Differential thioredoxin reductase activity from human normal hepatic and hepatoma cell lines.: Thioredoxin reductase (TrxR), a component of the thioredoxin sys

Shop Probable pyridine nucleotide-disulfide oxidoreductase ELISA Kit, Recombinant Protein and Probable pyridine nucleotide-disulfide oxidoreductase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.

PubMed Central Canada (PMC Canada) provides free access to a stable and permanent online digital archive of full-text, peer-reviewed health and life sciences research publications. It builds on PubMed Central (PMC), the U.S. National Institutes of Health (NIH) free digital archive of biomedical and life sciences journal literature and is a member of the broader PMC International (PMCI) network of e-repositories.

Author: Fritz-Wolf, Karin et al.; Genre: Journal Article; Published in Print: 2007-06-29; Keywords: thioredoxin reductase 1; structure; inhibitor development; catalysis; Title: The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis

TY - JOUR. T1 - Thioredoxin inhibitors attenuate platelet function and thrombus formation. AU - Metcalfe, Clive. AU - Ramasubramoni, Anjana. AU - Pula, Giordano. AU - Harper, Matthew T. AU - Mundell, Stuart J. AU - Coxon, Carmen H. PY - 2016/10/7. Y1 - 2016/10/7. N2 - Thioredoxin (Trx) is an oxidoreductase with important physiological function. Imbalances in the NADPH/thioredoxin reductase/thioredoxin system are associated with a number of pathologies, particularly cancer, and a number of clinical trials for thioredoxin and thioredoxin reductase inhibitors have been carried out or are underway. Due to the emerging role and importance of oxidoreductases for haemostasis and the current interest in developing inhibitors for clinical use, we thought it pertinent to assess whether inhibition of the NADPH/thioredoxin reductase/thioredoxin system affects platelet function and thrombosis. We used small molecule inhibitors of Trx (PMX 464 and PX-12) to determine whether Trx activity influences platelet ...

Thioredoxin reductases (TR, TrxR) (EC 1.8.1.9) are the only known enzymes to reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one class in bacteria and some eukaryotes and one in animals. Both classes are flavoproteins which function as homodimers. Each monomer contains a FAD prosthetic group, a NADPH binding domain, and an active site containing a redox-active disulfide bond. Thioredoxin reductase is the only enzyme known to catalyze the reduction of thioredoxin and hence is a central component in the thioredoxin system. Together with thioredoxin (Trx) and NADPH this systems most general description is as a method of forming reduced disulfide bonds in cells. Electrons are taken from NADPH via TrxR and are transferred to the active site of Trx, which goes on to reduce protein disulfides or other substrates. The Trx system exists in all living cells and has an evolutionary history tied to DNA as a genetic material, defense against oxidative damage due to ...

Mammalian thioredoxin reductase (TrxR) catalyzes reduction of thioredoxin and many other substrates, and is a central enzyme for cell proliferation and thiol redox control. The enzyme is a selenoprotein and can therefore, like all other mammalian selenoproteins, not be directly expressed in Escheric …

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.

The thioredoxin-dependent system is an essential regulator of cellular redox balance. Since oxidative stress has been linked with neurodegenerative disease, we studied the roles of thioredoxin reductases in brain using mice with nervous system (NS)-specific deletion of cytosolic (Txnrd1) and mitochondrial (Txnrd2) thioredoxin reductase. While NS-specific Txnrd2 null mice develop normally, mice lacking Txnrd1 in the NS were significantly smaller and displayed ataxia and tremor. A striking patterned cerebellar hypoplasia was observed. Proliferation of the external granular layer (EGL) was strongly reduced and fissure formation and laminar organisation of the cerebellar cortex was impaired in the rostral portion of the cerebellum. Purkinje cells were ectopically located and their dendrites stunted. The Bergmann glial network was disorganized and showed a pronounced reduction in fiber strength. Cerebellar hypoplasia did not result from increased apoptosis, but from decreased proliferation of granule ...

Chlamydomonas NtrC antibody, thioredoxin reductase plant antibody, Ntrc antibodies, thioredoxin reductase antibodyThioredoxin Reductase (TR, TrxR) is the only known enzyme (EC 1.8.1.9) which is reducing thoredoxin (Trx). Activity of thoredoxin is essenti

TY - CONF. T1 - The effect of oxidative stress on thioredoxin1 distribution and associated binding partners in T cells. AU - Remtulla, Ali. AU - Torrao, Rita. AU - Wilmot, Chloe. AU - Griffiths, Helen. PY - 2016/7/1. Y1 - 2016/7/1. N2 - Ageing is associated with a progressive decline in immune function that contributes to age-related diseases. Growing evidence suggests that increased reactive oxygen species (ROS) production occurs with age. This can alter a variety of immune functions including T cell function and proliferation. Key antioxidants are involved in removing ROS and maintaining the cellular redox state of the cell such as glutathione (GSH), peroxiredoxin (Prx) and thioredoxin (Trx) systems. The main objective of this study was to look at the effect of oxidative stress to these key systems and to identify the changes to binding partners and Trx1 distribution. Activation of T cells in PBMCs using anti-CD3/CD28 antibodies was undertaken to look at Trx1 distribution and secretion during ...

Styrene, a widely used industrial chemical, is ototoxic. It causes death of auditory hair cells after about 7 days of exposure (800 mg/kg/day) through apoptosis (Chen et al., 2007). This study was designed to determine styreneinduced alterations in the cochlea underlying the apoptotic cell death. Thioredoxin(Trx)/thioredoxin reductase(TrxR) system plays an important role in maintaining cellular re

Cytoplasmic thioredoxin reductase, key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive ...

Residues 10-304 span seven regions of similarity to blocks BL00573 A-E, which encompass pyridine nucleotide disulphide oxidoreductases class-II proteins. Residues 6-174 span several regions of similarity to blocks for aromatic-ring hydrolases, pyridine nucleotide-disulfide oxidoreductases class-I, bacterial-type phytoene dehydrogenases, adrenodoxin reductase family signatures, FMO signatures, fumarate reductase/succinate dehydrogenase FAD-binding site proteins, flavin-containing amine oxidase signatures ...

Gold(I) complexes of imidazole and thiazole-based diphos type ligands were prepared and their potential as chemotherapeutics investigated. Depending on the ligands employed and the reaction conditions complexes [L(AuCl)2] and [L2Au]X (X = Cl, PF6) are obtained. The ligands used are diphosphanes with azoyl substituents R2P(CH2)2PR2 {R = 1-methylimidazol-2-yl (1), 1-methylbenzimidazol-2-yl (4), thiazol-2-yl (5) and benzthiazol-2-yl (6)} as well as the novel ligands RPhP(CH2)2PRPh {R = 1-methylimidazol-2-yl (3)} and R2P(CH2)3PR2 {R = 1-methylimidazol-2-yl (2)}. The cytotoxic activity of the complexes was assessed against three human cancer cell lines and a rat hepatoma cell line and correlated to the lipophilicity of the compounds. The tetrahedral gold complexes [(3)2Au]PF6 and [(5)2Au]PF6 with intermediate lipophilicity (logD7.4 = 0.21 and 0.25) showed significant cytotoxic activity in different cell lines. Both compounds induce apoptosis and inhibit the enzymes thioredoxin reductase and ...

Specific mobile components including products of phosphatidylinositol (PI) metabolism play a significant role as signaling molecules in stomatal responses to environmental alerts. for 18 times in a rise chamber (continuous white light of 80 mol m-2 s-1 at 22C28C and 30C60% comparative dampness) after getting kept at 4C at night for 2 times. The plants had been transplanted onto a nutritional solution made up of the next macronutrients: 1.25 mM KNO3, 0.5 mM Ca(NO3)2, 0.5 mM MgSO4, 0.625 mM KH2PO4, and the next micronutrients: 17.5 M H3BO3, 12.5 M Fe EDTA 3H2O, 3.5 M MnCl2 4H2O, 2.5 M NaCl, 0.25 M ZnSO4 7H2O, 0.125 M CuSO4 5H2O, 0.05 M Na2Mo4 2H2O, and 0.0025 M CoCl2 6H2O. The ultimate option pH was 5.5. Plant life at 22C24 times old had been utilized to measure stomatal aperture. The transgenic range expressing GFP-PATROL1 was expanded on solid 1/2 Murashige and Skoog (MS) moderate for seven days in a rise chamber (18/6 h light/dark routine using white light of 60 mol m-2 s-1 at 23.5C). ...

Manipulation of hematopoietic come/progenitor cells (HSPCs) ex lover vivo is of clinical importance for come cell growth and gene therapy applications. engraftment and homing, offering a mechanistic description for the homing/engraftment problem of bicycling cells and a potential fresh restorative focus on to enhance engraftment. Intro Since the finding and refinement of the 1st hematopoietic cytokines even more than 2 years ago, ex lover vivo tradition methods possess been created for come cell growth and gene therapy applications. The capability to broaden hematopoietic control/progenitor cells (HSPCs) could widen the availability and improve the efficiency of cable bloodstream (CB) transplantation, swiftness recovery from cytopenias after transplantation, and assure engraftment in nonmyeloablative or mismatched allogeneic transplantation. Hereditary manipulation of HSPCs with retroviral vectors needs old flame vivo pleasure with cytokines to keep viability and to induce development through ...

p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...

TrxR1 antibody (thioredoxin reductase 1) for ICC/IF, IHC-P, WB. Anti-TrxR1 pAb (GTX103207) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.

MI 4 Vitja Gričar s.p., Kajuhova 7, 8270 Krško. Matična št. 7124724000, davčna št. SI 13576275, TRR SI56 1010 0005 5429 578 pri Banki Koper. ...

In Neisseria gonorrhoeae, the MerR family transcription factor NmlR activates 3 operons in response to disulfide stress. In the present study, we show that trxB, a monocistronic operon under the control of NmlR, encodes a functional thioredoxin reductase. It is shown that neisserial TrxB has biochemical properties similar to those of its homologue from Escherichia coli. Analysis of a trxB mutant of N. gonorrhoeae showed that it was more sensitive to disulfide stress and to stress induced by organic hydroperoxides, superoxide, and nitric oxide than wild-type gonococcus. TrxB was found to be essential for the microaerobic induction of aniA and norB, the genes encoding nitrite reductase and nitric oxide reductase, respectively. The importance of TrxB during natural infection was demonstrated by the fact that the survival of gonococci within human cervical epithelial cells, as well as biofilm formation on these cells, was greatly reduced for a trxB mutant compared with a wild-type strain ...

The purpose of this work was to study the prognostic influence in breast cancer of thioredoxin reductase 1 (TXNRD1) and thioredoxin interacting protein (TXNIP), key players in oxidative stress control that are currently evaluated as possible therapeutic targets. Analysis of the association of TXNRD1 and TXNIP RNA expression with the metastasis-free interval (MFI) was performed in 788 patients with node-negative breast cancer, consisting of three individual cohorts (Mainz, Rotterdam and Transbig). Correlation with metagenes and conventional clinical parameters (age, pT stage, grading, hormone and ERBB2 status) was explored. MCF-7 cells with a doxycycline-inducible expression of an oncogenic ERBB2 were used to investigate the influence of ERBB2 on TXNRD1 and TXNIP transcription. TXNRD1 was associated with worse MFI in the combined cohort (hazard ratio = 1.955; P | 0.001) as well as in all three individual cohorts. In contrast, TXNIP was associated with better prognosis (hazard ratio = 0.642; P | 0.001)

Beier E, Richardson J (2015) Parkinsons Disease: animal and in vitro studies on dopaminergic neurotoxicants. In Environmental Factors in Neurodevelopmental and Neurodegenerative Disorders. Elsevier, San Diego. 267-288. Eyo U, Gu N, De S, Dong H, Richardson J, Wu L (2015) Modulation of microglial process convergence toward neuronal dendrites by extracellular calcium. J Neurosci. 35: 2417-22. PMCID: PMC4323526. Gu N, Eyo U, Murugan M, Peng J, Matta S, Dong H, Wu L (2015) Microglial P2Y12 receptors regulate microglial activation and surveillance during neuropathic pain. Brain Behav Immun. S0889-1591 PMCID:PMC4864135. Jan Y, Heck D, Casillas R, Laskin D, Laskin J (2015) Thioredoxin cross-linking by nitrogen mustard in lung epithelial cells: formation of multimeric thioredoxin/thioredoxin reductase complexes and inhibition of disulfide reduction. Chem Res Toxicol 28: 2091-103 PMCID:PMC4877171. Jan Y, Richardson J, Baker A, Mishin V, Heck D, Laskin D, Laskin J (2015) Vitamin K3 (menadione) redox ...

Background: Thioredoxin (Trx) and thioredoxin reductase (TrxR), together with NADPH, constitute the Trx system, a major antioxidant entity that helps maintain a reducing environment within living cells. Trx designates a family of proteins that are related on the basis of structure and function. Human full-length Trx is a 12 kDa redox-active protein that contains the evolutionarily conserved active site sequence Cys-Gly Pro-Cys. Truncated Trx is a shorter, 10 kDa form of human Trx that shows complete homology to the N-terminal 80 or 84 amino acids of 12 kDa Trx. Truncated Trx displays no reducing activity, even though it contains an intact active site. Human TrxR is a homodimeric, FAD-containing, selenoprotein that reduces oxidized Trx back to the enzymatically active form by consuming NADPH. Expression of human Trx and TrxR is induced by a variety of stressors. The Trx system functions directly and indirectly in important biological features such as DNA synthesis, gene expression, co-cytokine ...

Read Identification and characterization of novel variants of the thioredoxin reductase 3 new transcript 1 TXNRD3NT1, Mammalian Genome on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.

Present study was undertaken to purify and characterize thioredoxin reductase (TrxR) of Plasmodium berghei, a rodent malaria parasite. Plasmodium contains thioredoxin redox system that acts as efficient antioxidant system preventing damage caused by enhanced oxidative stress. Thioredoxin (Trx) functions as redox messenger in the parasite maintaining a reduced intracellular environment. Thioredoxin reductase (E.C.1.8.1.9) was analysed in rodent malaria parasite, Plasmodium berghei. Cell-free parasite showed TrxR specific activity of 0.128±0.10 U mg-1. Maximum TrxR activity was observed in cytosolic fraction of P. berghei. The parasite enzyme was purified by ammonium sulphate precipitation and Sephadex G-200. Its molecular weight was 22 kDa and the enzyme remained maximally active at pH 7.4 while the higher temperatures inactivated the enzyme. Km (Michaelis constant) and Vmax (Maximum velocity of enzyme) values for dithionitrobenzene (DTNB) substrate were 1.25 and 0.1 mM, respectively. ...

Thioredoxin reductase 2 (TR2) activity, its gene transcripts, and hydrogen peroxide (H2O2) generation were examined in biochemically identified early-senescent P20 and senescent P30 fibroblasts subcultured in media (MEM2-MEM8) containing Se concentrations at 1.25, 2.5, 3.5, 5.0, 6.0, 7.0, and 8.0 µM, respectively. Although TR2 activity was moderately increased in P20 and P30 cells subcultured in routine growth medium (MEM1), there were progressive significant activity increases in the same cells subcultured in MEM2-MEM8. Such increases were proportional to Se concentration and peaked in P30 cells incubated with MEM7 and MEM8. H2O2 generation underwent progressive increases in MEM1-incubated P20 and P30 cells, peaking in the latter, but was gradually lowered in those incubated with MEM2-MEM8, reaching its lowest values when cells were incubated with MEM7 and MEM8. In parallel, TR2 gene transcripts underwent significant upregulation in P20 cells and higher magnitude upregulation in P30 cells subcultured

This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014 ...

Abstract: The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx). In the pyridine nucleotide-dependent Trx reduction pathway, reducing equivalents, typically from reduced nicotinamide adenine dinucleotide phosphate (NADPH), are transferred from NADPH-TR (NTR) to Trx and, in turn, to target proteins, thus resulting in the reversible modification of the structural and functional properties of the targets. NTR enzymes contain three functional sites: an NADPH binding pocket, a non-covalently bound flavin cofactor, and a redox-active disulfide in the form of CxxC. With the aim of increasing our knowledge of the thioredoxin system in archaea, we here report the high-resolution crystal structure of NTR from the methane-generating organism Methanosarcina mazei strain Gö1 (MmNTR) at 2.6 Å resolution. Based on the crystals presently described, MmNTR assumes ...

The antitrypanosomal and antitumour activities of (2,2:6,2-terpyridine)platinum(II) complexes have been postulated to be due to their ability to inhibit irreversibly the NADPH/FAD redox enzymes trypanothione reductase and human thioredoxin reductase respectively. Here we show that these platinum(II) complexes metallate recombinant human albumin (rHA) at the single free thiol group (Cys-34). Moreover, the (2,2:6,2-terpyridine)platinum(II) complex can be transferred from rHA to other thiols, such as 2-hydroxyethanethiol or glutathione. Human serum albumin could therefore provide a natural transport mechanism for the selective delivery of these agents to tumor cells by the enhanced permeability and retention (EPR) mechanism.

Thioredoxins [(PUBMED:3896121), (PUBMED:2668278), (PUBMED:7788289), (PUBMED:7788290)] are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide in the substrate protein [(PUBMED:3896121)].. Thioredoxin is present in prokaryotes and eukaryotes and the sequence around the redox-active disulphide bond is well conserved. All thioredoxins contain a cis-proline located in ...

Missirlis, F.; Ulschmid, J. K.; Hirosawa-Takamori, M.; Groenke, S.; Schaefer, U.; Becker, K.; Phillips, J. P.; Jaeckle, H.: Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. Journal of Biological Chemistry 277 (13), pp. 11521 - 11526 (2002 ...

The active-site protonation state is crucial to the reductive mechanism of Escherichia coli thioredoxin, which involves a nucleophilic attack by the thiolate form of Cys32. We have calculated the titration properties of the active-site residues using a continuum electrostatic model, the X-ray structure of the oxidized protein, and ensembles of NMR structures of the oxidized and reduced protein. Protein dipoles, especially the SH dipole of Cys35, can provide sufficient stabilization of the Cys32 thiolate to account for its low experimental pKa (approximately 7.4), but this effect is very sensitive to local conformational variations. The experimental finding that Cys32 titrates at a lower pH than Cys35 is explained by the latters deeper burial from solvent exposure, and stronger interaction with the carboxylate of Asp26, and not by helix dipoles or positively charged side chains. The calculated very strong interaction between Cys32 and Cys35 in their thiolate forms implies that their titration ...

The thioredoxin process is made up of the 12-kDa protein thioredoxin and its companion thioredoxin reductase.[159] Proteins associated with thioredoxin are present in all sequenced organisms. Crops, for instance Arabidopsis thaliana, have a particularly great variety of isoforms.[160] The Energetic internet site of thioredoxin consists of two neighboring cysteines, as A part of a highly conserved CXXC motif, that can cycle concerning an Energetic dithiol sort (diminished) and an oxidized disulfide kind ...

Oncotarget | https://doi.org/10.18632/oncotarget.5132 Fang-Yuan Shao, Zhi-Yun Du, Dong-Lei Ma, Wen-Bo Chen, Wu-Yu Fu, Bi-Bo Ruan, Wen Rui, Jia-Xuan Zhang, Sheng Wang, Nai Sum Wong, Hao Xiao, Man-Mei Li, Xiao...

The Thioredoxin Assay is a thioredoxin ELISA that can measure soluble human thioredoxin protein in serum, EDTA-plasma, urine or cell culture

The Thioredoxin Assay is a thioredoxin ELISA that can measure soluble human thioredoxin protein in serum, EDTA-plasma, urine or cell culture

Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

Purine and Pyrwhat bond links the base and sugar together in a Nt?Sam donates what?PAPS donates what|bond - N-glycosidic linkSam - methylPAPS - a sulfate donorPUR and PYRIMP - whats the baseWhat does thioredoxin do?|Base - HThioredoxin - co-enz reduces ribonucleotide reductase, an electron donoris reduced by NADPH in thioredoxin reductase

Human Thioredoxin ELISA Kit PicoKine™ (96 Tests). Quantitate Human TXN in cell culture supernatants, cell lysates, serum and plasma (heparin, EDTA).. Sensitivity: 10pg/ml.

Gentaur molecular products has all kinds of products like :search , Abfron \ Thioredoxin 1, Yeast, Protein \ LF-P0036 for more molecular products just contact us

Cellular processesCellular processesDetoxificationarsenate reductase (thioredoxin) (TIGR02691; EC 1.20.4.-,3.1.3.48; HMM-score: 28.3) ...

Cellular processesCellular processesDetoxificationarsenate reductase (thioredoxin) (TIGR02691; EC 1.20.4.-,3.1.3.48; HMM-score: 21.3) ...

QUESTIONS & ANSWERS: THE BASICS What are the most commonly reported benefits of TRX2®? The most common benefits reported by those who regularly take TRX2® i

Our website is authorized by eBay to help you find the Trx Cleats you are searching for and present them to you. If you dont immediately see the Trx Cleats

Methods and Results-In mice, α-MHC-restricted Cre-mediated Txnrd2 deficiency, induced by tamoxifen (Txnrd2−/−ic), aggravated systolic dysfunction and cardiomyocyte cell death after ischemia (90 minutes) and reperfusion (24 hours). Txnrd2−/−ic was accompanied by a loss of mitochondrial integrity and function, which was resolved on pretreatment with the reactive oxygen species scavenger N-acetylcysteine and the mitochondrial permeability transition pore blocker cyclosporin A. Likewise, Txnrd2 deletion in embryonic endothelial precursor cells and embryonic stem cell-derived cardiomyocytes, as well as introduction of Txnrd2-shRNA into adult HL-1 cardiomyocytes, increased cell death on hypoxia and reoxygenation, unless N-acetylcysteine was coadministered.. ...

TY - JOUR. T1 - Modulation of thioredoxin reductase-2 expression in EAhy926 cells. T2 - Implications for endothelial selenoprotein hierarchy AU - Crane, Michael S.. AU - Howie, Alexander F. AU - Arthur, John R. AU - Nicol, Fergus. AU - Crosley, Lynne K.. AU - Beckett, Geoffrey J.. PY - 2009/10. Y1 - 2009/10. N2 - Background: We examined the expression of the mitochondrial selenoenzyme TrxR2 in the endothelial cell line EAhy926 under conditions known to modify its cytoplasmic counterpart TrxR1.Methods: Cells were cultured with varying concentrations of selenite, sulforaphane or the Ca2+ ionophore A23187 for 72-h, prior to assay of TrxR concentration and activity. Further cultures underwent prolonged (7-day) Se-depletion before selenoprotein measurement.Results: In Se-deficient cultures, neither Se, A23187 or sulforaphane affected TrxR2 concentration, while these treatments induced TrxR1 concentration (p,0.05). When co-incubated, optimal concentrations of Se (40 nM) and sulforaphane (4 mu M) only ...

Trx2 (mitochondrial thioredoxin) is an antioxidant and anti-apoptotic factor essential for cell viability. Trx1 (cytoplasmic thioredoxin) is a co-factor and regulator of redox-sensitive transcription factors such as the GR (glucocorticoid receptor) and NF-κB (nuclear factor κB). Both transcription factors have been detected in mitochondria and a role in mitochondrial transcription regulation and apoptosis has been proposed. In the present study, we show using SPR (surface plasmon resonance) and immunoprecepitation that GR and the p65 subunit of NF-κB are Trx2-interacting proteins. The interaction of Trx2 with GR is independent of the presence of GR ligand and of redox conditions. The p65 subunit of NF-κB can interact with Trx2 in the oxidized, but not the reduced, form. Using HEK (human embryonic kidney)-293 cell lines with increased or decreased expression of Trx2, we show that Trx2 modulates transcription of GR and NF-κB reporter genes. Moreover, Trx2 overexpression modulates the mRNA ...

Locus: txnrd1 Allelic designation: txnrd1[cond] Homozygous condition: txnrd1[cond/cond] mRNA designation: Txnrd1 mRNA (also called TrxR1 mRNA, Tr1 mRNA) Protein designation: Txnrd1 (also called TrxR1, Tr1) Origin: Developed on a 129XI ES cell background and backcrossed > 10 generations onto C57Bl/6J. The purely backcrossed line was lost during elimination of MNV from the colony and the line was recovered from individuals that had some ancestors with less defined strain backgrounds (JAX stock #s 007576, 004847, and 003574). These are being continuously backcrossed onto C57Bl/6J. Status: Active. MNV-free. Related disease: Congenital, Hereditary, and Neonatal Diseases and Abnormalities Availability: Heterozygotes of either sex are freely available for unrestricted non-profit research use by qualified programs/institutions. Recipient will pay per diem for production of one liter and will cover costs for health reports and shipping. Thioredoxin reductase 1 - Conditional Null is an eagle-i resource

Domain architectures containing both YVTN repeat-like/Quinoprotein amine dehydrogenase and C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase in Malus domestica v196. Links to architectures containing these domain pairs in other groups of genomes are provided. Domain pairs which are not adjacent can be added/removed.

Reaktivität: Human, Maus, Ratte. 5 verschiedene TXNRD2 ELISA Kits vergleichen. Alle direkt auf antikoerper-online.de bestellbar!

Fig. 3 shows the spectra recorded during the time course of the experiment with 5 eq of NADPH. Spectrum 1 is that of Eox. The pattern appears much like that seen in the reduction of GR with only one molecule of NADPH reacting with the enzyme (cf. figure 3 of ref. 31). The pattern is completely different from that seen with eTrxR, in which two molecules of NADPH react (ref. 37 and B. W. Lennon and C. H. Williams, unpublished work). Spectrum 5 is predominantly that of the thiolate-flavin charge transfer complex (24). Please note, from the early work of Massey et al. (38) on LipDH, that the main peak of the thiolate-flavin charge transfer complex was distinctly blue-shifted relative to Eox. This also applies to GR (33-34). In spectrum 4, the A680 nm is higher than in spectrum 5, which indicates the presence of the FADH−-NADP+ charge transfer complex (39). This species is not favored under the conditions shown because the NADP+ is displaced by excess NADPH. Between 55 and 400 ms, the absorbance in ...

Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). The nucleotide sequence of Saccharomyces cerevisiae chromosome IV. Nature 387:75-78.9169867 ...

Complete information for TXNRD2 gene (Protein Coding), Thioredoxin Reductase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

Origami(DE3)pLysS Glycerol Stock from Novagen,Origami host strains are K-12 derivatives that have mutations in both the thioredoxin reductase (trxB) and glutathione reductase (gor) genes, which greatly enhances disulfide bond formation in the cytoplasm. Studies have shown that expression in Origami(DE3) yielded 10-fold more active protein than,biological,biology supply,biology supplies,biology product

References for Abcams Recombinant |em|S. cerevisiae|/em| Thioredoxin / TRX protein (ab82731). Please let us know if you have used this product in your…