogen peroxide. Hydrogen Peroxide 183-200 thioredoxin Homo sapiens 0-11 9497357-2 1998 With the use of recombinant proteins Prx I, II, and III, all have now been shown to possess peroxidase activity and to rely on Trx as a source of reducing equivalents for the reduction of H2O2. Hydrogen Peroxide 188-192 thioredoxin Homo sapiens 127-130 9497358-1 1998 A new type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces H2O2 with the use of electrons from thioredoxin and contains two essential cysteines was recently identified. Hydrogen Peroxide 82-86 thioredoxin Homo sapiens 39-50 9388242-6 1997 Thioredoxin peroxidase is the immediate enzyme that links reduction of H2O2 to thioredoxin. Hydrogen Peroxide 71-75 thioredoxin Homo sapiens 0-11 9388242-6 1997 Thioredoxin peroxidase is the immediate enzyme that links reduction of H2O2 to thioredoxin. Hydrogen Peroxide 71-75 thioredoxin Homo sapiens 79-90 9388242-12 1997 AOE372 function suggests thioredoxin peroxidase as an immediate regulator of H2O2-mediated activation of NF-kappaB. Hydrogen Peroxide 77-81 thioredoxin Homo sapiens 25-36 10233914-8 1999 The enhanced H2O2 production by monocytes from asymptomatic untreated patients with CD4(+) cell counts above 500/microliter was associated with a decrease in the levels of Bcl-2 and thioredoxin. Hydrogen Peroxide 13-17 thioredoxin Homo sapiens 182-193 10074082-10 1999 When a small thiol such as dithiothreitol was added to the medium, the rate of H2O2 decomposition in the DeltakatG mutant increased more than 10-fold, indicating that a thiol-specific peroxidase, for which thioredoxin may be the physiological electron donor, is present. Hydrogen Peroxide 79-83 thioredoxin Homo sapiens 206-217 7744824-7 1995 Hydrogen peroxide and 15-HPETE were reduced at approximately the same rate by HP-TR, thioredoxin, and selenocystine. Hydrogen Peroxide 0-17 thioredoxin Homo sapiens 85-96 9321654-4 1997 Addition of H2O2 at low concentrations lowered levels of pS2 mRNA and also down-regulated ERE-CAT activity, which was recovered by transfection of thioredoxin (TRX) expression vector. Hydrogen Peroxide 12-16 thioredoxin Homo sapiens 147-158 9321654-4 1997 Addition of H2O2 at low concentrations lowered levels of pS2 mRNA and also down-regulated ERE-CAT activity, which was recovered by transfection of thioredoxin (TRX) expression vector. Hydrogen Peroxide 12-16 thioredoxin Homo sapiens 160-163 9315320-6 1997 Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione. Hydrogen Peroxide 267-281 thioredoxin Homo sapiens 107-110 8761470-7 1996 The effects of H2O2 in vitro were reversed by the sulphydryl reducing agent dithiothreitol and the endogenous reductor thioredoxin (TRX), while the effects of iodoacetic acid were irreversible. Hydrogen Peroxide 15-19 thioredoxin Homo sapiens 119-130 8761470-7 1996 The effects of H2O2 in vitro were reversed by the sulphydryl reducing agent dithiothreitol and the endogenous reductor thioredoxin (TRX), while the effects of iodoacetic acid were irreversible. Hydrogen Peroxide 15-19 thioredoxin Homo sapiens 132-135 8761470-8 1996 In addition, TRX also restored the DNA-binding activity of HSF oxidized in vivo, while it was found to be itself induced in vivo by both HS and H2O2. Hydrogen Peroxide 144-148 thioredoxin Homo sapiens 13-16 8759006-2 1996 We found that expression of the ADF/Trx gene was increased by oxidative agents such as hydrogen peroxide, diamide and menadione in Jurkat cells. Hydrogen Peroxide 87-104 thioredoxin Homo sapiens 32-35 8759006-2 1996 We found that expression of the ADF/Trx gene was increased by oxidative agents such as hydrogen peroxide, diamide and menadione in Jurkat cells. Hydrogen Peroxide 87-104 thioredoxin Homo sapiens 36-39 7671238-5 1995 These thioredoxin antisense transfectants showed increased sensitivity to cisplatin and also to other superoxide-generating agents, i.e., doxorubicin, mitomycin C, etoposide, and hydrogen peroxide, as well as to UV irradiation, but not to the tubulin-targeting agents, vincristine, and colchicine. Hydrogen Peroxide 179-196 thioredoxin Homo sapiens 6-17 9137526-8 1997 Though TRX-transfected A2780 cells showed 1.8-fold increased resistance to H2O2, resistance to adriamycin and mitomycin C, which generate oxygen radicals, was not observed in the transfectants. Hydrogen Peroxide 75-79 thioredoxin Homo sapiens 7-10 7797250-7 1995 ADF/TRX was also induced in a HTLV-1 (+) T-cell line, MT-1, by UVB or H2O2 dose dependently. Hydrogen Peroxide 70-74 thioredoxin Homo sapiens 0-3 7797250-7 1995 ADF/TRX was also induced in a HTLV-1 (+) T-cell line, MT-1, by UVB or H2O2 dose dependently. Hydrogen Peroxide 70-74 thioredoxin Homo sapiens 4-7 7797250-8 1995 The augmentation of ADF/TRX was observed 6 h after treatment of H2O2. Hydrogen Peroxide 64-68 thioredoxin Homo sapiens 20-23 7797250-8 1995 The augmentation of ADF/TRX was observed 6 h after treatment of H2O2. Hydrogen Peroxide 64-68 thioredoxin Homo sapiens 24-27 7829134-0 1994 Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide. Hydrogen Peroxide 127-144 thioredoxin Homo sapiens 43-54 7961686-3 1994 The 25-kDa enzyme is now shown to be a peroxidase that reduces H2O2 and alkyl hydroperoxides with the use of hydrogens provided by thioredoxin, thioredoxin reductase, and NADPH. Hydrogen Peroxide 63-67 thioredoxin Homo sapiens 131-142 7961686-3 1994 The 25-kDa enzyme is now shown to be a peroxidase that reduces H2O2 and alkyl hydroperoxides with the use of hydrogens provided by thioredoxin, thioredoxin reductase, and NADPH. Hydrogen Peroxide 63-67 thioredoxin Homo sapiens 144-155 7829134-2 1994 In this study, the protective effect of ADF/TRX on the cytotoxicity of endothelial cells caused by phorbol myristate acetate (PMA)-activated neutrophils or hydrogen peroxide (H2O2) was examined. Hydrogen Peroxide 156-173 thioredoxin Homo sapiens 40-43 7829134-2 1994 In this study, the protective effect of ADF/TRX on the cytotoxicity of endothelial cells caused by phorbol myristate acetate (PMA)-activated neutrophils or hydrogen peroxide (H2O2) was examined. Hydrogen Peroxide 156-173 thioredoxin Homo sapiens 44-47 7829134-2 1994 In this study, the protective effect of ADF/TRX on the cytotoxicity of endothelial cells caused by phorbol myristate acetate (PMA)-activated neutrophils or hydrogen peroxide (H2O2) was examined. Hydrogen Peroxide 175-179 thioredoxin Homo sapiens 44-47 7829134-7 1994 These findings indicate that ADF/TRX is an oxidative stress-inducible endogenous protein and rADF/TRX plays a protective role against activated neutrophils- or H2O2-induced endothelial cytotoxicity. Hydrogen Peroxide 160-164 thioredoxin Homo sapiens 29-32 7829134-7 1994 These findings indicate that ADF/TRX is an oxidative stress-inducible endogenous protein and rADF/TRX plays a protective role against activated neutrophils- or H2O2-induced endothelial cytotoxicity. Hydrogen Peroxide 160-164 thioredoxin Homo sapiens 33-36 7829134-7 1994 These findings indicate that ADF/TRX is an oxidative stress-inducible endogenous protein and rADF/TRX plays a protective role against activated neutrophils- or H2O2-induced endothelial cytotoxicity. Hydrogen Peroxide 160-164 thioredoxin Homo sapiens 98-101 7953744-3 1994 We showed that ADF/TRX was actively released from U251 astrocytoma cells upon exposure to a low concentration of H2O2. Hydrogen Peroxide 113-117 thioredoxin Homo sapiens 15-18 7953744-3 1994 We showed that ADF/TRX was actively released from U251 astrocytoma cells upon exposure to a low concentration of H2O2. Hydrogen Peroxide 113-117 thioredoxin Homo sapiens 19-22 7694770-7 1993 Astroglial expression of ADF/TRX in postischemic injuries suggests a role in neuroprotection by hydrogen peroxide reducing and protein-refolding activities or in modulation of local immune responses. Hydrogen Peroxide 96-113 thioredoxin Homo sapiens 29-32 8206709-3 1994 The present investigation is to determine intracellular ADF localization in RPE after transient ischemia and in cultured human RPE cells after oxidative insult by H2O2. Hydrogen Peroxide 163-167 thioredoxin Homo sapiens 56-59 8206709-10 1994 CONCLUSIONS: This study shows the induction of ADF/hTx in mitochondria of RPE after oxidative stresses and its protective effect on cultured RPE exposed to H2O2. Hydrogen Peroxide 156-160 thioredoxin Homo sapiens 47-50 7694770-7 1993 Astroglial expression of ADF/TRX in postischemic injuries suggests a role in neuroprotection by hydrogen peroxide reducing and protein-refolding activities or in modulation of local immune responses. Hydrogen Peroxide 96-113 thioredoxin Homo sapiens 25-28 34523686-7 2022 Treatment of Hydra with hydrogen peroxide (H2O2), a highly reactive oxidizing agent, led to a significant increase in gene expression and enzyme activity of Trx1. Hydrogen Peroxide 24-41 thioredoxin Homo sapiens 157-161 2082835-3 1990 The thioredoxin reductase/thioredoxin system has been shown to reduce superoxide anion radicals through hydrogen peroxide to water. Hydrogen Peroxide 104-121 thioredoxin Homo sapiens 4-15 1425698-5 1992 Essentially all of the thioredoxin in endothelial cells at control state was in the reduced form and 70-85% remained in the reduced form even after the H2O2 treatment. Hydrogen Peroxide 152-156 thioredoxin Homo sapiens 23-34 1425698-7 1992 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. Hydrogen Peroxide 167-171 thioredoxin Homo sapiens 18-29 1510657-2 1992 Recombinant ADF/human thioredoxin produced by E. coli, which has an insulin-reducing activity as efficient as that of E. coli thioredoxin, also reduced some reactive oxygen species, such as hydrogen peroxide. Hydrogen Peroxide 190-207 thioredoxin Homo sapiens 12-15 1510657-2 1992 Recombinant ADF/human thioredoxin produced by E. coli, which has an insulin-reducing activity as efficient as that of E. coli thioredoxin, also reduced some reactive oxygen species, such as hydrogen peroxide. Hydrogen Peroxide 190-207 thioredoxin Homo sapiens 22-33 1510657-2 1992 Recombinant ADF/human thioredoxin produced by E. coli, which has an insulin-reducing activity as efficient as that of E. coli thioredoxin, also reduced some reactive oxygen species, such as hydrogen peroxide. Hydrogen Peroxide 190-207 thioredoxin Homo sapiens 126-137 34523686-7 2022 Treatment of Hydra with hydrogen peroxide (H2O2), a highly reactive oxidizing agent, led to a significant increase in gene expression and enzyme activity of Trx1. Hydrogen Peroxide 43-47 thioredoxin Homo sapiens 157-161 34356388-6 2021 betaHB also alleviated the H2O2-induced inhibition of mTOR and AMPK, known targets of Trx1, in a Trx1-dependent manner, suggesting that betaHB potentiates Trx1 function. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 86-90 34356388-6 2021 betaHB also alleviated the H2O2-induced inhibition of mTOR and AMPK, known targets of Trx1, in a Trx1-dependent manner, suggesting that betaHB potentiates Trx1 function. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 97-101 34356388-6 2021 betaHB also alleviated the H2O2-induced inhibition of mTOR and AMPK, known targets of Trx1, in a Trx1-dependent manner, suggesting that betaHB potentiates Trx1 function. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 155-159 35114579-7 2022 At high loads (>50 muM of H2O2), which caused the exhaustion of thioredoxin activity in the cell cytoplasm, the gradient stabilized, pointing out that it is the functional status of the thioredoxin-depended enzymatic system that drives the dependence of the H2O2 gradient on the oxidative load in human cells. Hydrogen Peroxide 26-30 thioredoxin Homo sapiens 64-75 35420473-3 2022 Here, we uncovered a critical role in this process of a multigene locus encoding a single, fused methionine sulfoxide reductase (MsrAB), a two-component signal transduction system (ModRS), and thioredoxin (Trx)- and cytochrome c (CcdA)-like proteins, which are induced when fusobacterial cells are exposed to hydrogen peroxide. Hydrogen Peroxide 309-326 thioredoxin Homo sapiens 193-204 35114579-7 2022 At high loads (>50 muM of H2O2), which caused the exhaustion of thioredoxin activity in the cell cytoplasm, the gradient stabilized, pointing out that it is the functional status of the thioredoxin-depended enzymatic system that drives the dependence of the H2O2 gradient on the oxidative load in human cells. Hydrogen Peroxide 26-30 thioredoxin Homo sapiens 186-197 35114579-7 2022 At high loads (>50 muM of H2O2), which caused the exhaustion of thioredoxin activity in the cell cytoplasm, the gradient stabilized, pointing out that it is the functional status of the thioredoxin-depended enzymatic system that drives the dependence of the H2O2 gradient on the oxidative load in human cells. Hydrogen Peroxide 258-262 thioredoxin Homo sapiens 64-75 35114579-7 2022 At high loads (>50 muM of H2O2), which caused the exhaustion of thioredoxin activity in the cell cytoplasm, the gradient stabilized, pointing out that it is the functional status of the thioredoxin-depended enzymatic system that drives the dependence of the H2O2 gradient on the oxidative load in human cells. Hydrogen Peroxide 258-262 thioredoxin Homo sapiens 186-197 35179864-7 2022 Mass spectrometry (MS) results show that excessive H2O2 leads to sulfonation modification (-SO3H) at the active sites of Trx1 (Cys32 and Cys35) and Prx1 (Cys52 and Cys173). Hydrogen Peroxide 51-55 thioredoxin Homo sapiens 121-125 33466723-0 2021 Qualitative Differences in Protection of PTP1B Activity by the Reductive Trx1 or TRP14 Enzyme Systems upon Oxidative Challenges with Polysulfides or H2O2 Together with Bicarbonate. Hydrogen Peroxide 149-153 thioredoxin Homo sapiens 73-77 33743241-3 2021 Hydrogen peroxide metabolism regulates cell redox status by driving changes in protein cysteine oxidation often via cycling of thioredoxin/peroxiredoxin and glutathione; however, regulation of enzymes controlling synthesis and utilization of H2O2 is not understood beyond broad outlines. Hydrogen Peroxide 0-17 thioredoxin Homo sapiens 127-138 33466723-8 2021 Comparing reductive activation of polysulfide-inactivated PTP1B with that of bicarbonate- and H2O2-treated enzyme, we found Trx1 to be more potent in reactivation than TRP14. Hydrogen Peroxide 94-98 thioredoxin Homo sapiens 124-128 31279089-2 2019 The present study investigated the roles of Trx1 and Trx reductase1 (TrxR1) proteins in regulation of cell growth, death, reactive oxygen species (ROS) and glutathione (GSH) levels in hydrogen peroxide (H2O2)-treated human pulmonary artery smooth muscle (HPASM) cells. Hydrogen Peroxide 203-207 thioredoxin Homo sapiens 44-48 31279089-0 2019 Upregulated thioredoxin and its reductase prevent H2O2-induced growth inhibition and death in human pulmonary artery smooth muscle cells. Hydrogen Peroxide 50-54 thioredoxin Homo sapiens 12-23 32160414-4 2020 Furthermore, treatment with recombinant human (rh)Trx significantly mitigated the effects of H2 O2 on the myogenic differentiation of BMSCs, and this was abrogated by co-treatment with wortmannin (a specific PI3K inhibitor). Hydrogen Peroxide 93-98 thioredoxin Homo sapiens 50-53 31279089-2 2019 The present study investigated the roles of Trx1 and Trx reductase1 (TrxR1) proteins in regulation of cell growth, death, reactive oxygen species (ROS) and glutathione (GSH) levels in hydrogen peroxide (H2O2)-treated human pulmonary artery smooth muscle (HPASM) cells. Hydrogen Peroxide 184-201 thioredoxin Homo sapiens 44-48 31279089-3 2019 H2O2 induced growth inhibition and cell death in HPASM cells over 24 h. Overexpression of Trx1 and TrxR1 using adenoviruses significantly weakened cell growth inhibition and cell death caused by H2O2. Hydrogen Peroxide 0-4 thioredoxin Homo sapiens 90-94 31279089-3 2019 H2O2 induced growth inhibition and cell death in HPASM cells over 24 h. Overexpression of Trx1 and TrxR1 using adenoviruses significantly weakened cell growth inhibition and cell death caused by H2O2. Hydrogen Peroxide 195-199 thioredoxin Homo sapiens 90-94 31279089-6 2019 adTrx1 and adTrxR1 significantly reduced the increases in O2 - level in H2O2-treated HPASM cells at 24 h. Furthermore, HPASM cells transfected with Trx1 or TrxR1 siRNA showed increases in ROS levels with or without H2O2 at 5 min. Hydrogen Peroxide 72-76 thioredoxin Homo sapiens 2-6 31279089-8 2019 In conclusion, upregulation of Trx1 and TrxR1 significantly attenuated cell growth inhibition and death in H2O2-treated HPASM cells. Hydrogen Peroxide 107-111 thioredoxin Homo sapiens 31-35 31279089-9 2019 As a whole, Trx-related adenoviruses diminished H2O2-induced ROS level in HPASM cells whereas Trx-related siRNAs increased ROS levels and decreased GSH level in these cells. Hydrogen Peroxide 48-52 thioredoxin Homo sapiens 12-15 31197039-4 2019 Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH. Hydrogen Peroxide 187-191 thioredoxin Homo sapiens 345-358 30864831-6 2019 Using human HeLa cells as a model system, we propose that the Trx system, but not the glutathione system, regulates intracellular H2O2 gradients. Hydrogen Peroxide 130-134 thioredoxin Homo sapiens 62-65 31197039-4 2019 Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH. Hydrogen Peroxide 187-191 thioredoxin Homo sapiens 360-364 30456590-5 2019 H2O2 treated cells showed characteristic senescence-associated features including increased cell size, senescence-associated beta-galactosidase activity (SA-beta-gal), development of senescence-associated secretory phenotype (SASP), activation of reactive oxygen species (ROS) and pathways, DNA damage as well as induction of cell cycle inhibitors (p53/p21WAF1/p16INK4a). Hydrogen Peroxide 0-4 thioredoxin Homo sapiens 226-230 31045571-4 2019 Thioredoxin1 (Trx1) counteracts oxidative stress by scavenging reactive oxygen species (ROS) and regulating other enzymes that metabolize H2O2. Hydrogen Peroxide 138-142 thioredoxin Homo sapiens 0-12 31045571-4 2019 Thioredoxin1 (Trx1) counteracts oxidative stress by scavenging reactive oxygen species (ROS) and regulating other enzymes that metabolize H2O2. Hydrogen Peroxide 138-142 thioredoxin Homo sapiens 14-18 30576925-0 2019 Inhibition of thioredoxin-dependent H2O2 removal sensitizes malignant B-cells to pharmacological ascorbate. Hydrogen Peroxide 36-40 thioredoxin Homo sapiens 14-25 30639567-10 2019 Moreover, it disrupted the H2O2-initiated polymerization of Trx and converted Trx from the oxidized to the reduced form. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 60-63 30639567-10 2019 Moreover, it disrupted the H2O2-initiated polymerization of Trx and converted Trx from the oxidized to the reduced form. Hydrogen Peroxide 27-31 thioredoxin Homo sapiens 78-81 30659092-0 2019 Pancreatic beta-cells detoxify H2O2 through the peroxiredoxin/thioredoxin antioxidant system. Hydrogen Peroxide 31-35 thioredoxin Homo sapiens 62-73 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 221-225 thioredoxin Homo sapiens 55-66 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 221-225 thioredoxin Homo sapiens 151-162 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 221-225 thioredoxin Homo sapiens 151-162 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 266-270 thioredoxin Homo sapiens 55-66 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 266-270 thioredoxin Homo sapiens 151-162 30659092-6 2019 This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selective chemical inhibition or siRNA-mediated depletion of thioredoxin reductase sensitized beta-cells to continuously generated H2O2 In contrast, when delivered as a bolus, H2O2 induced the DNA damage response, depleted cellular energy stores, and decreased beta-cell viability independently of thioredoxin reductase inhibition. Hydrogen Peroxide 266-270 thioredoxin Homo sapiens 151-162 30659092-7 2019 These findings show that beta-cells have the capacity to detoxify micromolar levels of H2O2 through a thioredoxin reductase-dependent mechanism and are not as sensitive to oxidative damage as previously thought. Hydrogen Peroxide 87-91 thioredoxin Homo sapiens 102-113 30576925-3 2019 Here we present that thioredoxin antioxidant system plays a key role in the scavenging of extracellularly-generated H2O2 in malignant B-cells. Hydrogen Peroxide 116-120 thioredoxin Homo sapiens 21-32 30576925-4 2019 We show that inhibition of peroxiredoxin 1, the enzyme that removes H2O2 in a thioredoxin system-dependent manner, increases the sensitivity of malignant B-cells to L-ASC. Hydrogen Peroxide 68-72 thioredoxin Homo sapiens 78-89 30576925-5 2019 Moreover, we demonstrate that auranofin (AUR), the inhibitor of the thioredoxin system that is used as an antirheumatic drug, diminishes the H2O2-scavenging capacity of malignant B-cells and potentiates pharmacological ascorbate anticancer activity in vitro and in vivo. Hydrogen Peroxide 141-145 thioredoxin Homo sapiens 68-79 30196924-8 2018 Interestingly, prior to H2O2 addition, gene expression of a thioredoxin and peroxiredoxin was much lower in the toxic strain than in its non-toxic mutant. Hydrogen Peroxide 24-28 thioredoxin Homo sapiens 60-71 30196924-9 2018 Thioredoxin and peroxiredoxin are both involved in H2O2 degradation, and microcystin may potentially suppress their activity. Hydrogen Peroxide 51-55 thioredoxin Homo sapiens 0-11 28939765-10 2017 Of note, Trx1 overexpression attenuated both H2O2-mediated mTOR oxidation and inhibition, whereas Trx1 knockdown increased mTOR oxidation and inhibition. Hydrogen Peroxide 45-49 thioredoxin Homo sapiens 9-13 28939765-11 2017 Moreover, Trx1 normalized H2O2-induced down-regulation of metabolic genes and stimulation of cell death, and an mTOR inhibitor abolished Trx1-mediated rescue of gene expression. Hydrogen Peroxide 26-30 thioredoxin Homo sapiens 10-14 28636040-4 2017 In vitro, all three TLMs became strong inhibitors of the cytosolic (TrxR1) and mitochondrial (TrxR2) isoforms of thioredoxin reductase after enzymatic oxidation with HRP/H2O2 while none of the organic analogues was effective. Hydrogen Peroxide 170-174 thioredoxin Homo sapiens 113-124 28270496-4 2017 In addition, stimulating AML-M5 cells with low concentrations of hydrogen peroxide led to increased Jab1 and Trx expression. Hydrogen Peroxide 65-82 thioredoxin Homo sapiens 109-112 28441057-5 2017 Chemokine-controlled NADPH oxidases and metabolically controlled mitochondrial sources of H2O2 as well as glutathione- and thioredoxin-related pathways, with powerful enzymatic back-up systems, are responsible for fine-tuning physiological redox signaling. Hydrogen Peroxide 90-94 thioredoxin Homo sapiens 123-134 28680816-12 2017 Consistent with the involvement of rTOP in a signaling redox cascade, the H2O2-oxidized rTOP reacted with dimeric thioredoxin-1 (TRx-1) and remained covalently bound to one subunit of TRx-1. Hydrogen Peroxide 74-78 thioredoxin Homo sapiens 114-127 28680816-12 2017 Consistent with the involvement of rTOP in a signaling redox cascade, the H2O2-oxidized rTOP reacted with dimeric thioredoxin-1 (TRx-1) and remained covalently bound to one subunit of TRx-1. Hydrogen Peroxide 74-78 thioredoxin Homo sapiens 129-134 28680816-12 2017 Consistent with the involvement of rTOP in a signaling redox cascade, the H2O2-oxidized rTOP reacted with dimeric thioredoxin-1 (TRx-1) and remained covalently bound to one subunit of TRx-1. Hydrogen Peroxide 74-78 thioredoxin Homo sapiens 184-189 28035213-1 2016 Peroxiredoxin-3 (Prdx3) is a mitochondrial protein of the thioredoxin family of antioxidant peroxidases and is the principal peroxidase responsible for metabolizing mitochondrial hydrogen peroxide. Hydrogen Peroxide 179-196 thioredoxin Homo sapiens 58-69