메뉴 건너뛰기




Volumn 116, Issue , 2016, Pages 23-28

Thioredoxin reductase inhibitor auranofin prevents membrane transport of diphtheria toxin into the cytosol and protects human cells from intoxication

Author keywords

Auranofin; Cellular uptake; Diphtheria toxin; Endosome; Membrane translocation; Thioredoxin reductase

Indexed keywords

AURANOFIN; DIPHTHERIA TOXIN; DIPHTHERIA TOXIN A; DISULFIDE; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG; PROTECTIVE AGENT;

EID: 84928389594     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2015.04.012     Document Type: Article
Times cited : (15)

References (42)
  • 3
    • 0029758834 scopus 로고    scopus 로고
    • Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen
    • S.R. Blanke, J.C. Milne, E.L. Benson, and R.J. Collier Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen Proc. Natl. Acad. Sci. U. S. A. 83 1996 7643 7647
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 7643-7647
    • Blanke, S.R.1    Milne, J.C.2    Benson, E.L.3    Collier, R.J.4
  • 4
    • 34447253589 scopus 로고    scopus 로고
    • The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol
    • B. Blumenthal, C. Hoffmann, K. Aktories, S. Backert, and G. Schmidt The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol Infect. Immun. 75 2007 3344 3353
    • (2007) Infect. Immun. , vol.75 , pp. 3344-3353
    • Blumenthal, B.1    Hoffmann, C.2    Aktories, K.3    Backert, S.4    Schmidt, G.5
  • 5
    • 0030743785 scopus 로고    scopus 로고
    • The mechanisms of action of disease-modifying antirheumatic drugs: A review with emphasis on macrophage signal transduction and the induction of proinflammatory cytokines
    • J. Bondeson The mechanisms of action of disease-modifying antirheumatic drugs: a review with emphasis on macrophage signal transduction and the induction of proinflammatory cytokines Gen. Pharmacol. 29 1997 127 150
    • (1997) Gen. Pharmacol. , vol.29 , pp. 127-150
    • Bondeson, J.1
  • 7
    • 0014665802 scopus 로고
    • Diphtheria toxin subunit active in vitro
    • R.J. Collier, and H.A. Cole Diphtheria toxin subunit active in vitro Science 164 1969 1179 1181
    • (1969) Science , vol.164 , pp. 1179-1181
    • Collier, R.J.1    Cole, H.A.2
  • 8
    • 0034878448 scopus 로고    scopus 로고
    • Understanding the mode of action of diphtheria toxin: A perspective on progress during the 20th century
    • R.J. Collier Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century Toxicon 39 2001 1793 1803
    • (2001) Toxicon , vol.39 , pp. 1793-1803
    • Collier, R.J.1
  • 9
    • 0015217337 scopus 로고
    • Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments
    • R.J. Collier, and J. Kandel Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments J. Biol. Chem. 246 1971 1496 1503
    • (1971) J. Biol. Chem. , vol.246 , pp. 1496-1503
    • Collier, R.J.1    Kandel, J.2
  • 11
    • 0015217329 scopus 로고
    • Structure and activity of DT II. Attack by trypsin at a specific site within the intact molecule
    • R. Drazin, J. Kandel, and R.J. Collier Structure and activity of DT II. Attack by trypsin at a specific site within the intact molecule J. Biol. Chem. 246 1971 1504 1510
    • (1971) J. Biol. Chem. , vol.246 , pp. 1504-1510
    • Drazin, R.1    Kandel, J.2    Collier, R.J.3
  • 12
    • 0026752616 scopus 로고
    • Replacement of negative by positive charges in the presumed membrane-inserted part of diphtheria toxin B fragment. Effect on membrane translocation and on formation of cation channels
    • P.O. Falnes, I.H. Madshus, K. Sandvig, and S. Olsnes Replacement of negative by positive charges in the presumed membrane-inserted part of diphtheria toxin B fragment. Effect on membrane translocation and on formation of cation channels J. Biol. Chem. 267 1992 12284 12290
    • (1992) J. Biol. Chem. , vol.267 , pp. 12284-12290
    • Falnes, P.O.1    Madshus, I.H.2    Sandvig, K.3    Olsnes, S.4
  • 13
    • 0028292770 scopus 로고
    • Inhibition of membrane translocation of diphtheria toxin A-fragment by internal disulfide bridges
    • P.O. Falnes, S. Choe, I.H. Madshus, B.A. Wilson, and S. Olsnes Inhibition of membrane translocation of diphtheria toxin A-fragment by internal disulfide bridges J. Biol. Chem. 269 1994 8402 8407
    • (1994) J. Biol. Chem. , vol.269 , pp. 8402-8407
    • Falnes, P.O.1    Choe, S.2    Madshus, I.H.3    Wilson, B.A.4    Olsnes, S.5
  • 14
    • 0015217293 scopus 로고
    • Structure activity relationships in diphtheria toxin
    • D.M. Gill, and A.M. Pappenheimer Structure activity relationships in diphtheria toxin J. Biol. Chem. 246 1971 1485 1491
    • (1971) J. Biol. Chem. , vol.246 , pp. 1485-1491
    • Gill, D.M.1    Pappenheimer, A.M.2
  • 15
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • A. Holmgren, and J. Lu Thioredoxin and thioredoxin reductase: current research with special reference to human disease Biochem. Biophys. Res. Commun. 396 2010 120 124
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 16
    • 0028284810 scopus 로고
    • Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity
    • R. Iwamoto, S. Higashiyama, T. Mitamura, N. Taniguchi, M. Klagsbrun, and E. Mekada Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity EMBO J. 13 1994 2322 2330
    • (1994) EMBO J. , vol.13 , pp. 2322-2330
    • Iwamoto, R.1    Higashiyama, S.2    Mitamura, T.3    Taniguchi, N.4    Klagsbrun, M.5    Mekada, E.6
  • 17
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0028001091 scopus 로고
    • Intermediates in translocation of diphtheria toxin across the plasma membrane
    • I.H. Madshus, A. Wiedlocha, and K. Sandvig Intermediates in translocation of diphtheria toxin across the plasma membrane J. Biol. Chem. 269 1994 4648 4652
    • (1994) J. Biol. Chem. , vol.269 , pp. 4648-4652
    • Madshus, I.H.1    Wiedlocha, A.2    Sandvig, K.3
  • 23
  • 24
    • 0023664687 scopus 로고
    • Cell-mediated reduction of the interfragment disulfide in nicked DT. A new system to study toxin entry at low pH
    • J.O. Moskaug, K. Sandvig, and S. Olsnes Cell-mediated reduction of the interfragment disulfide in nicked DT. A new system to study toxin entry at low pH J. Biol. Chem. 262 1987 10339 10345
    • (1987) J. Biol. Chem. , vol.262 , pp. 10339-10345
    • Moskaug, J.O.1    Sandvig, K.2    Olsnes, S.3
  • 25
    • 0025737882 scopus 로고
    • Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH. Characterization and topology of inserted regions
    • J.O. Moskaug, H. Stenmark, and S. Olsnes Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH. Characterization and topology of inserted regions J. Biol. Chem. 266 1991 2652 2659
    • (1991) J. Biol. Chem. , vol.266 , pp. 2652-2659
    • Moskaug, J.O.1    Stenmark, H.2    Olsnes, S.3
  • 26
    • 79953236969 scopus 로고    scopus 로고
    • Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process
    • J.R. Murphy Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process Toxins 3 2011 294 308
    • (2011) Toxins , vol.3 , pp. 294-308
    • Murphy, J.R.1
  • 29
    • 0027510933 scopus 로고
    • Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol
    • E. Papini, R. Rappuoli, M. Murgia, and C. Montecucco Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol J. Biol. Chem. 268 1993 1567 1574
    • (1993) J. Biol. Chem. , vol.268 , pp. 1567-1574
    • Papini, E.1    Rappuoli, R.2    Murgia, M.3    Montecucco, C.4
  • 30
    • 0024115012 scopus 로고
    • On the membrane translocation of diphtheria toxin: At low pH the toxin induces ion channels on cells
    • E. Papini, D. Sandoná, R. Rappuoli, and C. Montecucco On the membrane translocation of diphtheria toxin: at low pH the toxin induces ion channels on cells EMBO J. 7 1988 3353 3359
    • (1988) EMBO J. , vol.7 , pp. 3353-3359
    • Papini, E.1    Sandoná, D.2    Rappuoli, R.3    Montecucco, C.4
  • 32
    • 84872100030 scopus 로고    scopus 로고
    • The thioredoxin reductase-thioredoxin system is involved in the entry of tetanus and botulinum neurotoxins in the cytosol of nerve terminals
    • M. Pirazzini, F. Bordin, O. Rossetto, C.C. Shone, T. Binz, and C. Montecucco The thioredoxin reductase-thioredoxin system is involved in the entry of tetanus and botulinum neurotoxins in the cytosol of nerve terminals FEBS Lett. 587 2013 150 155
    • (2013) FEBS Lett. , vol.587 , pp. 150-155
    • Pirazzini, M.1    Bordin, F.2    Rossetto, O.3    Shone, C.C.4    Binz, T.5    Montecucco, C.6
  • 34
    • 78049398585 scopus 로고    scopus 로고
    • Noble metal targeting of thioredoxin reductase-covalent complexes with thioredoxin and thioredoxin-related protein of 14 kDa triggered by cisplatin
    • S. Prast-Nielsen, M. Cebula, I. Pader, and E.S. Arner Noble metal targeting of thioredoxin reductase-covalent complexes with thioredoxin and thioredoxin-related protein of 14 kDa triggered by cisplatin Free Radic. Biol. Med. 49 2010 1765 1778
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1765-1778
    • Prast-Nielsen, S.1    Cebula, M.2    Pader, I.3    Arner, E.S.4
  • 35
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • R. Ratts, H. Zeng, E.A. Berg, C. Blue, M.E. McComb, C.E. Costello, J.C. vanderSpek, and R. Murphy The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex J. Cell. Biol. 160 2003 1139 1150
    • (2003) J. Cell. Biol. , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6    VanderSpek, J.C.7    Murphy, R.8
  • 36
    • 0019811089 scopus 로고
    • Rapid entry of nicked diphtheria toxin into cells at low pH. Characterization of the entry process and effects of low pH on the toxin molecule
    • K. Sandvig, and S. Olsnes Rapid entry of nicked diphtheria toxin into cells at low pH. Characterization of the entry process and effects of low pH on the toxin molecule J. Biol. Chem. 256 1981 9068 9076
    • (1981) J. Biol. Chem. , vol.256 , pp. 9068-9076
    • Sandvig, K.1    Olsnes, S.2
  • 37
    • 0024270539 scopus 로고
    • Diphtheria toxin-induced channels in Vero cells selective for monovalent cations
    • K. Sandvig, and S. Olsnes Diphtheria toxin-induced channels in Vero cells selective for monovalent cations J. Biol. Chem. 263 1988 12352 12359
    • (1988) J. Biol. Chem. , vol.263 , pp. 12352-12359
    • Sandvig, K.1    Olsnes, S.2
  • 38
    • 0025981906 scopus 로고
    • Elimination of the disulphide bridge in fragment B of diphtheria toxin: Effect on membrane insertion, channel formation, and ATP binding
    • H. Stenmark, S. Olsnes, and I.H. Madshus Elimination of the disulphide bridge in fragment B of diphtheria toxin: effect on membrane insertion, channel formation, and ATP binding Mol. Microbiol. 5 1991 595 606
    • (1991) Mol. Microbiol. , vol.5 , pp. 595-606
    • Stenmark, H.1    Olsnes, S.2    Madshus, I.H.3
  • 39
    • 58149352993 scopus 로고    scopus 로고
    • Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy
    • K.F. Tonissen, and G. Di Trapani Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy Mol. Nutr. Food Res. 53 2009 87 103
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 87-103
    • Tonissen, K.F.1    Di Trapani, G.2
  • 40
    • 0027495717 scopus 로고
    • Evidence for the involvement of furin in cleavage and activation of diphtheria toxin
    • M. Tsuneoka, K. Nakayama, K. Hatsuzawa, M. Komada, N. Kitamura, and E. Mekada Evidence for the involvement of furin in cleavage and activation of diphtheria toxin J. Biol. Chem. 268 1993 26461 26465
    • (1993) J. Biol. Chem. , vol.268 , pp. 26461-26465
    • Tsuneoka, M.1    Nakayama, K.2    Hatsuzawa, K.3    Komada, M.4    Kitamura, N.5    Mekada, E.6
  • 41
    • 0025649278 scopus 로고
    • The cytotoxic action of diphtheria toxin and its degradation in intact Vero cells are inhibited by bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase
    • T. Umata, Y. Moriyama, M. Futai, and E. Mekada The cytotoxic action of diphtheria toxin and its degradation in intact Vero cells are inhibited by bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase J. Biol. Chem. 265 1990 21940 21945
    • (1990) J. Biol. Chem. , vol.265 , pp. 21940-21945
    • Umata, T.1    Moriyama, Y.2    Futai, M.3    Mekada, E.4
  • 42
    • 0027048990 scopus 로고
    • Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector
    • A. Wiedlocha, I.H. Madshus, H. Mach, C.R. Middaugh, and S. Olsnes Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector EMBO J. 11 1992 4835 4842
    • (1992) EMBO J. , vol.11 , pp. 4835-4842
    • Wiedlocha, A.1    Madshus, I.H.2    Mach, H.3    Middaugh, C.R.4    Olsnes, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.