Regulacja układu zależnego od tioredoksyny jako element farmakoterapii w chorobach z zaburzeniami równowagi redoks
References
- Ahsan M.K., Lekli I., Ray D., Yodoi J., Das D.K.: Redox regulation of cell survival by the thioredoxin superfamily: An implication of redox gene therapy in the heart. Antioxid. Redox Signal., 2009; 11: 2741–2758
- An N., Kang Y.: Thioredoxin and hematologic malignancies. W: Advances in Cancer Research, t. 122, red.: D.M. Townsend, K.D. Tew. Academic Press, London, 2014, 245–279
- Arnér E.S.: Focus on mammalian thioredoxin reductases – important selenoproteins with versatile functions. Biochim. Biophys. Acta, 2009; 1790: 495–526
- Arnér E.S.: Selenocysteine insertion and reactivity: Mammalian thioredoxin reductases in relation to cellular redox signaling. W: Cellular Implications of Redox Signaling, red.: C. Gitler, A. Danon. Imperial College Press, London 2003, 27–45
- Avval F.Z., Holmgren A.: Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase. J. Biol. Chem., 2009; 284: 8233–8240
- Baker A.F., Adab K.N., Raghunand N., Chow H., Stratton S.P., Squire S.W., Boice M., Pestano L.A., Kirkpatrick D.L., Dragovich T.: A phase IB trial of 24-hour intravenous PX-12, a thioredoxin-1 inhibitor, in patients with advanced gastrointestinal cancers. Invest. New Drugs, 2013; 31: 631–641
- Baker A.F., Dragovich T., Tate W.R., Ramanathan R.K., Roe D., Hsu C.H., Kirkpatrick D.L., Powis G.: The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma. J. Lab. Clin. Med., 2006; 147: 83–90
- Berdicevsky I., Kaufman G., Newman D.J., Horwitz B.A.: Preliminary study of activity of the thioredoxin inhibitor pleurotin against Trichophyton mentagrophytes: A novel anti-dermatophyte possibility. Mycoses, 2009; 52: 313–317
- Berndt C., Lillig C.H., Holmgren A.: Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim. Biophys. Acta, 2008; 1783: 641–650
- Bignon E., Allega M.F., Lucchetta M., Tiberti M., Papaleo E.: Computational structural biology of S-nitrosylation of cancer targets. Front. Oncol., 2018; 8: 272
- Bilska A., Kryczyk A., Włodek L.: Różne oblicza biologicznej roli glutationu. Postępy Hig. Med. Dośw., 2007; 61: 438–453
- Brandstaedter C., Fritz-Wolf K., Weder S., Fischer M., Hecker B., Rahlfs S., Becker K.: Kinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms., FEBS J., 2018; 285; 542–558
- Cai W., Zhang B., Duan D., Wu J., Fang J.: Curcumin targeting the thioredoxin system elevates oxidative stress in HeLa cells. Toxicol. Appl. Pharmacol., 2012; 262: 341–348
- Chen X., Tang W., Liu S., Yu L., Chen Z.: Thioredoxin-1 phosphorylated at T100 is needed for its anti-apoptotic activity in HepG2 cancer cells. Life Sci., 2010; 87, 254–260
- Chondrogianni N., Petropoulos I., Grimm S., Georgila K., Catalgol B., Friguet B., Grune T., Gonos, E.S.: Protein damage, repair and proteolysis. Mol. Aspects Med., 2014; 35: 1–71
- Circu M.L., Aw T.Y.: Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med., 2010; 48: 749–762
- Citta A., Folda A., Scutari G., Cesaro L., Bindoli A., Rigobello, M.P.: Inhibition of thiore8doxin reductase by lanthanum chloride. J. Inorg. Biochem., 2012; 117: 18–24
- Collet J.F., Messens J.: Structure, function, and mechanism of thioredoxin proteins. Antioxid. Redox Signal., 2010; 13: 1205–1216
- Cortes-Bratti X., Bassères E., Herrera-Rodriguez F., Botero-Kleiven S., Coppotelli G., Andersen J.B., Masucci M.G., Holmgren A., Chaves-Olarte E., Frisan T., Avila-Carino J.: Thioredoxin 80-activated-monocytes (TAMs) inhibit the replication of intracellular pathogens. PLoS One, 2011; 6: e16960
- Cutillas N., Yellol G.S., de Haro C., Vicente C., Rodríguez V., Ruiz J.: Anticancer cyclometalated complexes of platinum group metals and gold. Coord. Chem. Rev., 2013; 257: 2784–2791
- de Oliveira K.N., Andermark V., Onambele L.A., Dahl G., Prokop A., Ott, I.: Organotin complexes containing carboxylate ligands with maleimide and naphthalimide derived partial structures: TrxR inhibition, cytotoxicity and activity in resistant cancer cells. Eur. J. Med. Chem., 2014; 87: 794–800
- Dmitrenko O., Orlova T., Terenetskaya I.: Medium controlled photochemistry of provitamin D: From solutions to liquid crystals. J. Mol. Liq., 2018; 267: 428–435
- Dobrovolska O., Rychkov G., Shumilina E., Nerinovski K., Schmidt A., Shabalin K., Yakimov A., Dikiy A.: Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin. J. Biomed. Biotechnol., 2012; 2012: 586539
- Dóka É., Pader I., Bíró A., Johansson K., Cheng Q., Ballagó K., Prigge J.R., Pastor-Flores D., Dick T.P., Schmidt E.E., Arnér E.S., Nagy P.: A novel persulfide detection method reveals protein persulfideand polysulfide-reducing functions of thioredoxin and glutathione systems. Sci. Adv., 2016; 2: e1500968
- Ellgaard L. Ruddock L.W.: The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Rep., 2005; 6: 28–32
- Fang J., Holmgren A.: Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. J. Am. Chem. Soc., 2006; 128: 1879–1885
- Fujiwara N., Fujii T., Fujii J., Taniguchi N.: Roles of N-terminal active cysteines and C-terminal cysteine-selenocysteine in the catalytic mechanism of mammalian thioredoxin reductase. J. Biochem., 2001; 129: 803–812
- Galligan J.J., Petersen D.R.: The human protein disulfide isomerase gene family. Hum. Genomics, 2012; 6: 6
- Gandin V., Fernandes A.P.: Metal-and semimetal-containing inhibitors of thioredoxin reductase as anticancer agents. Molecules, 2015; 20: 12732–12756
- Gaschler M.M., Stockwell B.R.: Lipid peroxidation in cell death. Biochem. Biophys. Res. Commun., 2017; 482: 419–425
- Ghezzi P.: Protein glutathionylation in health and disease. Biochim. Biophys. Acta, 2013; 1830: 3165–3172
- Gil-Bea F., Akterin S., Persson T., Mateos L., Sandebring A., Avila-Cariño J., Gutierrez-Rodriguez A., Sundström E., Holmgren A., Winblad B., Cedazo-Minguez A.: Thioredoxin-80 is a product of alpha-secretase cleavage that inhibits amyloid-beta aggregation and is decreased in Alzheimer’s disease brain. EMBO Mol. Med., 2012; 4: 1097–1111
- Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Inoue M., Tanaka A., Sugano S., Kigawa T., Yokoyama S.: Solution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein. Proteins, 2010; 78: 2176–2180
- Gromer S., Urig S., Becker K.: The thioredoxin system – from science to clinic. Med. Res. Rev., 2004; 24: 40–89
- Hashemy S.I., Ungerstedt J.S., Avval F.Z., Holmgren A.: Motexafin gadolinium, a tumor-selective drug targeting thioredoxin reductase and ribonucleotide reductase. J. Biol. Chem., 2006; 281: 10691–10697
- Hatahet F., Ruddock L.W.: Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal., 2009; 11: 2807–2850
- Hickey J.L., Ruhayel R.A., Barnard P.J., Baker M.V., Berners-Price S.J., Filipovska A.: Mitochondria-targeted chemotherapeutics: The rational design of gold (I) N-heterocyclic carbene complexes that are selectively toxic to cancer cells and target protein selenols in preference to thiols. J. Am. Chem. Soc., 2008; 130: 12570–12571
- Holmgren A., Lu J.: Thioredoxin and thioredoxin reductase: Current research with special reference to human disease. Biochem. Biophys. Res. Commun., 2010; 396: 120–124
- Hruza L.L., Pentland A.P.: Mechanisms of UV–induced inflammation. J. Invest. Dermatol., 1993; 100: S35–S41
- Ishii T., Funato Y., Miki H.: Thioredoxin-related protein 32 (TRP32) specifically reduces oxidized phosphatase of regenerating liver (PRL). J. Biol. Chem., 2013; 288: 7263–7270
- Jiménez A., Zu W., Rawe V.Y., Pelto-Huikko M., Flickinger C.J., Sutovsky P., Gustafsson J.Å. Oko R., Miranda-Vizuete A.: Spermatocyte/spermatid-specific thioredoxin-3, a novel Golgi apparatus-associated thioredoxin, is a specific marker of aberrant spermatogenesis. J. Biol. Chem., 2004; 279: 34971–34982
- Jones D.A.: Rosacea, reactive oxygen species, and azelaic acid. J. Clin. Aesthet. Dermatol., 2009; 2: 26–30
- Ju Y., Wu L., Yang G.: Thioredoxin 1 regulation of protein S-desulfhydration. Biochem. Biophys. Rep., 2016; 5: 27–34
- Kakkar P., Singh B.K.: Mitochondria: A hub of redox activities and cellular distress control. Mol. Cell. Biochem., 2007; 305: 235–253
- Karlenius T.C., Tonissen, K.F.: Thioredoxin and cancer:A role for thioredoxin in all states of tumor oxygenation. Cancers, 2010; 2: 209–232
- Korkina L.: Metabolic and redox barriers in the skin exposed to drugs and xenobiotics. Expert Opin. Drug Metab. Toxicol., 2016; 12: 377–388
- Lee S., Kim S.M., Lee R.T.: Thioredoxin and thioredoxin target proteins: From molecular mechanisms to functional significance. Antioxid. Redox Signal., 2013; 18: 1165–1207
- Lehmann B., Meurer M.: Vitamin D metabolism. Dermatol. Ther., 2010; 23, 2–12
- Li G.Z., Liang H.F., Liao B., Zhang L., Ni Y.A., Zhou H.H., Zhang E.L., Zhang B.X., Chen X.P.: PX-12 inhibits the growth of hepatocelluar carcinoma by inducing S-phase arrest, ROS-dependent apoptosis and enhances 5-FU cytotoxicity. Am. J. Transl. Res., 2015; 7: 1528–1540
- Li H., Xu C., Li Q., Gao X., Sugano E., Tomita H., Yang L., Shi S.: Thioredoxin 2 offers protection against mitochondrial oxidative stress in H9c2 cells and against myocardial hypertrophy induced by hyperglycemia. Int. J. Mol. Sci., 2017; 18: 1958
- Liao J., Wang K., Yao W., Yi X., Yan H., Chen M., Lan X.: Cloning, expression and antioxidant activity of a thioredoxin peroxidase from Branchiostoma belcheri tsingtaunese. PLoS One, 2017; 12: e0175162
- Lillig C.H., Holmgren A.: Thioredoxin and related molecules – from biology to health and disease. Antioxid. Redox Signal., 2007; 9: 25–47
- Lu J., Papp L.V., Fang J., Rodriguez-Nieto S., Zhivotovsky B., Holmgren A.: Inhibition of mammalian thioredoxin reductase by some flavonoids: Implications for myricetin and quercetin anti-cancer activity. Cancer Res., 2006; 66: 4410–4418
- Lu Y., Wang X., Liu Z., Jin B., Chu D., Zhai H., Zhang F., Li K., Ren G., Miranda-Vizuete A., Guo X., Fan D.: Identification and distribution of thioredoxin-like 2 as the antigen for the monoclonal antibody MC3 specific to colorectal cancer. Proteomics, 2008; 8: 2220–2229
- Maillet A., Pervaiz S.: Redox regulation of p53, redox effectors regulated by p53: A subtle balance. Antioxid. Redox Signal., 2012; 16: 1285–1294
- Maulik N., Das D.K.: Emerging potential of thioredoxin and thioredoxin interacting proteins in various disease conditions. Biochim. Biophys. Acta, 2008; 1780: 1368–1382
- Mukherjee A., Martin S.G.: The thioredoxin system: A key target in tumour and endothelial cells. Br. J. Radiol., 2008; 81: S57–S68
- Mura P., Camalli M., Bindoli A., Sorrentino F., Casini A., Gabbiani C., Corsini M., Zanello P., Rigobello M.P., Messori L.: Activity of rat cytosolic thioredoxin reductase is strongly decreased by trans-[bis (2-amino-5-methylthiazole) tetrachlororuthenate (III)]: First report of relevant thioredoxin reductase inhibition for a ruthenium compound. J. Med. Chem., 2007; 50: 5871–5874
- Ng H.L., Chen S., Chew E.H., Chui W.K.: Applying the designed multiple ligands approach to inhibit dihydrofolate reductase and thioredoxin reductase for anti-proliferative activity. Eur. J. Med. Chem., 2016; 115: 63–74
- Oehninger L., Küster L.N., Schmidt C., Muñoz-Castro A., Prokop A., Ott I.: A chemical-biological evaluation of rhodium (I) N-heterocyclic carbene complexes as prospective anticancer drugs. Chem. Eur. J., 2013; 19: 17871–17880
- Oguro A., Imaoka S.: Thioredoxin-related transmembrane protein 2 (TMX2) regulates the Ran protein gradient and importin-β-dependent nuclear cargo transport. Sci. Rep., 2019; 9: 15296
- Oka O.B., Bulleid N.J.: Forming disulfides in the endoplasmic reticulum. Biochim. Biophys. Acta, 2013; 1833: 2425–2429
- Orlova T.N., Terenetskaya I.P.: Possible use of provitamin D3 photoisomerization for spectral dosimetry of bioactive antirachitic UV radiation. J. Appl. Spectrosc., 2009; 76, 240–244
- Ortego L., Cardoso F., Martins S., Fillat M.F., Laguna A., Meireles M., Villacampa M.D., Gimeno M.C.: Strong inhibition of thioredoxin reductase by highly cytotoxic gold (I) complexes. DNA binding studies. J. Inorg. Biochem., 2014; 130: 32–37
- Palanisamy R., Bhatt P., Kumaresan V., Chaurasia M.K., Gnanam A.J., Pasupuleti M., Kasi M., Arockiaraj J.: A redox active site containing murrel cytosolic thioredoxin: Analysis of immunological properties. Fish Shellfish Immunol., 2014; 36: 141–150
- Poet G.J., Oka O.B., van Lith M., Cao Z., Robinson P.J., Pringle M.A., Arnér E.S., Bulleid N.J.: Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER. EMBO J., 2017; 36: 693–702
- Powis G., Wipf P., Lynch S.M., Birmingham A., Kirkpatrick D.L.: Molecular pharmacology and antitumor activity of palmarumycin-based inhibitors of thioredoxin reductase. Mol. Cancer Ther., 2006; 5: 630–636
- Prast-Nielsen S., Huang H.H., Williams, D.L.: Thioredoxin glutathione reductase: Its role in redox biology and potential as a target for drugs against neglected diseases. Biochim. Biophys. Acta, 2011; 1810: 1262–1271
- Ramanathan R.K., Stephenson J.J., Weiss G.J., Pestano L.A., Lowe A., Hiscox A., Leos R.A., Martin J.C., Kirkpatrick L., Richards D.A.: A phase I trial of PX-12, a small-molecule inhibitor of thioredoxin-1, administered as a 72-hour infusion every 21 days in patients with advanced cancers refractory to standard therapy. Invest. New Drugs, 2012; 30: 1591–1596
- Raninga P.V., Di Trapani G., Vuckovic S., Bhatia M., Tonissen K.F.: Inhibition of thioredoxin 1 leads to apoptosis in drug-resistant multiple myeloma. Oncotarget, 2015; 6: 15410–15424
- Ren X., Zou L., Lu J., Holmgren A.: Selenocysteine in mammalian thioredoxin reductase and application of ebselen as a therapeutic. Free Radic. Biol. Med., 2018; 127: 238–247
- Ren X., Zou L., Zhang X., Branco V., Wang J., Carvalho C., Holmgren A., Lu J.: Redox signaling mediated by thioredoxin and glutathione systems in the central nervous system. Antioxid. Redox Signal., 2017; 27: 989–1010
- Rendón J.L., Miranda-Leyva M., Guevara-Flores A., Martínez-González J.J., Del Arenal I.P., Flores-Herrera O., Pardo J.P.: Insight into the mechanistic basis of the hysteretic-like kinetic behavior of thioredoxin-glutathione reductase (TGR). Enzyme Res., 2018; 2018: 3215462
- Rhee S.G.: Overview on peroxiredoxin. Mol. Cells, 2016; 39: 1–5
- Rhee S.G., Woo H.A., Kil I.S., Bae S.H.: Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides. J. Biol. Chem., 2012; 287: 4403–4410
- Rodriguez-Garcia A., Hevia D., Mayo J.C., Gonzalez-Menendez P., Coppo L., Lu J., Holmgren A., Sainz R.M.: Thioredoxin 1 modulates apoptosis induced by bioactive compounds in prostate cancer cells. Redox Biol., 2017; 12: 634–647
- Roos G., Foloppe N., Van Laer K., Wyns L., Nilsson L., Geerlings P., Messens J.: How thioredoxin dissociates its mixed disulfide. PLoS Comput. Biol., 2009; 5: e1000461
- Saccoccia, F., Angelucci F., Boumis G., Carotti D., Desiato G., Miele A.E., Bellelli A.: Thioredoxin reductase and its inhibitors. Curr. Protein Pept. Sci., 2014; 15, 621–646
- Sandargo B., Thongbai B., Praditya D., Steinmann E., Stadler M., Surup F.: Antiviral 4-hydroxypleurogrisein and antimicrobial pleurotin derivatives from cultures of the nematophagous basidiomycete Hohenbuehelia grisea. Molecules, 2018; 23: 2697
- Sugiura Y., Araki K., Iemura S.I., Natsume T., Hoseki J., Nagata, K.: Novel thioredoxin-related transmembrane protein TMX4 has reductase activity. J. Biol. Chem., 2010; 285: 7135–7142
- Sweeney M., Coyle R., Kavanagh P., Berezin A.A., Re D.L., Zissimou G.A., Koutentis P.A., Carty M.P., Aldabbagh F.: Discovery of anti-cancer activity for benzo [1,2,4] triazin-7-ones: Very strong correlation to pleurotin and thioredoxin reductase inhibition. Bioorg. Med. Chem., 2016; 24: 3565–3570
- Tan S.X., Greetham D., Raeth S., Grant C.M., Dawes I.W., Perrone G.G.: The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae. J. Biol. Chem., 2010; 285: 6118–6126
- Toledano M.B., Delaunay-Moisan A., Outten C.E., Igbaria A.: Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast. Antioxid. Redox Signal., 2013; 18: 1699–1711
- Tonissen K.F., Di Trapani G.: Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy. Mol. Nutr. Food Res., 2009; 53: 87–103
- Ukuwela A.A., Bush A.I., Wedd A.G., Xiao Z.: Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thioldisulfide exchanges with protein disulfides. Chem. Sci., 2018; 9: 1173–1183
- Vandervore L.V., Schot R., Milanese C., Smits D.J., Kasteleijn E., Fry A.E., Pilz D.T., Brock S., Börklü-Yücel E., Post M., Bahi-Buisson N., Sánchez-Soler M.J., van Slegtenhors M., Keren B., Afenjar A. i wsp.: TMX2 is a crucial regulator of cellular redox state, and its dysfunction causes severe brain developmental abnormalities. Am. J. Hum. Genet, 2019; 105: 1126–1147
- Watanabe R., Nakamura H., Masutani H., Yodoi J.: Anti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2. Pharmacol. Ther., 2010; 127: 261–270
- Wu C., Parrott A.M., Fu C., Liu T., Marino S.M., Gladyshev V.N., Jain M.R., Baykal A.T., Li Q., Oka S., Sadoshima J., Beuve A., Simmons W.J., Li H.: Thioredoxin 1-mediated post-translational modifications: Reduction, transnitrosylation, denitrosylation, and related proteomics methodologies. Antioxid. Redox Signal., 2011; 15: 2565–2604
- Yoshioka J.: Thioredoxin superfamily and its effects on cardiac physiology and pathology. Compr. Physiol., 2011; 5: 513–530
- Zeng H.H., Wang L.H.: Targeting thioredoxin reductase: Anticancer agents and chemopreventive compounds. Med. Chem., 2010; 6: 286–297
- Zhang J., Zhang B., Li X., Han X., Liu R., Fang J.: Small molecule inhibitors of mammalian thioredoxin reductase as potential anti-cancer agents: An update. Med. Res. Rev., 2019; 39: 5–39
- Zhang J.J., Muenzner J.K., Abu El Maaty M.A., Karge B., Schobert R., Wölfl S., Ott I.: A multi-target caffeine derived rhodium (I) N-heterocyclic carbene complex: Evaluation of the mechanism of action. Dalton Trans., 2016; 45: 13161–13168
- Zhu H., Tao X., Zhou L., Sheng B., Zhu X., Zhu X.: Expression of thioredoxin 1 and peroxiredoxins in squamous cervical carcinoma and its predictive role in NACT. BMC Cancer, 2019; 19: 865
DOI: https://doi.org/10.5604/01.3001.0014.6952 | Journal eISSN: 1732-2693
Language: English
Page range: 35 - 47
Submitted on: Mar 25, 2020
Accepted on: Nov 9, 2020
Published on: Jan 26, 2021
Published by: Hirszfeld Institute of Immunology and Experimental Therapy
In partnership with: Paradigm Publishing Services
Publication frequency: 1 times per year
Related subjects:
© 2021 Anna Jastrząb, Elżbieta Skrzydlewska, published by Hirszfeld Institute of Immunology and Experimental Therapy
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.