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NTRC plays a pivotal role in chloroplast redox regulation, being necessary for the activity of diverse thioredoxins with unrelated functions.
NTRC-mediated regulation of the Calvin-Benson cycle and ATP synthesis occurs both directly and through interaction with the ferredoxin-thioredoxin (Montrer TXN Protéines) system and is crucial when availability of light is limiting photosynthesis.
NTRC is highly sensitive to rapidly changing light intensities.NTRC is not responsible for 'metabolism-related' regulation of the ATP synthase.
cooperative control of chloroplast functions via the FTR/Trx (Montrer TXN Protéines) and NTRC pathways is essential for plant viability
These data uncover a new role for NTRC in the control of photosynthetic yield.
An Arabidopsis thaliana double knockout mutant lacking NTRC and Srx (Montrer SRX1 Protéines) shows a phenotype similar to the ntrc mutant, while the srx (Montrer SRX1 Protéines) mutant resembles wild-type plants. NTRC deficiency causes reduced overoxidation of 2-Cys (Montrer DNAJC5 Protéines) peroxiredoxins.
NADPH thioredoxin reductase C is involved in redox regulation of the Mg-chelatase I subunit in Arabidopsis thaliana chloroplasts
interaction of chloroplast 2-Cys (Montrer DNAJC5 Protéines) peroxiredoxin with NADPH (Montrer NQO1 Protéines)-thioredoxin reductase C (NTRC) and thioredoxin (Montrer TXN Protéines) x
The strongest reduction in ntrc growth occurred under photoperiods with nights longer than 14 h, whereas knockout of the NTRC gene did not alter the circadian-clock-controlled growth. Lack of NTRC modulated chloroplast reactive oxygen species metabolism.
heat shock-mediated holdase chaperone function of NTRC is responsible for the increased thermotolerance of Arabidopsis and the activity is significantly supported by NADPH
Selenoprotein TRXR-1 and GSR-1 (Montrer GSR Protéines) are essential for removal of old cuticle during molting in Caenorhabditis elegans.
this study shows that miR-125a suppressed TrxR1 expression by targeting its 3'-UTR in endothelial cells
Based on recent research, it has been reported that the modulation of the Trx/TrxR (Montrer GSR Protéines) system may be considered as a new target in the management of the metabolic syndrome, insulin (Montrer INS Protéines) resistance, and type 2 diabetes, as well as in the treatment of hypertension and atherosclerosis. In this review evidence about a possible role of this system as a marker of the metabolic syndrome is reported. [review]
In human colonic epithelial cells, significant upregulation of NAD(P)H dehydrogenase (Montrer NQO1 Protéines) [quinone] 1 (up to threefold) and thioredoxin reductase 1 (up to twofold) by 10muM sulforaphane (from broccoli), 5muM carnosol (rosemary), and 20muM cinnamaldehyde (cinnamon) was observed.
The reducing system of PTEN was comprised of NADPH (Montrer NQO1 Protéines), thioredoxin reductase (TrxR1 (Montrer GSR Protéines)), and thioredoxin (Trx (Montrer TXN Protéines)).
These results suggest that TrxR1 suppresses anabolic metabolism and adipogenesis by inhibition of intracellular signaling pathways downstream of insulin (Montrer INS Protéines) stimulation.
However, Ethaselen can induce a high level of ROS (Montrer ROS1 Protéines) in K562/CDDP by TrxR activity inhibition and increased ratio of Bax (Montrer BAX Protéines) to Bcl-2 (Montrer BCL2 Protéines) in K562/CDDP by nuclear factor kappaB (NF-kappaB (Montrer NFKB1 Protéines)) suppression, which subsequently induces the release of cytochrome c (Montrer CYCS Protéines) in K562/CDDP. This response is partly responsible for the reversal of the cisplatin resistance in K562/CDDP cells.
Multivariate analysis found TXNRD1 was an independent prognostic factor for hepatocellular carcinoma (HCC (Montrer FAM126A Protéines))patients. In conclusion, our data suggested that TXNRD1 was a biomarker for the prognosis of patients with HCC (Montrer FAM126A Protéines).
Mechanistic study uncovers for the first time that the selenoprotein thioredoxin reductase (TrxR) is one of the targets by which PL-CL promotes the ROS generation
Endogenous TrxR1 is sensitive to nitrosylation-dependent inactivation.
This study thus provides novel insights into the catalytic mechanisms of TrxR1. One-electron juglone reduction by TrxR1 producing superoxide should furthermore contribute to the well-known prooxidant cytotoxicity of juglone
The developmental expression of cytosolic glutathione peroxidase (Montrer GPX1 Protéines) and TRXR1 during fetal development and the effect of maternal selenium consumption on the expression of these proteins are reported.
regenerated coronary endothelial cells exhibit downregulation of thioredoxin reductase
These results suggest that thioredoxin reductase (Montrer PRDX5 Protéines) may act as a positive regulator of NF-kappa B (Montrer NFKB1 Protéines) and may play an important role in the cellular inflammatory response.
data provide evidence for the involvement of the Trx/TrxR (Montrer GSR Protéines) system, in the regulation of haem oxygenase-1 expression in aortic endothelial cells during pro-oxidant challenge
GSR (Montrer GSR Protéines) is not essential for the maintenance of antioxidant defenses in mouse cochlea; the thioredoxin/thioredoxin (Montrer TXN Protéines) reductase (Montrer PRDX2 Protéines) system can probably operate as a functional backup for GSR (Montrer GSR Protéines).
TrxR1 represents a novel therapeutic target to prevent oxygen-mediated neonatal lung injury through Nrf2 (Montrer NFE2L2 Protéines).
The results demonstrate that DATS protects against oxidative stress-induced (Montrer SQSTM1 Protéines) DNA damage and apoptosis in C2C12 cells in part through the activation of Nrf2 (Montrer NFE2L2 Protéines)-mediated TrxR1 induction via the ERK (Montrer EPHB2 Protéines) signaling pathway.
Collectively, our results suggest that MsrA (Montrer MSR1 Protéines) protects hepatocytes from APAP-induced cytotoxicity through the modulation of TXNRD1 expression.
the timely upregulation of Trx1 (Montrer TXN Protéines)/TrxR1 and the active control of intracellular redox status is critical for the survival of thymocytes during and short after positive selection.
Considering the variable expression levels of Sep15 (Montrer SEP15 Protéines) and TR1 found within the human population, our results provide insights into new roles of selenoproteins in cancer
Data suggest TXNRD1 and TXRNRD2 function at the top of a redox pyramid that governs the oxidation state of peroxiredoxins and other protein factors, thereby dictating a hierarchy of phenotypic responses to oxidative insults.
Augmentation of GSH systems by TrxR1 inhibition could represent a promising therapeutic approach to attenuate oxidant-mediated lung injury and improve patient outcomes.
Because the N-terminal domain of Sepp1 (Montrer SEPP1 Protéines) has a thioredoxin (Montrer TXN Protéines) fold, Sepp1 (Montrer SEPP1 Protéines)(UF) were compared with full-length Sepp1 (Montrer SEPP1 Protéines), Sepp1 (Montrer SEPP1 Protéines)(Delta240-361), and Sepp1 (Montrer SEPP1 Protéines)(U40S) as a substrate of thioredoxin reductase-1 (TrxR1).
This gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms.
thioredoxin reductase 1, cytoplasmic
, thioredoxin reductase 3
, thioredoxin reductase 1
, thioredoxin reductase 1, cytoplasmic-like
, KM-102-derived reductase-like factor
, gene associated with retinoic and IFN-induced mortality 12 protein
, gene associated with retinoic and interferon-induced mortality 12 protein
, thioredoxin reductase GRIM-12
, thioredoxin reductase TR1
, redox enzyme thioredoxin reductase
, NADPH-dependent thioredoxin reductase
, selenoprotein oxidoreductase
, TR alpha