메뉴 건너뛰기




Volumn 105, Issue 3, 2011, Pages 515-528

Differential cytotoxic actions of Shiga toxin 1 and Shiga toxin 2 on microvascular and macrovascular endothelial cells

Author keywords

Apoptosis; Endothelial cells; Enterohaemorrhagic e. Coli; Necrosis; Shiga toxin; Single cell analysis

Indexed keywords

VEROTOXIN 1; VEROTOXIN 2;

EID: 79952531667     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH10-02-0140     Document Type: Article
Times cited : (87)

References (71)
  • 1
    • 72949118298 scopus 로고    scopus 로고
    • Between microbial attack and defence: The endothelium as a vulnerable player in infectious diseases
    • Schnittler H, Preissner KT. Between microbial attack and defence: the endothelium as a vulnerable player in infectious diseases. Thromb Haemost 2009; 102: 1011-1013.
    • (2009) Thromb Haemost , vol.102 , pp. 1011-1013
    • Schnittler, H.1    Preissner, K.T.2
  • 2
    • 75749139748 scopus 로고    scopus 로고
    • Breaking the wall: Targeting of the endothelium by pathogenic bacteria
    • Lemichez E, Lecuit M, Nassif X, et al. Breaking the wall: targeting of the endothelium by pathogenic bacteria. Nat Rev Microbiol 2010; 8: 93-104.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 93-104
    • Lemichez, E.1    Lecuit, M.2    Nassif, X.3
  • 3
    • 0037247739 scopus 로고    scopus 로고
    • Interaction of pathogens with the endothelium
    • Hippenstiel S, Suttorp N. Interaction of pathogens with the endothelium. Thromb Haemost 2003; 89: 18-24. (Pubitemid 36149788)
    • (2003) Thrombosis and Haemostasis , vol.89 , Issue.1 , pp. 18-24
    • Hippenstiel, S.1    Suttorp, N.2
  • 4
    • 4143084550 scopus 로고    scopus 로고
    • Infection by Shiga toxin-producing Escherichia coli: An overview
    • Karmali MA. Infection by Shiga toxin-producing Escherichia coli: an overview. Mol Biotechnol 2004; 26: 117-122.
    • (2004) Mol Biotechnol , vol.26 , pp. 117-122
    • Karmali, M.A.1
  • 5
    • 24044469996 scopus 로고    scopus 로고
    • Enterohaemorrhagic Escherichia coli in human medicine
    • Karch H, Tarr PI, Bielaszewska M. Enterohaemorrhagic Escherichia coli in human medicine. Int J Med Microbiol 2005; 295: 405-418.
    • (2005) Int J Med Microbiol , vol.295 , pp. 405-418
    • Karch, H.1    Tarr, P.I.2    Bielaszewska, M.3
  • 6
    • 15244348050 scopus 로고    scopus 로고
    • Shiga-toxin-producing Escherichia coli and haemolytic uraemic syndrome
    • Tarr PI, Gordon CA, Chandler WL. Shiga-toxin-producing Escherichia coli and haemolytic uraemic syndrome. Lancet 2005; 365: 1073-1086.
    • (2005) Lancet , vol.365 , pp. 1073-1086
    • Tarr, P.I.1    Gordon, C.A.2    Chandler, W.L.3
  • 7
    • 0034924948 scopus 로고    scopus 로고
    • Pathogenesis of Shiga toxin - Associated hemolytic uremic syndrome
    • Proulx F, Seidman EG, Karpman D. Pathogenesis of Shiga toxin-associated hemolytic uremic syndrome. Pediatr Res 2001; 50: 163-171. (Pubitemid 32701188)
    • (2001) Pediatric Research , vol.50 , Issue.2 , pp. 163-171
    • Proulx, F.1    Seidman, E.G.2    Karpman, D.3
  • 8
    • 61949434893 scopus 로고    scopus 로고
    • Treatment options for HUS secondary to Escherichia coli O157:H7
    • Bitzan M. Treatment options for HUS secondary to Escherichia coli O157:H7. Kidney Int Suppl 2009; 112: S62-66.
    • (2009) Kidney Int Suppl , vol.112
    • Bitzan, M.1
  • 9
    • 23744481459 scopus 로고    scopus 로고
    • Consequences of enterohaemorrhagic Escherichia coli infection for the vascular endothelium
    • Bielaszewska M, Karch H. Consequences of enterohaemorrhagic Escherichia coli infection for the vascular endothelium. Thromb Haemost 2005; 94: 312-318.
    • (2005) Thromb Haemost , vol.94 , pp. 312-318
    • Bielaszewska, M.1    Karch, H.2
  • 10
    • 0034877295 scopus 로고    scopus 로고
    • Shiga toxins
    • DOI 10.1016/S0041-0101(01)00150-7, PII S0041010101001507
    • Sandvig K. Shiga toxins. Toxicon 2001; 39: 1629-1635. (Pubitemid 32786996)
    • (2001) Toxicon , vol.39 , Issue.11 , pp. 1629-1635
    • Sandvig, K.1
  • 12
    • 0000009853 scopus 로고
    • Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli
    • Jackson MP, Neill RJ, O'Brien AD, et al. Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli. FEMS Microbiol Lett 1987; 44: 109-114.
    • (1987) FEMS Microbiol Lett , vol.44 , pp. 109-114
    • Jackson, M.P.1    Neill, R.J.2    O'Brien, A.D.3
  • 13
    • 0023664612 scopus 로고
    • Glycolipid binding of purified and recombinant Escherichia coli produced verotoxin in vitro
    • Lingwood CA, Law H, Richardson S, et al. Glycolipid binding of purified and recombinant Escherichia coli produced verotoxin in vitro. J Biol Chem 1987; 262: 8834-8839.
    • (1987) J Biol Chem , vol.262 , pp. 8834-8839
    • Lingwood, C.A.1    Law, H.2    Richardson, S.3
  • 14
    • 0024299352 scopus 로고
    • Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2
    • Waddell T, Head S, Petric M, et al. Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2. Biochem Biophys Res Commun 1988; 152: 674-679.
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 674-679
    • Waddell, T.1    Head, S.2    Petric, M.3
  • 15
    • 62449181018 scopus 로고    scopus 로고
    • Shiga toxins, glycosphingolipid diversity, and endothelial cell injury
    • Müthing J, Schweppe CH, Karch H, et al. Shiga toxins, glycosphingolipid diversity, and endothelial cell injury. Thromb Haemost 2009; 101: 252-264.
    • (2009) Thromb Haemost , vol.101 , pp. 252-264
    • Müthing, J.1    Schweppe, C.H.2    Karch, H.3
  • 16
    • 0025878152 scopus 로고
    • Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits: Evidence for B subunit modulation of a subunit function
    • Head SC, Karmali MA, Lingwood CA. Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits. Evidence for B subunit modulation of a subunit function. J Biol Chem 1991; 266: 3617-3621. (Pubitemid 21909257)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.6 , pp. 3617-3621
    • Head, S.C.1    Karmali, M.A.2    Lingwood, C.A.3
  • 18
    • 0034819738 scopus 로고    scopus 로고
    • Shiga toxin translocation across intestinal epithelial cells is enhanced by neutrophil transmigration
    • DOI 10.1128/IAI.69.10.6148-6155.2001
    • Hurley BP, Thorpe CM, Acheson DW. Shiga toxin translocation across intestinal epithelial cells is enhanced by neutrophil transmigration. Infect Immun 2001; 69: 6148-6155. (Pubitemid 32885176)
    • (2001) Infection and Immunity , vol.69 , Issue.10 , pp. 6148-6155
    • Hurley, B.P.1    Thorpe, C.M.2    Acheson, D.W.K.3
  • 20
    • 54249108555 scopus 로고    scopus 로고
    • Interactions between Shiga toxins and human polymorphonuclear leukocytes
    • Brigotti M, Carnicelli D, Ravanelli E, et al. Interactions between Shiga toxins and human polymorphonuclear leukocytes. J Leukoc Biol 2008; 84: 1019-1027.
    • (2008) J Leukoc Biol , vol.84 , pp. 1019-1027
    • Brigotti, M.1    Carnicelli, D.2    Ravanelli, E.3
  • 21
    • 0034139657 scopus 로고    scopus 로고
    • Facing inward from compartment shores: How many pathways were we looking for?
    • Johannes L, Goud B. Facing inward from compartment shores: how many pathways were we looking for? Traffic 2000; 1: 119-123.
    • (2000) Traffic , vol.1 , pp. 119-123
    • Johannes, L.1    Goud, B.2
  • 22
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • DOI 10.1016/S0014-5793(02)03182-4, PII S0014579302031824
    • Sandvig K, van Deurs B. Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett 2002; 529: 49-53. (Pubitemid 35283911)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 49-53
    • Sandvig, K.1    Van Deurs, B.2
  • 24
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • Sandvig K, Garred O, Prydz K, et al. Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 1992; 358: 510-512.
    • (1992) Nature , vol.358 , pp. 510-512
    • Sandvig, K.1    Garred, O.2    Prydz, K.3
  • 25
    • 0029760597 scopus 로고    scopus 로고
    • Aglycone modulation of glycolipid receptor function
    • Lingwood CA. Aglycone modulation of glycolipid receptor function. Glycoconj J 1996; 13: 495-503. (Pubitemid 26271265)
    • (1996) Glycoconjugate Journal , vol.13 , Issue.4 , pp. 495-503
    • Lingwood, C.A.1
  • 27
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • DOI 10.1038/nrm1985, PII NRM1985
    • Bonifacino JS, Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat Rev Mol Cell Biol 2006; 7: 568-579. (Pubitemid 44325348)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.8 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 28
    • 16244400431 scopus 로고    scopus 로고
    • Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone HEDJ/ERdj3
    • DOI 10.1128/IAI.73.4.2524-2532.2005
    • Yu M, Haslam DB. Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone HEDJ/ERdj3. Infect Immun 2005; 73: 2524-2532. (Pubitemid 40470856)
    • (2005) Infection and Immunity , vol.73 , Issue.4 , pp. 2524-2532
    • Yu, M.1    Haslam, D.B.2
  • 29
    • 0029009879 scopus 로고
    • Role of processing and intracellular transport for optimal toxicity of Shiga toxin and toxin mutants
    • Garred O, Dubinina E, Holm PK, et al. Role of processing and intracellular transport for optimal toxicity of Shiga toxin and toxin mutants. Exp Cell Res 1995; 218: 39-49.
    • (1995) Exp Cell Res , vol.218 , pp. 39-49
    • Garred, O.1    Dubinina, E.2    Holm, P.K.3
  • 30
    • 0026704042 scopus 로고
    • Shiga toxin: Biochemistry, genetics, mode of action, and role in pathogenesis
    • O'Brien AD, Tesh VL, Donohue-Rolfe A, et al. Shiga toxin: biochemistry, genetics, mode of action, and role in pathogenesis. Curr Top Microbiol Immunol 1992; 180: 65-94.
    • (1992) Curr Top Microbiol Immunol , vol.180 , pp. 65-94
    • O'Brien, A.D.1    Tesh, V.L.2    Donohue-Rolfe, A.3
  • 31
    • 0031595095 scopus 로고    scopus 로고
    • Shiga-like toxin I is a polynucleotide:adenosine glycosidase
    • Barbieri L, Valbonesi P, Brigotti M, et al. Shiga-like toxin I is a polynucleotide:adenosine glycosidase. Mol Microbiol 1998; 29: 661-662.
    • (1998) Mol Microbiol , vol.29 , pp. 661-662
    • Barbieri, L.1    Valbonesi, P.2    Brigotti, M.3
  • 32
    • 0023854742 scopus 로고
    • Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins
    • Endo Y, Tsurugi K, Yutsudo T, et al. Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. Eur J Biochem. 1988, 171: 45-50.
    • (1988) Eur J Biochem. , vol.171 , pp. 45-50
    • Endo, Y.1    Tsurugi, K.2    Yutsudo, T.3
  • 34
    • 4444265798 scopus 로고    scopus 로고
    • Shiga toxin binding to globotriaosyl ceramide induces intracellular signals that mediate cytoskeleton remodeling in human renal carcinoma-derived cells
    • DOI 10.1242/jcs.01246
    • Takenouchi H, Kiyokawa N, Taguchi T, et al. Shiga toxin binding to globotriaosyl ceramide induces intracellular signals that mediate cytoskeleton remodeling in human renal carcinoma-derived cells. J Cell Sci 2004; 117: 3911-3922. (Pubitemid 39207328)
    • (2004) Journal of Cell Science , vol.117 , Issue.17 , pp. 3911-3922
    • Takenouchi, H.1    Kiyokawa, N.2    Taguchi, T.3    Matsui, J.4    Katagiri, Y.U.5    Okita, H.6    Okuda, K.7    Fujimoto, J.8
  • 35
    • 48849111923 scopus 로고    scopus 로고
    • Shiga toxin 2 causes apoptosis in human brain microvascular endothelial cells via C/EBP homologous protein
    • Fujii J, Wood K, Matsuda F, et al. Shiga toxin 2 causes apoptosis in human brain microvascular endothelial cells via C/EBP homologous protein. Infect Immun 2008; 76: 3679-3689.
    • (2008) Infect Immun , vol.76 , pp. 3679-3689
    • Fujii, J.1    Wood, K.2    Matsuda, F.3
  • 36
    • 0034598651 scopus 로고    scopus 로고
    • Shiga toxin 1: Damage to DNA in vitro
    • Brigotti M, Accorsi P, Carnicelli D, et al. Shiga toxin 1: damage to DNA in vitro. Toxicon 2001; 39: 341-348.
    • (2001) Toxicon , vol.39 , pp. 341-348
    • Brigotti, M.1    Accorsi, P.2    Carnicelli, D.3
  • 37
    • 2942668193 scopus 로고    scopus 로고
    • Shiga toxin 1 acting on DNA in vitro is a heatstable enzyme not requiring proteolytic activation
    • Brigotti M, Carnicelli D, Vara AG. Shiga toxin 1 acting on DNA in vitro is a heatstable enzyme not requiring proteolytic activation. Biochimie 2004; 86: 305-309.
    • (2004) Biochimie , vol.86 , pp. 305-309
    • Brigotti, M.1    Carnicelli, D.2    Vara, A.G.3
  • 39
    • 39749147148 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: From nonexisting to an extreme degree of complexity
    • Sandvig K, Torgersen ML, Raa HA, et al. Clathrin-independent endocytosis: from nonexisting to an extreme degree of complexity. Histochem Cell Biol 2008; 129: 267-276.
    • (2008) Histochem Cell Biol , vol.129 , pp. 267-276
    • Sandvig, K.1    Torgersen, M.L.2    Raa, H.A.3
  • 40
    • 0023801292 scopus 로고
    • Direct cytotoxic action of Shiga toxin on human vascular endothelial cells
    • Obrig TG, Del Vecchio PJ, Brown JE, et al. Direct cytotoxic action of Shiga toxin on human vascular endothelial cells. Infect Immun 1988; 56: 2373-2378.
    • (1988) Infect Immun , vol.56 , pp. 2373-2378
    • Obrig, T.G.1    Del Vecchio, P.J.2    Brown, J.E.3
  • 41
    • 0028889506 scopus 로고
    • Specific interaction of Escherichia coli O157:H7-derived Shiga-like toxin II with human renal endothelial cells
    • Louise CB, Obrig TG. Specific interaction of Escherichia coli O157:H7-derived Shiga-like toxin II with human renal endothelial cells. J Infect Dis 1995; 172: 1397-1401.
    • (1995) J Infect Dis , vol.172 , pp. 1397-1401
    • Louise, C.B.1    Obrig, T.G.2
  • 44
    • 0033382907 scopus 로고    scopus 로고
    • Interaction of Shiga toxins with human brain microvascular endothelial cells: Cytokines as sensitizing agents
    • DOI 10.1086/314982
    • Ramegowda B, Samuel JE, Tesh VL. Interaction of Shiga toxins with human brain microvascular endothelial cells: cytokines as sensitizing agents. J Infect Dis 1999; 180: 1205-1213. (Pubitemid 30070205)
    • (1999) Journal of Infectious Diseases , vol.180 , Issue.4 , pp. 1205-1213
    • Ramegowda, B.1    Samuel, J.E.2    Tesh, V.L.3
  • 45
    • 0030917425 scopus 로고    scopus 로고
    • Selective expression of adhesion molecules on human brain microvascular endothelial cells
    • DOI 10.1016/S0165-5728(97)00036-2, PII S0165572897000362
    • Stins MF, Gilles F, Kim KS. Selective expression of adhesion molecules on human brain microvascular endothelial cells. J Neuroimmunol 1997; 76: 81-90. (Pubitemid 27272632)
    • (1997) Journal of Neuroimmunology , vol.76 , Issue.1-2 , pp. 81-90
    • Stins, M.F.1    Gilles, F.2    Kim, K.S.3
  • 47
    • 0015100243 scopus 로고
    • The transmissible nature of enterotoxin production in human enteropathogenic strain of Escherichia coli
    • Smith HW, Linggood MA. The transmissible nature of enterotoxin production in human enteropathogenic strain of Escherichia coli. J Med Microbiol 1971; 4: 301-305.
    • (1971) J Med Microbiol , vol.4 , pp. 301-305
    • Smith, H.W.1    Linggood, M.A.2
  • 48
    • 0022512195 scopus 로고
    • Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities
    • Strockbine NA, Marques LR, Newland JW, et al. Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities. Infect Immun 1986; 53: 135-140.
    • (1986) Infect Immun , vol.53 , pp. 135-140
    • Strockbine, N.A.1    Marques, L.R.2    Newland, J.W.3
  • 49
    • 0023219973 scopus 로고
    • Effects of cycloheximide and puromycin on cytotoxic activity of Escherichia coli verocytotoxin (Shiga-like toxin)
    • Petric M, Karmali MA, Arbus GS, et al. Effects of cycloheximide and puromycin on cytotoxic activity of Escherichia coli verocytotoxin (Shiga-like toxin). J Clin Microbiol 1987; 25: 1265-1268.
    • (1987) J Clin Microbiol , vol.25 , pp. 1265-1268
    • Petric, M.1    Karmali, M.A.2    Arbus, G.S.3
  • 50
    • 0023695342 scopus 로고
    • Serological differences between verocytotoxin 2 and Shiga-like toxin II
    • Head SC, Karmali MA, Roscoe ME, et al. Serological differences between verocytotoxin 2 and Shiga-like toxin II. Lancet 1988; 2: 751.
    • (1988) Lancet , vol.2 , pp. 751
    • Head, S.C.1    Karmali, M.A.2    Roscoe, M.E.3
  • 51
    • 0021946215 scopus 로고
    • The association between idiopathic hemolytic uremic syndrome and infection by verotoxin-producing Escherichia coli
    • Karmali MA, Petric M, Lim C, et al. The association between idiopathic hemolytic uremic syndrome and infection by verotoxin-producing Escherichia coli. J Infect Dis 1985; 151: 775-782. (Pubitemid 15094592)
    • (1985) Journal of Infectious Diseases , vol.151 , Issue.5 , pp. 775-782
    • Karmali, M.A.1    Petric, M.2    Lim, C.3
  • 52
    • 79952505809 scopus 로고    scopus 로고
    • Scanning Electron Microscopy
    • Springer
    • Reichelt R. Scanning Electron Microscopy. In: Science of Microscopy. Springer, 2007. pp. 133-272.
    • (2007) Science of Microscopy , pp. 133-272
    • Reichelt, R.1
  • 53
    • 33745156457 scopus 로고    scopus 로고
    • Modular digital holographic microscopy system for marker free quantitative phase contrast imaging of living cells
    • Kemper B, Carl D, Höink A, et al. Modular digital holographic microscopy system for marker free quantitative phase contrast imaging of living cells. Proc SPIE 2006; 6191: 61910T.
    • (2006) Proc SPIE , vol.6191
    • Kemper, B.1    Carl, D.2    Höink, A.3
  • 54
    • 12344282852 scopus 로고    scopus 로고
    • Parameter-optimized digital holographic microscope for high-resolution living-cell analysis
    • DOI 10.1364/AO.43.006536
    • Carl D, Kemper B, Wernicke G, et al. Parameter-optimized digital holographic microscope for high-resolution living-cell analysis. Appl Opt 2004; 43: 6536-6544. (Pubitemid 40120770)
    • (2004) Applied Optics , vol.43 , Issue.36 , pp. 6536-6544
    • Carl, D.1    Kemper, B.2    Wernicke, G.3    Von Bally, G.4
  • 55
    • 33748462726 scopus 로고    scopus 로고
    • Investigation of living pancreas tumor cells by digital holographic microscopy
    • Kemper B, Carl D, Schnekenburger J, et al. Investigation of living pancreas tumor cells by digital holographic microscopy. J Biomed Opt 2006; 11: 34005.
    • (2006) J Biomed Opt , vol.11 , pp. 34005
    • Kemper, B.1    Carl, D.2    Schnekenburger, J.3
  • 56
    • 79952506491 scopus 로고    scopus 로고
    • Label-free quantitative cell division monitoring of endothelial cells by digital holographic microscopy
    • Kemper B, Bauwens A, Vollmer A et al. Label-free quantitative cell division monitoring of endothelial cells by digital holographic microscopy. J Biomed Opt 2010; 15: 036009.
    • (2010) J Biomed Opt , vol.15 , pp. 036009
    • Kemper, B.1    Bauwens, A.2    Vollmer, A.3
  • 57
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, et al. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide and flow cytometry. J Immunol Methods 1991; 139: 271-279.
    • (1991) J Immunol Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3
  • 58
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins - From cell biology to biomedical applications
    • Johannes L, Römer W. Shiga toxins - from cell biology to biomedical applications. Nat Rev Microbiol 2010; 8: 105-116.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 105-116
    • Johannes, L.1    Römer, W.2
  • 59
    • 0037217906 scopus 로고    scopus 로고
    • Induction of apoptosis of human brain microvascular endothelial cells by Shiga toxin 1
    • DOI 10.1086/345861
    • Ergonul Z, Hughes AK, Kohan DE. Induction of apoptosis of human brain microvascular endothelial cells by Shiga toxin 1. J Infect Dis 2003; 187: 154-158. (Pubitemid 36034486)
    • (2003) Journal of Infectious Diseases , vol.187 , Issue.1 , pp. 154-158
    • Ergonul, Z.1    Hughes, A.K.2    Kohan, D.E.3
  • 60
    • 41149089223 scopus 로고    scopus 로고
    • Glycosphingolipids in vascular endothelial cells: Relationship of heterogeneity in Gb3Cer/CD77 receptor expression with differential Shiga toxin 1 cytotoxicity
    • Schweppe CH, Bielaszewska M, Pohlentz G, et al. Glycosphingolipids in vascular endothelial cells: relationship of heterogeneity in Gb3Cer/CD77 receptor expression with differential Shiga toxin 1 cytotoxicity. Glycoconj J 2008; 25: 291-304.
    • (2008) Glycoconj J , vol.25 , pp. 291-304
    • Schweppe, C.H.1    Bielaszewska, M.2    Pohlentz, G.3
  • 62
    • 0028301437 scopus 로고
    • Glycosphingolipid receptor function is modified by fatty acid content. Verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues
    • Kiarash A, Boyd B, Lingwood CA. Glycosphingolipid receptor function is modified by fatty acid content. Verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues. J Biol Chem 1994; 269: 11138-11146.
    • (1994) J Biol Chem , vol.269 , pp. 11138-11146
    • Kiarash, A.1    Boyd, B.2    Lingwood, C.A.3
  • 63
    • 0029923621 scopus 로고    scopus 로고
    • Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes: Comparison of a supported bilayer film and liposomes
    • DOI 10.1007/BF00731490
    • Arab S, Lingwood CA. Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes: comparison of a supported bilayer film and liposomes. Glycoconj J 1996; 13: 159-166. (Pubitemid 26132723)
    • (1996) Glycoconjugate Journal , vol.13 , Issue.2 , pp. 159-166
    • Arab, S.1    Lingwood, C.A.2
  • 64
    • 0035900715 scopus 로고    scopus 로고
    • Kinetic analysis of binding between Shiga toxin and receptor glycolipid Gb3Cer by surface plasmon resonance
    • Nakajima H, Kiyokawa N, Katagiri YU, et al. Kinetic analysis of binding between Shiga toxin and receptor glycolipid Gb3Cer by surface plasmon resonance. J Biol Chem 2001; 276: 42915-42922.
    • (2001) J Biol Chem , vol.276 , pp. 42915-42922
    • Nakajima, H.1    Kiyokawa, N.2    Katagiri, Y.U.3
  • 65
    • 0036694806 scopus 로고    scopus 로고
    • Effect of globotriaosyl ceramide fatty acid α-hydroxylation on the binding by verotoxin 1 and verotoxin 2
    • Binnington B, Lingwood D, Nutikka A, et al. Effect of globotriaosyl ceramide fatty acid α-hydroxylation on the binding by verotoxin 1 and verotoxin 2. Neurochem Res 2002; 27: 807-813.
    • (2002) Neurochem Res , vol.27 , pp. 807-813
    • Binnington, B.1    Lingwood, D.2    Nutikka, A.3
  • 66
    • 0032559646 scopus 로고    scopus 로고
    • Toxin entry: Retrograde transport through the secretory pathway
    • DOI 10.1083/jcb.140.4.733
    • Lord JM, Roberts LM. Toxin entry: retrograde transport through the secretory pathway. J Cell Biol 1998; 140: 733-736. (Pubitemid 28141213)
    • (1998) Journal of Cell Biology , vol.140 , Issue.4 , pp. 733-736
    • Lord, J.M.1    Roberts, L.M.2
  • 67
    • 48749104439 scopus 로고    scopus 로고
    • Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies
    • Tam P, Mahfoud R, Nutikka A, et al. Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies. J Cell Physiol 2008; 216: 750-763.
    • (2008) J Cell Physiol , vol.216 , pp. 750-763
    • Tam, P.1    Mahfoud, R.2    Nutikka, A.3
  • 68
    • 0023787493 scopus 로고
    • The histopathology of the hemolytic uremic syndrome associated with verocytotoxin-producing Escherichia coli infections
    • Richardson SE, Karmali MA, Becker LE, et al. The histopathology of the hemolytic uremic syndrome associated with verocytotoxin-producing Escherichia coli infections. Hum Pathol 1988; 19: 1102-1108.
    • (1988) Hum Pathol , vol.19 , pp. 1102-1108
    • Richardson, S.E.1    Karmali, M.A.2    Becker, L.E.3
  • 70
    • 0036139657 scopus 로고    scopus 로고
    • Escherichia coli harboring Shiga toxin 2 gene variants: Frequency and association with clinical symptoms
    • Friedrich AW, Bielaszewska M, Zhang W, et al. Escherichia coli harboring Shiga toxin 2 gene variants: frequency and association with clinical symptoms. J Infect Dis 2002; 185: 74-84.
    • (2002) J Infect Dis , vol.185 , pp. 74-84
    • Friedrich, A.W.1    Bielaszewska, M.2    Zhang, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.