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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 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 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 shows a phenotype similar to the ntrc mutant, while the srx mutant resembles wild-type plants. NTRC deficiency causes reduced overoxidation of 2-Cys 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 peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin 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
analysis of electron transfer pathways and dynamics of chloroplast NADPH-dependent thioredoxin reductase C (NTRC)
NADPH-thioredoxin reductase C (NTRC), previously reported as exclusive to green tissues, is also expressed in nonphotosynthetic tissues of Arabidopsis thaliana.
ANTR-C functions as an electron donor for plastidial 2-Cys peroxiredoxins and represents the NADPH-dependent thioredoxin/thioredoxin reductase system in chloroplasts. [ANTR-C]
Arabidopsis knock-out mutant showed growth inhibition and hypersensitivity to methyl viologen.
NTRC and 2-Cys Prx are involved in the protection of at least the later part of the chlorophyll biosynthetic pathway; NTRC and 2-Cys Prx in vitro stimulate the aerobic cyclase step of this pathway.
Chloroplast NADPH-thioredoxin reductase, NTRC, regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. [NTRC]
Selenoprotein TRXR-1 and GSR-1 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 system may be considered as a new target in the management of the metabolic syndrome, insulin 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 [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, thioredoxin reductase (TrxR1), and thioredoxin (Trx).
These results suggest that TrxR1 suppresses anabolic metabolism and adipogenesis by inhibition of intracellular signaling pathways downstream of insulin stimulation.
However, Ethaselen can induce a high level of ROS in K562/CDDP by TrxR activity inhibition and increased ratio of Bax to Bcl-2 in K562/CDDP by nuclear factor kappaB (NF-kappaB) suppression, which subsequently induces the release of cytochrome c 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)patients. In conclusion, our data suggested that TXNRD1 was a biomarker for the prognosis of patients with HCC.
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
Mutation of TXNRD1 was identified in a family with genetic generalized epilepsy.
Data show that small molecule B19 targets and inactivates thioredoxin reductase 1 (TrxR1) in gastric cancer cells.
Analysis of 25 independent cohorts with 5910 patients showed that Trx1 and TrxR1 were both associated with a poor patient prognosis in terms of overall survival, distant metastasis free survival and disease free survival.
High TRXR1 expression is associated with oral squamous cell carcinoma.
Inhibition of thioredoxin reductase-1 by brevetoxin-2 is via the formation of a Michael adduct between selenocysteine and the alpha, beta-unsaturated aldehyde moiety of the toxin.
Here, the authors use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1).
Taken together, these findings indicate that auranofin inhibition of TrxR activity in Hep3B cells activates ROS- and caspase-dependent apoptotic signaling pathways and triggers cancer cell death.
It was observed that the combination of redox/protonation states of the N-terminal (FAD and Cys59/64) and C-terminal (Cys497/Selenocysteine498) redox centers defines the preferred relative positions and allows for the flexible arm to work as the desired electron "shuttle."
Our results clearly demonstrate that DIMC can synergistically enhance the cancer cell killing when combined with radiation by targeting thioredoxin system.
thioredoxin reductase is inhibited by plumbagin, which leads to apoptosis in HL-60 cells
The developmental expression of cytosolic glutathione peroxidase 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 may act as a positive regulator of NF-kappa B and may play an important role in the cellular inflammatory response.
data provide evidence for the involvement of the Trx/TrxR system, in the regulation of haem oxygenase-1 expression in aortic endothelial cells during pro-oxidant challenge
Study in transgenic mice finds that T-cell activation is linked to a drastic downregulation of Txnip and an increase in Txn1/Txnrd1 expression, which is absolutely required for synthesis of 2'-deoxyribonucleotides during T-cell metabolic reprogramming. Txnrd1 is critical for expansion of the activated T-cell population during viral and parasite infection.
GSR is not essential for the maintenance of antioxidant defenses in mouse cochlea; the thioredoxin/thioredoxin reductase system can probably operate as a functional backup for GSR.
TrxR1 represents a novel therapeutic target to prevent oxygen-mediated neonatal lung injury through Nrf2.
The results demonstrate that DATS protects against oxidative stress-induced DNA damage and apoptosis in C2C12 cells in part through the activation of Nrf2-mediated TrxR1 induction via the ERK signaling pathway.
Collectively, our results suggest that MsrA protects hepatocytes from APAP-induced cytotoxicity through the modulation of TXNRD1 expression.
the timely upregulation of Trx1/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 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 has a thioredoxin fold, Sepp1(UF) were compared with full-length Sepp1, Sepp1(Delta240-361), and Sepp1(U40S) as a substrate of thioredoxin reductase-1 (TrxR1).
Sec-containing TrxR1 is absolutely required for self-sufficient growth of MEFs under high-glucose conditions, owing to an essential importance of this enzyme for elimination of glucose-derived H2O2.
The exaggerated TrxR release to serum upon liver injury may reflect more complex events than a mere passive release of hepatic enzymes to the extracellular milieu.
TrxR1-deficient cells are more sensitive to TNF-alpha induced apoptosis than control cells.
Txnrd1-null livers did not have more effective gene expression responses to APAP challenge; however, their constitutive metabolic state supported more robust GSH biosynthesis, glutathionylation, and glucuronidation systems
TR1 protects against chemically induced hepatocarcinogenesis via the control of the cellular redox state, whereas its role in promoting this type of cancer is minimal
new role for TR1 in cancer that is independent of Trx reduction and compensated for by the glutathione system
TR1 down-regulation is important in maintaining high levels of reactive oxygen species (ROS) under hypoxic conditions and HIF stabilization and activity do not require hypoxic generation of ROS.
hepatocyte proliferation in vivo requires either glutathione (GSH) or at least one functional allele of txnrd1, demonstrating that either the GSH- or the TrxR1-dependent redox pathway can independently support hepatocyte proliferation during liver growth.
results reveal TR1 as both a regulator and a regulated target in the macrophage gene expression network
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