메뉴 건너뛰기




Volumn 287, Issue 12, 2012, Pages 8792-8802

High throughput screening against the peroxidase cascade of African trypanosomes identifies antiparasitic compounds that inactivate tryparedoxin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AFRICAN TRYPANOSOMES; ANTI-CANCER THERAPEUTICS; ANTICANCER DRUG; BROAD SPECTRUM; COMPLETE SYSTEM; DETAILED KINETICS; DRUG TARGETS; GEL SHIFT ASSAYS; GLUTATHIONES; HELA CELL; HIGH THROUGHPUT SCREENING; HYDROPEROXIDES; IN-VITRO ASSAYS; MOLAR EXCESS; OXIDOREDUCTASES; TARGET PROTEINS; THIOREDOXINS; TIME-DEPENDENT; TRYPANOSOMA BRUCEI; TRYPANOTHIONE; TRYPANOTHIONE REDUCTASE;

EID: 84858596191     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.338285     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel, R. L., and Comini, M. A. (2008) Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim. Biophys. Acta 1780, 1236-1248
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 2
    • 46449133760 scopus 로고    scopus 로고
    • Peroxidases of trypanosomatids
    • DOI 10.1089/ars.2008.2050
    • Castro, H., and Tomás, A. M. (2008) Peroxidases of trypanosomatids. Antioxid. Redox. Signal. 10, 1593-1606 (Pubitemid 351934269)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.9 , pp. 1593-1606
    • Castro, H.1    Tomas, A.M.2
  • 3
    • 79960934330 scopus 로고    scopus 로고
    • A tryparedoxin-dependent peroxidase protects African trypanosomes from membrane damage
    • Diechtierow, M., and Krauth-Siegel, R. L. (2011) A tryparedoxin-dependent peroxidase protects African trypanosomes from membrane damage. Free Radic. Biol. Med. 51, 856-868
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 856-868
    • Diechtierow, M.1    Krauth-Siegel, R.L.2
  • 4
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb, A. H., and Cerami, A. (1992) Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46, 695-729
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 7
    • 79251537792 scopus 로고    scopus 로고
    • Improved inhibitors of trypanothione reductase by combination of motifs. Synthesis, inhibitory potency, binding mode, and antiprotozoal activities
    • Eberle, C., Lauber, B. S., Fankhauser, D., Kaiser, M., Brun, R., Krauth-Siegel, R. L., and Diederich, F. (2011) Improved inhibitors of trypanothione reductase by combination of motifs. Synthesis, inhibitory potency, binding mode, and antiprotozoal activities. Chem. Med. Chem. 6, 292-301
    • (2011) Chem. Med. Chem. , vol.6 , pp. 292-301
    • Eberle, C.1    Lauber, B.S.2    Fankhauser, D.3    Kaiser, M.4    Brun, R.5    Krauth-Siegel, R.L.6    Diederich, F.7
  • 8
    • 13444280474 scopus 로고    scopus 로고
    • Dithiol proteins as guardians of the intracellular redox milieu in parasites: Old and new drug targets in trypanosomes and malaria-causing plasmodia
    • DOI 10.1002/anie.200300639
    • Krauth-Siegel, R. L., Bauer, H., and Schirmer, R. H. (2005) Dithiol proteins as guardians of the intracellular redox milieu in parasites. Old and new drug targets in trypanosomes and malaria-causing plasmodia. Angew. Chem. Int. Ed. Engl. 44, 690-715 (Pubitemid 40203977)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.5 , pp. 690-715
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 10
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke, E., Gommel, D. U., Kiess, M., Kalisz, H. M., and Flohé, L. (1997) A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378, 827-836 (Pubitemid 27388943)
    • (1997) Biological Chemistry , vol.378 , Issue.8 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kiess, M.3    Kalisz, H.M.4    Flohe, L.5
  • 11
    • 0038790585 scopus 로고    scopus 로고
    • Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes
    • DOI 10.1016/S0014-5793(98)00793-5, PII S0014579398007935
    • Lüdemann, H., Dormeyer, M., Sticherling, C., Stallmann, D., Follmann, H., and Krauth-Siegel, R. L. (1998) Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes. FEBS Lett. 431, 381-385 (Pubitemid 28352394)
    • (1998) FEBS Letters , vol.431 , Issue.3 , pp. 381-385
    • Ludemann, H.1    Dormeyer, M.2    Sticherling, C.3    Stallmann, D.4    Follmann, H.5    Krauth-Siegel, R.L.6
  • 14
    • 0035815655 scopus 로고    scopus 로고
    • Trypanothione-dependent Synthesis of Deoxyribonucleotides by Trypanosoma brucei Ribonucleotide Reductase
    • DOI 10.1074/jbc.M010352200
    • Dormeyer, M., Reckenfelderbäumer, N., Ludemann, H., and Krauth-Siegel, R. L. (2001) Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase. J. Biol. Chem. 276, 10602-10606 (Pubitemid 38094248)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10602-10606
    • Dormeyer, M.1    Reckenfelderbaumer, N.2    Ludemann, H.3    Krauth-Siegel, R.L.4
  • 15
    • 33846933089 scopus 로고    scopus 로고
    • High-throughput screening affords novel and selective trypanothione reductase inhibitors with anti-trypanosomal activity
    • DOI 10.1016/j.bmcl.2006.12.016, PII S0960894X0601403X
    • Martyn, D. C., Jones, D. C., Fairlamb, A. H., and Clardy, J. (2007) High throughput screening affords novel and selective trypanothione reductase inhibitors with anti-trypanosomal activity. Bioorg. Med. Chem. Lett. 17, 1280-1283 (Pubitemid 46240853)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.5 , pp. 1280-1283
    • Martyn, D.C.1    Jones, D.C.2    Fairlamb, A.H.3    Clardy, J.4
  • 16
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • DOI 10.1046/j.1365-2958.2000.01721.x
    • Krieger, S., Schwarz, W., Ariyanayagam, M. R., Fairlamb, A. H., Krauth-Siegel, R. L., and Clayton, C. (2000) Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol. Microbiol. 35, 542-552 (Pubitemid 30085272)
    • (2000) Molecular Microbiology , vol.35 , Issue.3 , pp. 542-552
    • Krieger, S.1    Schwarz, W.2    Arlyanayagam, M.R.3    Fairlamb, A.H.4    Krauth-Siegel, R.L.5    Clayton, C.6
  • 17
    • 0041355353 scopus 로고    scopus 로고
    • RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome
    • DOI 10.1074/jbc.M303035200
    • Wilkinson, S. R., Horn, D., Prathalingam, S. R., and Kelly, J. M. (2003)RNA interference identifies two hydroperoxide-metabolizing enzymes that are essential to the bloodstream form of the African trypanosome. J. Biol. Chem. 278, 31640-31646 (Pubitemid 37048342)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31640-31646
    • Wilkinson, S.R.1    Horn, D.2    Prathalingam, S.R.3    Kelly, J.M.4
  • 18
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • DOI 10.1074/jbc.M413338200
    • Schlecker, T., Schmidt, A., Dirdjaja, N., Voncken, F., Clayton, C., and Krauth-Siegel, R. L. (2005) Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J. Biol. Chem. 280, 14385-14394 (Pubitemid 40562777)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 19
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes
    • Comini, M. A., Krauth-Siegel, R. L., and Flohé, L. (2007) Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes. Biochem. J. 402, 43-49
    • (2007) Biochem. J. , vol.402 , pp. 43-49
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Flohé, L.3
  • 20
    • 79953128738 scopus 로고    scopus 로고
    • Antitumor quinol PMX464 is a cytocidal anti-trypanosomal inhibitor targeting trypanothione metabolism
    • König, J., Wyllie, S., Wells, G., Stevens, M. F., Wyatt, P. G., and Fairlamb, A. H. (2011) Antitumor quinol PMX464 is a cytocidal anti-trypanosomal inhibitor targeting trypanothione metabolism. J. Biol. Chem. 286, 8523-8533
    • (2011) J. Biol. Chem. , vol.286 , pp. 8523-8533
    • König, J.1    Wyllie, S.2    Wells, G.3    Stevens, M.F.4    Wyatt, P.G.5    Fairlamb, A.H.6
  • 22
    • 34547920652 scopus 로고    scopus 로고
    • A cellular and molecular investigation of the action of PMX464, a putative thioredoxin inhibitor, in normal and colorectal cancer cell lines
    • DOI 10.1038/sj.bjp.0707342, PII 0707342
    • Mukherjee, A., Huber, K., Evans, H., Lakhani, N., and Martin, S. (2007) A cellular and molecular investigation of the action of PMX464, a putative thioredoxin inhibitor, in normal and colorectal cancer cell lines. Br. J. Pharmacol. 151, 1167-1175 (Pubitemid 47255909)
    • (2007) British Journal of Pharmacology , vol.151 , Issue.8 , pp. 1167-1175
    • Mukherjee, A.1    Huber, K.2    Evans, H.3    Lakhani, N.4    Martin, S.5
  • 23
    • 78650783356 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis thioredoxin in complex with quinol inhibitor PMX464
    • Hall, G., Bradshaw, T. D., Laughton, C. A., Stevens, M. F., and Emsley, J. (2011) Structure of Mycobacterium tuberculosis thioredoxin in complex with quinol inhibitor PMX464. Protein Sci. 20, 210-215
    • (2011) Protein Sci. , vol.20 , pp. 210-215
    • Hall, G.1    Bradshaw, T.D.2    Laughton, C.A.3    Stevens, M.F.4    Emsley, J.5
  • 24
    • 57649213965 scopus 로고    scopus 로고
    • 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase
    • 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase. Biomol. NMR Assign. 2, 65-68
    • (2008) Biomol. NMR Assign. , vol.2 , pp. 65-68
    • Melchers, J.1    Krauth-Siegel, L.2    Muhle-Goll, C.3
  • 25
    • 0037959650 scopus 로고    scopus 로고
    • Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of trypanosoma brucei brucei
    • DOI 10.1515/BC.2003.069
    • Budde, H., Flohé, L., Hecht, H. J., Hofmann, B., Stehr, M., Wissing, J., and Lünsdorf, H. (2003) Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol. Chem. 384, 619-633 (Pubitemid 36609177)
    • (2003) Biological Chemistry , vol.384 , Issue.4 , pp. 619-633
    • Budde, H.1    Flohe, L.2    Hecht, H.-J.3    Hofmann, B.4    Stehr, M.5    Wissing, J.6    Lunsdorf, H.7
  • 26
    • 0026098498 scopus 로고
    • Cloning, sequencing, overproduction, and purification of trypanothione reductase from Trypanosoma cruzi
    • Sullivan, F. X., and Walsh, C. T. (1991) Cloning, sequencing, overproduction, and purification of trypanothione reductase from Trypanosoma cruzi. Mol. Biochem. Parasitol. 44, 145-147
    • (1991) Mol. Biochem. Parasitol. , vol.44 , pp. 145-147
    • Sullivan, F.X.1    Walsh, C.T.2
  • 27
    • 67649656107 scopus 로고    scopus 로고
    • Preparative enzymatic synthesis of trypanothione and trypanothione analogues
    • Comini, M. A., Dirdjaja, N., Kaschel, M., and Krauth-Siegel, R. L. (2009) Preparative enzymatic synthesis of trypanothione and trypanothione analogues. Int. J. Parasitol. 39, 1059-1062
    • (2009) Int. J. Parasitol. , vol.39 , pp. 1059-1062
    • Comini, M.A.1    Dirdjaja, N.2    Kaschel, M.3    Krauth-Siegel, R.L.4
  • 28
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(00)00129-0, PII S0169409X00001290
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46, 3-26 (Pubitemid 33653411)
    • (2000) Advanced Drug Delivery Reviews , vol.46 , Issue.1-3 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 29
    • 34249881909 scopus 로고    scopus 로고
    • Evaluation of different glutathione s-transferase-tagged protein captures for screening E6/E6AP interaction inhibitors using AlphaScreen
    • DOI 10.1177/1087057107301246
    • Sehr, P., Pawlita, M., and Lewis, J. (2007) Evaluation of different glutathione S-transferase-tagged protein captures for screening E6/E6AP interaction inhibitors using AlphaScreen. J. Biomol. Screen. 12, 560-567 (Pubitemid 46871835)
    • (2007) Journal of Biomolecular Screening , vol.12 , Issue.4 , pp. 560-567
    • Sehr, P.1    Pawlita, M.2    Lewis, J.3
  • 30
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • DOI 10.1177/108705719900400206
    • Zhang, J. H., Chung, T. D., and Oldenburg, K. R. (1999)Asimple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4, 67-73 (Pubitemid 29278954)
    • (1999) Journal of Biomolecular Screening , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 31
    • 49249126411 scopus 로고    scopus 로고
    • Work flow for multiplexing siRNA assays by solid-phase reverse transfection in multiwell plates
    • Erfle, H., Neumann, B., Rogers, P., Bulkescher, J., Ellenberg, J., and Pepperkok, R. (2008) Work flow for multiplexing siRNA assays by solid-phase reverse transfection in multiwell plates. J. Biomol. Screen. 13, 575-580
    • (2008) J. Biomol. Screen. , vol.13 , pp. 575-580
    • Erfle, H.1    Neumann, B.2    Rogers, P.3    Bulkescher, J.4    Ellenberg, J.5    Pepperkok, R.6
  • 32
    • 20444424558 scopus 로고    scopus 로고
    • Rapid desalting of protein samples for on-line microflow electrospray ionization mass spectrometry
    • DOI 10.1016/j.ab.2004.11.043, PII S0003269704009479
    • Rist, W., Mayer, M. P., Andersen, J. S., Roepstorff, P., and Jørgensen, T. J. (2005) Rapid desalting of protein samples for on-line microflow electrospray ionization mass spectrometry. Anal. Biochem. 342, 160-162 (Pubitemid 40805640)
    • (2005) Analytical Biochemistry , vol.342 , Issue.1 , pp. 160-162
    • Rist, W.1    Mayer, M.P.2    Andersen, J.S.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 33
    • 0037470229 scopus 로고    scopus 로고
    • A second class of peroxidases linked to the trypanothione metabolism
    • DOI 10.1074/jbc.M210392200
    • Hillebrand, H., Schmidt, A., and Krauth-Siegel, R. L. (2003) A second class of peroxidases linked to the trypanothione metabolism. J. Biol. Chem. 278, 6809-6815 (Pubitemid 36800670)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6809-6815
    • Hillebrand, H.1    Schmidt, A.2    Krauth-Siegel, R.L.3
  • 34
    • 0027375651 scopus 로고
    • Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages
    • Carnieri, E. G., Moreno, S. N., and Docampo, R. (1993) Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages. Mol. Biochem. Parasitol. 61, 79-86
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 79-86
    • Carnieri, E.G.1    Moreno, S.N.2    Docampo, R.3
  • 36
    • 77949807477 scopus 로고    scopus 로고
    • Miniaturization and validation of the Ellman's reaction-based acetylcholinesterase inhibitory assay into 384-well plate format and screening of a chemical library
    • Järvinen, P. P., Fallarero, A., Gupta, S., Mohan, G. C., Hatakka, A. I., and Vuorela, P. M. (2010) Miniaturization and validation of the Ellman's reaction-based acetylcholinesterase inhibitory assay into 384-well plate format and screening of a chemical library. Comb. Chem. High Throughput Screen. 13, 278-284
    • (2010) Comb. Chem. High Throughput Screen. , vol.13 , pp. 278-284
    • Järvinen, P.P.1    Fallarero, A.2    Gupta, S.3    Mohan, G.C.4    Hatakka, A.I.5    Vuorela, P.M.6
  • 39
    • 34547402111 scopus 로고    scopus 로고
    • Catalytic mechanism of the glutathione peroxidase-type tryparedoxin peroxidase of Trypanosoma brucei
    • DOI 10.1042/BJ20070259
    • Schlecker, T., Comini, M. A., Melchers, J., Ruppert, T., and Krauth-Siegel, R. L. (2007) Catalytic mechanism of the glutathione peroxidase-type tryparedoxin peroxidase of Trypanosoma brucei. Biochem. J. 405, 445-454 (Pubitemid 47172041)
    • (2007) Biochemical Journal , vol.405 , Issue.3 , pp. 445-454
    • Schlecker, T.1    Comini, M.A.2    Melchers, J.3    Ruppert, T.4    Krauth-Siegel, R.L.5
  • 40
    • 0033520329 scopus 로고    scopus 로고
    • The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I
    • Alphey, M. S., Leonard, G. A., Gourley, D. G., Tetaud, E., Fairlamb, A. H., and Hunter, W. N. (1999) The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I. J. Biol. Chem. 274, 25613-25622
    • (1999) J. Biol. Chem. , vol.274 , pp. 25613-25622
    • Alphey, M.S.1    Leonard, G.A.2    Gourley, D.G.3    Tetaud, E.4    Fairlamb, A.H.5    Hunter, W.N.6
  • 42
    • 0141717106 scopus 로고    scopus 로고
    • Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESI-MS/MS
    • DOI 10.1515/BC.2003.146
    • Budde, H., Flohé, L., Hofmann, B., and Nimtz, M. (2003) Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESIMS/MS. Biol. Chem. 384, 1305-1309 (Pubitemid 37168699)
    • (2003) Biological Chemistry , vol.384 , Issue.9 , pp. 1305-1309
    • Budde, H.1    Flohe, L.2    Hofmann, B.3    Nimtz, M.4
  • 45
    • 0942298136 scopus 로고    scopus 로고
    • Identification and Characterization of TRP14, a Thioredoxin-related Protein of 14 kDa: New insights into the specificity of thioredoxin function
    • DOI 10.1074/jbc.M307932200
    • Jeong, W., Yoon, H. W., Lee, S. R., and Rhee, S. G. (2004) Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function. J. Biol. Chem. 279, 3142-3150 (Pubitemid 38140546)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3142-3150
    • Jeong, W.1    Yoon, H.W.2    Lee, S.-R.3    Rhee, S.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.