Characterization of human thioredoxin system and the potential cellular responses encoded to observe the Thioredoxin-Trx1 reversibly regulated redox sites.

Thioredoxin: human TXN, is a oxidoreductase enzyme in the status of a 12 kDa cellular redox-reductase reaction (70-kDa in bacteria, fungi and plants), a cellular defense mechanisms against oxidative stress of the cell, and numerous cytosolic processes in all cells. Txn1 is a pleiotropic cellular causative gene factor which has numerous functions. Chromosome 3p12-p11 shares homology with human thioredoxin gene Trx1, Trx80: 9q31.3; (§, ). Here the following reaction is the possible mechanisms of the thioredoxin-catalyzed reduction and re-oxidation of its characteristic cystine residues.

 The TXN gene, consists of the first of 5 exons  separated by 4 introns and is located 22 bp downstream from the only known basal TATA box factor TBP-2/TXNIP vitamin D(3) up-regulated protein 1-VDUP1, negatively regulating TRX function, and exhibiting cellular growth and suppressive (cancer) activity.

 TRX inhibited Apoptosis signal-regulating kinase-ASK1 kinase (MAP3K5), activity, dependent on two cysteine residues in the N-terminal domain of ASK1 on the redox (regulation) forming intramolecular disulfide between the status of TXN. Two cysteine residues (N-terminal C32S or Trx C-terminal C35S and/or a Trx-CS double mutation) remaining trapped with the Ask1 as a inactive high-molecular-mass complex, blocking its reduction to release Trx from ASK1 depends on intramolecular disulfide to catalyze the reduction of the redox regulation of TRX. Trx and a thiol-specific antioxidant thioredoxin peroxidase-2 orthologue (Tpx) in various* biological phenomena is involved in redox regulation (NADPH-the thioredoxin system) of the dithioldisulfide active site.

 An apoptosis signal transduction pathway through stimulus-coupled S-nitrosation of cysteine, has two critical (almost identical) cysteine residues in the Trx redox-active center. Where a disulfide exchange reaction between oxidized Txnip [thioredoxin-interacting protein; mouse Vdup1] and reduced TXN occurs. Txnip (-when used to investigate cardiac hypertrophy) is a regulator of biomechanical signaling. Hydrogen peroxide downregulated expression is the only known function associated with an incomplete TRX response through stimulus-coupled S-nitrosation of cysteine residues. Peroxiredoxin PrxIII-‘Tpx1 serves as’ a tandem (dimer) thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2-TxnR1), are Trx mechanisms of the two electron donor system.

 Cytosolic caspase-3 was maintained by S-nitrosation, consistent with cytosolic and mitochondria, Trx-1 contain equivalent Trx systems, which enabled identification of caspase-3 substrates where TXN may regulate S-nitrosation with the redox center of TXN specific (C73S) to Nitric oxide-NO cellular signal transduction associated with  inhibition of apoptosis or mutant Trx neurotoxicity. EGCG° (epigallocatechin-3-gallate) may be useful in cell survival on caspase-(3_dependent)-neuronal apoptosis where a membrane reaction, a reduced hormesis consequently triggers the apoptosis effect and direct or indirectly numerous protein-protein interactions and basal cofactor substrates which occur between caspase-3 and Trx. The effect of  exercise training via activation of caspase-3 has a decrease in superoxide, and increase of Trx-1 levels in brain. Protection from mechanical stress identified, NSF- N-ethylmaleimide transduced into a TRX peroxidase response via mechanical force of a typical transnitrosylated  Casp3, attenuated  Trx1 2-cysteines which directly transnitrosylates Peroxiredoxins. C32S ( redox potential) was identified as thiol-reducing system, which lacks reducing activitiy (nonactive C69S and Cys(73) both monomeric) or a reversible regulating function in the presence of caspase 3 activity is a process found in the presence of NADP and TrxR.

 There are at least two thioredoxin reductive or oxidative** (reductases / peroxiredoxin) regulated systems. The mutant 32CXXC35′ motif of thioredoxin nitrosation sites, where two cysteines are separated by two other amino acids, and codes for an additional three cysteines where the Cys 62/C73S (not monomers) sidechain the active site of Cys 62 also can form several disulphides and be modified by the carbon-bonded sulfhydryl, where the  thiol reducing system, was evident.

 Intracellular TRX/ADF (Adult T cell leukemia-derived factor HTLV-I) can regulate cell nuclei, protein-nucleic acid interactions. Transnitrosylation and denitrosylation is a reversible Post-translational (PTM) altered by redox modification of different cysteine residues (C3273S) in Trx1, S-nitrosation or its interactions with other proteins and DNA-dependent nuclear processes. NFKappaB REF-1 redox factor 1  involving Cys62, in the two complexes, are correlated as N ⇔ C-terminal responses with  TRX-1 nuclear migration through the reduction of a pleiotropic cellular factor. TRX redox activities of protein-protein cysteine residues is identical to a DNA repair enzyme through various cytoplasmic aspects mediating cellular responses in the ‘nucleus‘. The DNA binding activity and transactivation of ‘AP-1‘ activator proteins (JUNproto* oncogen) depends on the reduction between the sulfhydryl of cysteines to keep Trx1 reduced, is demonstrated in cells. Selenium-dependent seleneocysteine based peroxidase reductants, reduce Lipoic acid stereoselectively under the same TRX rather than GSH-PX1-glutathione peroxidase oxidative stress conditions. Senseantisense (TRX) antiapoptoitic interactions nitrosylated at Cys73 are attenuated and integrated into the host cell under oxidative conditions, in which thioredoxin (TRX), and a cellular TRX reducing catalyst agent (DTT-redox reagent) to S-nitrosoglutathione (GSNO) intermediate via cysteine residues ‘influences’-catalyst mediated (post-translational modifications) PTMs; and possibly 1,25D(3)-Calcitriol; NADPH:oxygen oxidoreductases correlated with  (Trx-1) a protein disulfide oxidoreductase.

 Peroxynitrite** converts superoxide to hydrogen peroxide (H2O2)-induced Trx degradation, in concentrations that detoxify reactive oxygen species (ROS), demonstrated by superoxide dismutases (SOD)-catalyse and peroxidases, converting superoxide to hydrogen peroxide which is decomposed to water plus oxidized thioredoxin to maintain the anti-apoptotic (C62) function of thioredoxins additional five sulfhydryl group thiols in the fully reduced state, in a Trx-dependent manner. Reactive oxygen species (ROS) can cause DNA damage, and uncontrolled cellular proliferation or apoptotic death of cancer cells.The NADPH (Trx system) oxidizing substrate-dependent reduction of Thioredoxin reductase-TrxR has a reversibly modulated role in restoration of GR (glucocorticoid receptor) function, and DNA binding domain.

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NADP  1XOB Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases. PMID: 14503974 the molecular mechanisms underlying functional the TR1-Trx1 redox pair and structure determination of an active site of the ligand mini-stromelysin-1 TR-1 augmentation composed of TR (Trx reductase activities) the main function of TR1 here is to reduce Trx1 also validated as a ligand PMID; 23105116, have been characterized between ligand bound and free structures PMID; 20661909, for specific isolation of  C35S selenocysteine (SeCys)-containing protein shows the best docking position found, consists of one strand at position [PROline]76:A.side chain: from the four-stranded antiparallel beta sheet was with wild-type TrxA C32-35S located in the Thioredoxin_fold (PDB accession code 1XOB: PMID: 15987909) , TR1 as a single hybrid PDB (Cys32 and Cys35 for Trx1, and for TR1) pubmed/20536427 investigate the possible mechanism. {{{During this reduction, the thiol-disulfide oxidoreductase thioredoxin-1 (Trx1) linked thioredoxin reductase (TRR2) a working model suggesting that deregulation of the thioredoxin reductase TXNRD1 and|}}} its characteristic substrate thioredoxin (TR [1]), concomitant with diminution of their Trx reductase cellular contents is highly related to glutamate excitotoxicity PMID: 20620191; TR1: hStromelysin-1

enlargeNADPAn ET (electron transfer) mechanism from NADPH and another  enzyme thioredoxin reductase pubmed/17369362 the charged residue aspartate D60 (Fig.2) pubmed/9369469/ plays a role in the degradation of proteins and in apoptotic processes induced by oxidative stress  PMID: 16263712  to determine the effect of  zerumbone ZSD1 Zerumbone-loaded nanostructured lipid carriers Int J        Nanomedicine. 2013;8:2769-81. doi: 10.2147/IJN.S45313. Epub 2013        Aug 2 PMID:23946649 [PubMed - indexed for MEDLINE]        PMCID:PMC3739459 (from shampoo ginger; Name: Alpha-humulene) on NADP-malate dehydrogenase, TRX dependent oxidoreductase, that NADPH does not contain. Monomeric Thioredoxin is present across phyla from humans to plants PMID: 20661909, 11012661 mediated in vivo by thioredoxin-catalyzed reduction and re-oxidation of cystine residues PubMed id: 10196131 (Fig.3-PDB: 1CIV, NADP). Trx is able to activate vegetal NADP-malate dehydrogenase PMID: 3170595 (excluding the initial methionine) Met is located at the N-terminal – PMID: 11807942, 2684271. A relatively rigid local configuration for the aspartate residue D60 is found but which implies that the (NADP-TrxR) protein fluctuates among the numerous protein models and mutations over the time scales fluctuations.

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Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose.Du Y, Zhang H, Lu J, Holmgren A.J Biol Chem. 2012 Nov 2;287(45):38210-9. doi: 10.1074/jbc.M112.392225. Epub 2012 Sep 13.PMID:22977247

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Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose.Du Y, Zhang H, Lu J, Holmgren A.J Biol Chem. 2012 Nov 2;287(45):38210-9. doi: 10.1074/jbc.M112.392225. Epub 2012 Sep 13.PMID:22977247

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Small changes huge impact: the role of thioredoxin 1 in the regulation of apoptosis by S-nitrosylation.Li H, Wan A, Xu G, Ye D.Acta Biochim Biophys Sin (Shanghai). 2013 Mar;45(3):153-61. doi: 10.1093/abbs/gms103. Epub 2012 Dec 4. Review.PMID:23212077

Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach.Wu C, Parrott AM, Liu T, Jain MR, Yang Y, Sadoshima J, Li H.J Proteomics. 2011 Oct 19;74(11):2498-509. doi: 10.1016/j.jprot.2011.06.001. Epub 2011 Jun 17.PMID:21704743

Redox regulatory mechanism of transnitrosylation by thioredoxin.Wu C, Liu T, Chen W, Oka S, Fu C, Jain MR, Parrott AM, Baykal AT, Sadoshima J, Li H.Mol Cell Proteomics. 2010 Oct;9(10):2262-75. doi: 10.1074/mcp.M110.000034. Epub 2010 Jul 21.PMID:20660346

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The thioredoxin system in retroviral infection and apoptosis.Masutani H, Ueda S, Yodoi J.Cell Death Differ. 2005 Aug;12 Suppl 1:991-8. Review.PMID:15818395

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Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose.Du Y, Zhang H, Lu J, Holmgren A.J Biol Chem. 2012 Nov 2;287(45):38210-9. doi: 10.1074/jbc.M112.392225. Epub 2012 Sep 13.PMID:22977247

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Tagging single-nucleotide polymorphisms in antioxidant defense enzymes and susceptibility to breast cancer.Cebrian A, Pharoah PD, Ahmed S, Smith PL, Luccarini C, Luben R, Redman K, Munday H, Easton DF, Dunning AM, Ponder BA.Cancer Res. 2006 Jan 15;66(2):1225-33.PMID:16424062

Interacting with thioredoxin-1–disease or no disease?Zschauer TC, Matsushima S, Altschmied J, Shao D, Sadoshima J, Haendeler J.Antioxid Redox Signal. 2013 Mar 20;18(9):1053-62. doi: 10.1089/ars.2012.4822. Epub 2012 Sep 24. Review.PMID:22867430

Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium.Gallegos A, Berggren M, Gasdaska JR, Powis G.Cancer Res. 1997 Nov 1;57(21):4965-70.PMID:9354464

Selenium and the thioredoxin and glutaredoxin systems.Björnstedt M, Kumar S, Björkhem L, Spyrou G, Holmgren A.Biomed Environ Sci. 1997 Sep;10(2-3):271-9. Review.PMID:9315320

Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity.Urig S, Lieske J, Fritz-Wolf K, Irmler A, Becker K.FEBS Lett. 2006 Jun 26;580(15):3595-600. Epub 2006 May 23.PMID:16750198

Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose.Du Y, Zhang H, Lu J, Holmgren A.J Biol Chem. 2012 Nov 2;287(45):38210-9. doi: 10.1074/jbc.M112.392225. Epub 2012 Sep 13.PMID:22977247

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Thioredoxin reductase regulates AP-1 activity as well as thioredoxin nuclear localization via active cysteines in response to ionizing radiation.Karimpour S, Lou J, Lin LL, Rene LM, Lagunas L, Ma X, Karra S, Bradbury CM, Markovina S, Goswami PC, Spitz DR, Hirota K, Kalvakolanu DV, Yodoi J, Gius D.Oncogene. 2002 Sep 12;21(41):6317-27.PMID:12214272

Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system.Makino Y, Okamoto K, Yoshikawa N, Aoshima M, Hirota K, Yodoi J, Umesono K, Makino I, Tanaka H.J Clin Invest. 1996 Dec 1;98(11):2469-77.PMID:8958209

Thioredoxin in the endocrine response to stress.Tanaka H, Makino Y, Okamoto K.Vitam Horm. 1999;57:153-75. Review.PMID:10232049

Role of thioredoxin reductase 1 and thioredoxin interacting protein in prognosis of breast cancer.Cadenas C, Franckenstein D, Schmidt M, Gehrmann M, Hermes M, Geppert B, Schormann W, Maccoux LJ, Schug M, Schumann A, Wilhelm C, Freis E, Ickstadt K, Rahnenführer J, Baumbach JI, Sickmann A, Hengstler JG.Breast Cancer Res. 2010;12(3):R44. doi: 10.1186/bcr2599. Epub 2010 Jun 28.PMID:20584310

Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening.Lysell J, Stjernholm Vladic Y, Ciarlo N, Holmgren A, Sahlin L.Gynecol Endocrinol. 2003 Aug;17(4):303-10.PMID:14503974

Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.Aragão AZ, Nogueira ML, Granato DC, Simabuco FM, Honorato RV, Hoffman Z, Yokoo S, Laurindo FR, Squina FM, Zeri AC, Oliveira PS, Sherman NE, Paes Leme AF.J Biol Chem. 2012 Dec 14;287(51):43071-82. doi: 10.1074/jbc.M112.364513. Epub 2012 Oct 26.PMID:23105116

Thioredoxin and glutaredoxin system proteins-immunolocalization in the rat central nervous system.Aon-Bertolino ML, Romero JI, Galeano P, Holubiec M, Badorrey MS, Saraceno GE, Hanschmann EM, Lillig CH, Capani F.Biochim Biophys Acta. 2011 Jan;1810(1):93-110. doi: 10.1016/j.bbagen.2010.06.011. Epub 2010 Jul 8.PMID:20620191

Dissection of complex protein dynamics in human thioredoxin.Qiu W, Wang L, Lu W, Boechler A, Sanders DA, Zhong D.Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5366-71. Epub 2007 Mar 16.PMID:17369362

Cathepsin D and H2O2 stimulate degradation of thioredoxin-1: implication for endothelial cell apoptosis.Haendeler J, Popp R, Goy C, Tischler V, Zeiher AM, Dimmeler S.J Biol Chem. 2005 Dec 30;280(52):42945-51. Epub 2005 Nov 1.PMID:16263712

Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction.Carr PD, Verger D, Ashton AR, Ollis DL.Structure. 1999 Apr 15;7(4):461-75.PMID:10196131

Cloning and expression of a cDNA for human thioredoxin.Wollman EE, d’Auriol L, Rimsky L, Shaw A, Jacquot JP, Wingfield P, Graber P, Dessarps F, Robin P, Galibert F, et al.J Biol Chem. 1988 Oct 25;263(30):15506-12.PMID:3170595

A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin.Forman-Kay JD, Clore GM, Driscoll PC, Wingfield P, Richards FM, Gronenborn AM.Biochemistry. 1989 Aug 22;28(17):7088-97.PMID:2684271

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