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Volumn 2, Issue 6, 2010, Pages 1515-1535

Shiga toxins: Intracellular trafficking to the ER leading to activation of host cell stress responses

Author keywords

Apoptosis; ER stress response; Retrograde transport; Ribotoxic stress response; Shiga toxins

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; BACTERIUM LIPOPOLYSACCHARIDE; CELL SURFACE RECEPTOR; DEATH RECEPTOR 5; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN IRE1; SHIGA TOXIN; STRESS ACTIVATED PROTEIN KINASE; VEROTOXIN 1; VEROTOXIN 2;

EID: 79952085254     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins2061515     Document Type: Article
Times cited : (25)

References (130)
  • 1
    • 77949399113 scopus 로고    scopus 로고
    • Renal diseases in the Pediatric Intensive Care Unit: Thrombotic microangiopathy, hemolytic uremic syndrome, and thrombotic thrombocytopenic purpura
    • Wheeler, D.S., Wong, H.R., Shanley, T.P., Eds.; Springer Verlag: London, UK
    • Proulx, F.; Tesh V.L. Renal diseases in the Pediatric Intensive Care Unit: Thrombotic microangiopathy, hemolytic uremic syndrome, and thrombotic thrombocytopenic purpura. In Pediatric Critical Care Medicine: Basic Science and Clinical Evidence; Wheeler, D.S., Wong, H.R., Shanley, T.P., Eds.; Springer Verlag: London, UK, 2007; pp. 1189-1204.
    • (2007) Pediatric Critical Care Medicine: Basic Science and Clinical Evidence , pp. 1189-1204
    • Proulx, F.1    Tesh, V.L.2
  • 2
    • 51549116628 scopus 로고    scopus 로고
    • Treatment and outcome of Shiga-toxin-associated hemolytic uremic syndrome (HUS)
    • Scheiring, J.; Andreoli, S.P.; Zimmerhackl, L.B. Treatment and outcome of Shiga-toxin-associated hemolytic uremic syndrome (HUS). Pediatr. Nephrol. 2008, 23, 1749-1760.
    • (2008) Pediatr. Nephrol , vol.23 , pp. 1749-1760
    • Scheiring, J.1    Andreoli, S.P.2    Zimmerhackl, L.B.3
  • 3
    • 24044469996 scopus 로고    scopus 로고
    • Enterohaemorrhagic Escherichia coli in human medicine
    • Karch, H.; Tarr, P.I.; 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
  • 4
    • 0018903835 scopus 로고
    • CNS manifestations of the hemolytic-uremic syndrome. Relationship to metabolic alterations and prognosis
    • Bale, J.F.; Brasher, C.; Siegler, R.L. CNS manifestations of the hemolytic-uremic syndrome. Relationship to metabolic alterations and prognosis. Am. J. Dis. Child. 1980, 134, 869-872.
    • (1980) Am. J. Dis. Child , vol.134 , pp. 869-872
    • Bale, J.F.1    Brasher, C.2    Siegler, R.L.3
  • 8
    • 0344061522 scopus 로고    scopus 로고
    • Characterization of the baboon responses to Shiga-like toxin: Descriptive study of a new primate model of toxic responses to Stx-1
    • Taylor, F.B.; Tesh, V.L.; DeBault, L.; Li, A.; Chang, A.C.K.; Kosanke, S.D.; Pysher, T.J.; Siegler, R.L. Characterization of the baboon responses to Shiga-like toxin: Descriptive study of a new primate model of toxic responses to Stx-1. Am. J. Path. 1999, 154, 1285-1299.
    • (1999) Am. J. Path , vol.154 , pp. 1285-1299
    • Taylor, F.B.1    Tesh, V.L.2    Debault, L.3    Li, A.4    Chang, A.C.K.5    Kosanke, S.D.6    Pysher, T.J.7    Siegler, R.L.8
  • 11
    • 0037209059 scopus 로고    scopus 로고
    • Shiga toxin receptor glycolipid binding. Pathology and utility
    • Philpott, D., Ebel. F., Eds.; Humana Press, Inc.: Totowa, NJ, USA
    • Lingwood,C.A. Shiga toxin receptor glycolipid binding. Pathology and utility. In Methods in Molecular Medicine. E. coli Shiga Toxin Methods and Protocols; Philpott, D., Ebel. F., Eds.; Humana Press, Inc.: Totowa, NJ, USA, 2003; Volume 73, pp. 165-186.
    • (2003) Methods in Molecular Medicine. E. coli Shiga Toxin Methods and Protocols , vol.73 , pp. 165-186
    • Lingwood, C.A.1
  • 13
    • 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
  • 14
    • 0025749699 scopus 로고
    • Investigation of Shiga-like toxin binding to chemically synthesized oligosaccharide sequences
    • Armstrong, G.D.; Fodor, E.; Vanmaele, R. Investigation of Shiga-like toxin binding to chemically synthesized oligosaccharide sequences. J. Infect. Dis. 1991, 164, 1160-1167.
    • (1991) J. Infect. Dis , vol.164 , pp. 1160-1167
    • Armstrong, G.D.1    Fodor, E.2    Vanmaele, R.3
  • 15
    • 0002441116 scopus 로고    scopus 로고
    • Clinical trials of Synsorb-Pk in preventing hemolytic-uremic syndrome
    • coli Strains; Kaper, J.B., O'Brien, A.D., Eds.; ASM Press: Washington, DC, USA
    • Armstrong, G.D.; McLaine, P.N.; Rowe, P.C. Clinical trials of Synsorb-Pk in preventing hemolytic-uremic syndrome. In Escherichia coli O157:H7 and Other Shiga toxin-producing E. coli Strains; Kaper, J.B., O'Brien, A.D., Eds.; ASM Press: Washington, DC, USA, 1998; pp. 374-384.
    • (1998) Escherichia Coli O157:H7 and Other Shiga Toxin-producing E , pp. 374-384
    • Armstrong, G.D.1    McLaine, P.N.2    Rowe, P.C.3
  • 16
    • 0041411080 scopus 로고    scopus 로고
    • Effect of an oral Shiga toxin-binding agent on diarrhea-associated Hemolytic Uremic Syndrome in children: A randomized controlled trial
    • Trachtman, H.; Cnaan, A.; Christen, E.; Gibbs, K.; Zhao, S.; Acheson, D.W.K.; Weiss, R.; Kaskel, F.J.; Spitzer, A.; Hirschman, G.H. Effect of an oral Shiga toxin-binding agent on diarrhea-associated Hemolytic Uremic Syndrome in children: A randomized controlled trial. JAMA 2003, 290, 1337-1344.
    • (2003) JAMA , vol.290 , pp. 1337-1344
    • Trachtman, H.1    Cnaan, A.2    Christen, E.3    Gibbs, K.4    Zhao, S.5    Acheson, D.W.K.6    Weiss, R.7    Kaskel, F.J.8    Spitzer, A.9    Hirschman, G.H.10
  • 18
    • 34548490308 scopus 로고    scopus 로고
    • Identification and characterization of small molecules that inhibit intracellular toxin transport
    • Saenz, J.B.; Doggett, T.A.; Haslam, D.B. Identification and characterization of small molecules that inhibit intracellular toxin transport. Infect. Immun. 2007, 75, 4552-4561.
    • (2007) Infect. Immun , vol.75 , pp. 4552-4561
    • Saenz, J.B.1    Doggett, T.A.2    Haslam, D.B.3
  • 20
    • 2442573691 scopus 로고    scopus 로고
    • Refinement of a therapeutic Shiga toxin-Binding probiotic for human trials
    • Pinyon, R.A.; Paton, J.C.; Paton, A.W.; Botten, J.A.; Morona, R. Refinement of a therapeutic Shiga toxin-Binding probiotic for human trials. J. Infect. Dis. 2004, 189, 1547-1555.
    • (2004) J. Infect. Dis , vol.189 , pp. 1547-1555
    • Pinyon, R.A.1    Paton, J.C.2    Paton, A.W.3    Botten, J.A.4    Morona, R.5
  • 21
    • 0022512195 scopus 로고
    • Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities
    • Strockbine, N.A.; Marques, L.R.M.; Newland, J.W.; Williams-Smith, H.; Holmes, R.K.; O'Brien, A.D. 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.M.2    Newland, J.W.3    Williams-Smith, H.4    Holmes, R.K.5    O'Brien, A.D.6
  • 23
    • 0023121139 scopus 로고
    • Nucleotide sequence analysis of the structural genes for Shiga-like toxin I encoded by bacteriophage 933J from Escherichia coli
    • Jackson, M. P.; Newland, J.W.; Holmes, R.K.; O'Brien, A.D. Nucleotide sequence analysis of the structural genes for Shiga-like toxin I encoded by bacteriophage 933J from Escherichia coli. Microb. Pathog. 1987, 2, 147-153.
    • (1987) Microb. Pathog , vol.2 , pp. 147-153
    • Jackson, M.P.1    Newland, J.W.2    Holmes, R.K.3    O'Brien, A.D.4
  • 25
    • 0028367338 scopus 로고
    • Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 Å resolution
    • Fraser, M.E.; Chernaia, M.M.; Kozlov, Y.V.; James, M.N.G. Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 Å resolution. Nat. Struct. Biol. 1994, 1, 59-64.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 59-64
    • Fraser, M.E.1    Chernaia, M.M.2    Kozlov, Y.V.3    James, M.N.G.4
  • 27
    • 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.; Takeda, Y.; Ogasawara, T.; Igarashi, K. 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    Takeda, Y.4    Ogasawara, T.5    Igarashi, K.6
  • 28
    • 0024558887 scopus 로고
    • Shiga toxin, Shiga-like toxin II variant, and ricin are all single-site RNA N-glycosidases of 28 S RNA when microinjected into Xenopus oocytes
    • Saxena, S.K.; O''Brien, A.D.; Ackerman, E.J. Shiga toxin, Shiga-like toxin II variant, and ricin are all single-site RNA N-glycosidases of 28 S RNA when microinjected into Xenopus oocytes. J. Biol. Chem. 1989, 264, 596-601.
    • (1989) J. Biol. Chem , vol.264 , pp. 596-601
    • Saxena, S.K.1    O''brien, A.D.2    Ackerman, E.J.3
  • 29
    • 0024564286 scopus 로고
    • Endocytosis from coated pits of Shiga toxin: A glycolipid-binding protein from Shigella dysenteriae 1
    • Sandvig, K.; Olsnes, S.; Brown, J.E.; Petersen, O.W.; van Deurs, B. Endocytosis from coated pits of Shiga toxin: A glycolipid-binding protein from Shigella dysenteriae 1. J. Cell Biol. 1989, 108, 1331-1343.
    • (1989) J. Cell Biol , vol.108 , pp. 1331-1343
    • Sandvig, K.1    Olsnes, S.2    Brown, J.E.3    Petersen, O.W.4    van Deurs, B.5
  • 30
    • 77957898655 scopus 로고    scopus 로고
    • Endocytosis and retrograde transport of Shiga toxin
    • 2009, doi 10.1016/j.toxicon
    • Sandvig, K.; Bergan, J.; Dyve, A.-B.; Skotland, T.; Torgersen, M.L. Endocytosis and retrograde transport of Shiga toxin. Toxicon 2009, doi 10.1016/j.toxicon.2009.11.021.
    • (2009) Toxicon , vol.11 , pp. 21
    • Sandvig, K.1    Bergan, J.2    Dyve, A.-B.3    Skotland, T.4    Torgersen, M.L.5
  • 31
    • 0024375644 scopus 로고
    • Globotetraosylceramide is recognized by the pig edema disease toxin
    • DeGrandis, S.; Law, H.; Brunton, J.; Gyles, C.; Lingwood, C.A. Globotetraosylceramide is recognized by the pig edema disease toxin. J. Biol. Chem. 1989, 264, 12520-12525.
    • (1989) J. Biol. Chem , vol.264 , pp. 12520-12525
    • Degrandis, S.1    Law, H.2    Brunton, J.3    Gyles, C.4    Lingwood, C.A.5
  • 33
  • 34
    • 0033062483 scopus 로고    scopus 로고
    • The identification of three biologically relevant globotriaosyl ceramide receptor binding sites on the Verotoxin 1 B subunit
    • Bast, D.J.; Banerjee, L.; Clark, C.; Read, R.J.; Brunton, J.L. The identification of three biologically relevant globotriaosyl ceramide receptor binding sites on the Verotoxin 1 B subunit. Mol. Microbiol. 1999, 32, 953-960.
    • (1999) Mol. Microbiol , vol.32 , pp. 953-960
    • Bast, D.J.1    Banerjee, L.2    Clark, C.3    Read, R.J.4    Brunton, J.L.5
  • 36
    • 33744519950 scopus 로고    scopus 로고
    • Targeted Disruption of Gb3/CD77 Synthase Gene Resulted In the Complete Deletion of Globo-series Glycosphingolipids and Loss of Sensitivity to Verotoxins
    • Okuda, T.; Tokuda, N.; Numata, S.; Ito, M.; Ohta, M.; Kawamura, K.; Wiels, J.; Urano, T.; Tajima, O.; Furukawa, K. Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion of globo-series glycosphingolipids and loss of sensitivity to verotoxins. J. Biol. Chem. 2006, 281, 10230-10235.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10230-10235
    • Okuda, T.1    Tokuda, N.2    Numata, S.3    Ito, M.4    Ohta, M.5    Kawamura, K.6    Wiels, J.7    Urano, T.8    Tajima, O.9    Furukawa, K.10
  • 37
    • 79952093082 scopus 로고    scopus 로고
    • Receptors for bacterial toxins
    • Burns, D.L., Barbieri, J.T., Iglewski, B.H., Rappuoli, R., Eds.; ASM Press: Washington, DC, USA
    • Saelinger, C.B. Receptors for bacterial toxins. In Bacterial Protein Toxins; Burns, D.L., Barbieri, J.T., Iglewski, B.H., Rappuoli, R., Eds.; ASM Press: Washington, DC, USA, 2003; pp. 131-148.
    • (2003) Bacterial Protein Toxins , pp. 131-148
    • Saelinger, C.B.1
  • 38
    • 0036694806 scopus 로고    scopus 로고
    • Effect of globotriaosyl ceramide fatty acid alpha-hydroxylation on the binding by verotoxin 1 and verotoxin 2
    • Binnington, B.; Lingwood, D.; Nutikka, A.; Lingwood, C.A. Effect of globotriaosyl ceramide fatty acid alpha-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    Lingwood, C.A.4
  • 40
    • 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
    • Arab, S.; Lingwood, C.A. 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.
    • (1996) Glycoconj. J , vol.13 , pp. 159-166
    • Arab, S.1    Lingwood, C.A.2
  • 41
    • 0031773458 scopus 로고    scopus 로고
    • Intracellular targeting of the endoplasmic reticulum/nuclear envelope by retrograde transport may determine cell hypersensitivity to verotoxin via globotriaosyl ceramide fatty acid isoform traffic
    • Arab, S.; Lingwood, C.A. Intracellular targeting of the endoplasmic reticulum/nuclear envelope by retrograde transport may determine cell hypersensitivity to verotoxin via globotriaosyl ceramide fatty acid isoform traffic. J. Cell. Physiol. 1998, 177, 646-660.
    • (1998) J. Cell. Physiol , vol.177 , pp. 646-660
    • Arab, S.1    Lingwood, C.A.2
  • 42
    • 1342284069 scopus 로고    scopus 로고
    • Interaction of Shiga toxin from Escherichia coli with human intestinal epithelial cell lines and explants: Stx2 induces epithelial damage in organ culture
    • Schüller, S.; Frankel, G.; Phillips, A.D. Interaction of Shiga toxin from Escherichia coli with human intestinal epithelial cell lines and explants: Stx2 induces epithelial damage in organ culture. Cell. Microbiol. 2004, 6, 289-301.
    • (2004) Cell. Microbiol , vol.6 , pp. 289-301
    • Schüller, S.1    Frankel, G.2    Phillips, A.D.3
  • 43
    • 36448958290 scopus 로고    scopus 로고
    • Differential binding of Shiga toxin 2 to human and murine neutrophils
    • Griener, T.P.; Mulvey, G.L.; Marcato, P.; Armstrong, G.D. Differential binding of Shiga toxin 2 to human and murine neutrophils. J. Med. Microbiol. 2007, 56, 1423-1430.
    • (2007) J. Med. Microbiol , vol.56 , pp. 1423-1430
    • Griener, T.P.1    Mulvey, G.L.2    Marcato, P.3    Armstrong, G.D.4
  • 44
    • 0023787493 scopus 로고
    • The histopathology of the hemolytic uremic syndrome associated with verocytotoxin-producing Escherichia coli infections
    • Richardson, S.E.; Karmali, M.A.; Becker, L.E.; Smith, C.R. 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    Smith, C.R.4
  • 45
    • 0002394738 scopus 로고
    • Pathology of the hemolytic uremic syndrome
    • Kaplan, B.S., Trompeter, R.S., Moake, J.L., Eds.; Decker: New York, NY, USA
    • Habib, R. Pathology of the hemolytic uremic syndrome. In Hemolytic Uremic Syndrome and Thrombotic Thrombocytopenic Purpura; Kaplan, B.S., Trompeter, R.S., Moake, J.L., Eds.; Decker: New York, NY, USA, 1992; pp. 315-353.
    • (1992) Hemolytic Uremic Syndrome and Thrombotic Thrombocytopenic Purpura , pp. 315-353
    • Habib, R.1
  • 49
    • 62449181018 scopus 로고    scopus 로고
    • Shiga toxins, glycosphingolipid diversity, and endothelial cell injury
    • Müthing, J.; Schweppe, C.H.; Karch, H.; Friedrich, A.W. 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    Friedrich, A.W.4
  • 50
    • 0034877295 scopus 로고    scopus 로고
    • Shiga toxins
    • Sandvig, K. Shiga toxins. Toxicon 2001, 39, 1629-1635.
    • (2001) Toxicon , vol.39 , pp. 1629-1635
    • Sandvig, K.1
  • 51
    • 77953127589 scopus 로고    scopus 로고
    • Protein toxins from plants and bacteria: Probes for intracellular transport and tools in medicine
    • 2010, doi:10.1016/j.febslet
    • Sandvig, K.; Torgersen, M.L.; Engedal, N.; Skotland, T.; Iversen, T.G. Protein toxins from plants and bacteria: Probes for intracellular transport and tools in medicine. FEBS Lett. 2010, doi:10.1016/j.febslet.2010.04.008.
    • (2010) FEBS Lett , vol.4 , pp. 008
    • Sandvig, K.1    Torgersen, M.L.2    Engedal, N.3    Skotland, T.4    Iversen, T.G.5
  • 52
    • 0029009879 scopus 로고
    • Role of processing and intracellular transport for optimal toxicity of Shiga toxin and toxin mutants
    • Garred, Ø.; Dubinina, E.; Holm, P.K.; Olsnes, S.; van Deurs, B.; Kozlov, J.V.; Sandvig, K. 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    Olsnes, S.4    van Deurs, B.5    Kozlov, J.V.6    Sandvig, K.7
  • 53
    • 0028961149 scopus 로고
    • Furin-induced cleavage and activation of Shiga toxin
    • Garred, Ø.; van Deurs, B.; Sandvig, K. Furin-induced cleavage and activation of Shiga toxin. J. Biol. Chem. 1995, 270, 10817-10821.
    • (1995) J. Biol. Chem , vol.270 , pp. 10817-10821
    • Garred, O.1    van Deurs, B.2    Sandvig, K.3
  • 54
    • 0025729065 scopus 로고
    • Endocytosis and intracellular transport of the glycolipid-binding ligand Shiga toxin in polarized MDCK cells
    • Sandvig, K.; Prydz, K.; Ryd, M.; van Deurs, B. Endocytosis and intracellular transport of the glycolipid-binding ligand Shiga toxin in polarized MDCK cells. J. Cell Biol. 1991, 113, 553-562.
    • (1991) J. Cell Biol , vol.113 , pp. 553-562
    • Sandvig, K.1    Prydz, K.2    Ryd, M.3    van Deurs, B.4
  • 56
    • 3042639390 scopus 로고    scopus 로고
    • Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin
    • Lauvrak, S.U.; Torgersen, M.L.; Sandvig, K. Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin. J. Cell Sci. 2004, 117, 2321-2331.
    • (2004) J. Cell Sci , vol.117 , pp. 2321-2331
    • Lauvrak, S.U.1    Torgersen, M.L.2    Sandvig, K.3
  • 57
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguières, T.; Mallard, F.; Baron, C.; Hanau, D.; Lingwood, C.; Goud, B.; Salamero, J.; Johannes, L. Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 2001, 12, 2453-2468.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguières, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5    Goud, B.6    Salamero, J.7    Johannes, L.8
  • 58
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport
    • Mallard, F.; Antony, C.; Tenza, D.; Salamero, J.; Goud, B.; Johannes, L. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport. J. Cell Biol. 1998, 143, 973-990.
    • (1998) J. Cell Biol , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 59
    • 6344274847 scopus 로고    scopus 로고
    • A cycling cis-Golgi protein mediates endosome-to-Golgi traffic
    • Natarajan, R.; Linstedt, A.D. A cycling cis-Golgi protein mediates endosome-to-Golgi traffic. Mol. Biol. Cell 2004, 15, 4798-4806.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4798-4806
    • Natarajan, R.1    Linstedt, A.D.2
  • 60
    • 0027375270 scopus 로고
    • Inefficient degradation of triglyceride-rich lipoprotein by HepG2 cells is due to a retarded transport to the lysosomal compartment
    • Lombardi, P.; Mulder, M.; van der Boom, H.; Frants, R.R.; Havekes, L.M. Inefficient degradation of triglyceride-rich lipoprotein by HepG2 cells is due to a retarded transport to the lysosomal compartment. J. Biol. Chem. 1993, 268, 26113-26119.
    • (1993) J. Biol. Chem , vol.268 , pp. 26113-26119
    • Lombardi, P.1    Mulder, M.2    van der Boom, H.3    Frants, R.R.4    Havekes, L.M.5
  • 61
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer, M.A.; Soldati, T.; Shapiro, A.D.; Lin, J.; Pfeffer, S.R. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 1994, 125, 573-582.
    • (1994) J. Cell Biol , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.R.5
  • 62
    • 0035008062 scopus 로고    scopus 로고
    • Cholesterol requirement for cation-independent mannose 6-phosphate receptor exit from multivesicular late endosomes to the Golgi
    • Miwako, I.; Yamamoto, A.; Kitamura, T.; Nagayama, K.; Ohashi, M. Cholesterol requirement for cation-independent mannose 6-phosphate receptor exit from multivesicular late endosomes to the Golgi. J. Cell Sci. 2001, 114, 1765-1776.
    • (2001) J. Cell Sci , vol.114 , pp. 1765-1776
    • Miwako, I.1    Yamamoto, A.2    Kitamura, T.3    Nagayama, K.4    Ohashi, M.5
  • 63
    • 1342296932 scopus 로고    scopus 로고
    • Transport of toxins across intracellular membranes
    • Burns, D.L., Barbieri, J.T., Iglewski, B.H., Rappuoli, R., Eds.; ASM Press: Washington, DC, USA
    • Sandvig, K. Transport of toxins across intracellular membranes. In Bacterial Protein Toxins; Burns, D.L., Barbieri, J.T., Iglewski, B.H., Rappuoli, R., Eds.; ASM Press: Washington, DC, USA, 2003; pp. 157-172.
    • (2003) Bacterial Protein Toxins , pp. 157-172
    • Sandvig, K.1
  • 66
    • 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
  • 70
    • 34347364716 scopus 로고    scopus 로고
    • The retromer component sorting nexin-1 is required for efficient retrograde transport of Shiga toxin from early endosome to the trans Golgi network
    • Bujny, M.V.; Popoff, V.; Johannes, L.; Cullen, P.J. The retromer component sorting nexin-1 is required for efficient retrograde transport of Shiga toxin from early endosome to the trans Golgi network. J. Cell Sci. 2007, 120, 2010-2021.
    • (2007) J. Cell Sci , vol.120 , pp. 2010-2021
    • Bujny, M.V.1    Popoff, V.2    Johannes, L.3    Cullen, P.J.4
  • 72
    • 0032969203 scopus 로고    scopus 로고
    • The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Jackson, M.E.; Simpson, J.C.; Girod, A.; Pepperkok, R.; Roberts, L.M.; Lord, J.M. The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum. J. Cell Sci. 1999, 112, 467-475.
    • (1999) J. Cell Sci , vol.112 , pp. 467-475
    • Jackson, M.E.1    Simpson, J.C.2    Girod, A.3    Pepperkok, R.4    Roberts, L.M.5    Lord, J.M.6
  • 75
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • Sandvig, K.; Garred, Ø.; Prydz, K.; Kozlov, J.V.; Hansen, S.H.; van Deurs, B. 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    Kozlov, J.V.4    Hansen, S.H.5    van Deurs, B.6
  • 76
    • 0034661251 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic protein mediates verotoxin II-induced cell death: Possible association between Bcl-2 and tissue failure by E. coli O157:H7
    • Suzuki, A.; Doi, H.; Matsuzawa, F.; Aikawa, S.; Takiguchi, K.; Kawano, H.; Hayashida, M.; Ohno, S. Bcl-2 antiapoptotic protein mediates verotoxin II-induced cell death: possible association between Bcl-2 and tissue failure by E. coli O157:H7. Genes Dev. 2000, 14, 1734-1740.
    • (2000) Genes Dev , vol.14 , pp. 1734-1740
    • Suzuki, A.1    Doi, H.2    Matsuzawa, F.3    Aikawa, S.4    Takiguchi, K.5    Kawano, H.6    Hayashida, M.7    Ohno, S.8
  • 79
    • 0036710553 scopus 로고    scopus 로고
    • Exploitation of the endoplasmic reticulum by bacterial pathogens
    • Roy, C.R. Exploitation of the endoplasmic reticulum by bacterial pathogens. Trends Microbiol. 2002, 10, 418-424.
    • (2002) Trends Microbiol , vol.10 , pp. 418-424
    • Roy, C.R.1
  • 80
    • 77956288440 scopus 로고    scopus 로고
    • Cholera toxin: An intracellular journey into the cytosol by way of the endoplasmic reticulum
    • Wernick, N.L.B.; Chinnapen, D.J.-F; Cho, J.A.; Lencer, W.I. Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum. Toxins 2010, 2, 310-325.
    • (2010) Toxins , vol.2 , pp. 310-325
    • Wernick, N.L.B.1    Chinnapen, D.J.-F.2    Cho, J.A.3    Lencer, W.I.4
  • 82
    • 16244400431 scopus 로고    scopus 로고
    • Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone HEDJ/ERdj3
    • Yu, M.; Haslam, D.B. Shiga toxin is transported from the endoplasmic reticulum following interaction with the luminal chaperone HEDJ/ERdj3. Infect. Immun. 2005, 73, 2524-2532.
    • (2005) Infect. Immun , vol.73 , pp. 2524-2532
    • Yu, M.1    Haslam, D.B.2
  • 83
    • 32544457086 scopus 로고    scopus 로고
    • Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23
    • Falguières, T.; Johannes, L. Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23. Biol. Cell 2006, 98, 125-134.
    • (2006) Biol. Cell , vol.98 , pp. 125-134
    • Falguières, T.1    Johannes, L.2
  • 85
    • 0030973162 scopus 로고    scopus 로고
    • Ribotoxic stress response: Activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA
    • Iordanov, M.S.; Pribnow, D.; Magun, J.L.; Dinh, T.-H.; Pearson, J.A.; Chen, S.L.; Magun, B.E. Ribotoxic stress response: Activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA. Mol. Cell. Biol. 1997, 17, 3373-3381.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 3373-3381
    • Iordanov, M.S.1    Pribnow, D.2    Magun, J.L.3    Dinh, T.-H.4    Pearson, J.A.5    Chen, S.L.6    Magun, B.E.7
  • 86
    • 33646457879 scopus 로고    scopus 로고
    • Shiga toxin 1-induced cytokine production is mediated by MAP kinase pathways and translation initiation factor eIF4E in the macrophage-like THP-1 cell line
    • Cherla, R.P.; Lee, S.-Y.; Mees, P.L.; Tesh, V.L. Shiga toxin 1-induced cytokine production is mediated by MAP kinase pathways and translation initiation factor eIF4E in the macrophage-like THP-1 cell line. J. Leukoc. Biol. 2006, 79, 397-407.
    • (2006) J. Leukoc. Biol , vol.79 , pp. 397-407
    • Cherla, R.P.1    Lee, S.-Y.2    Mees, P.L.3    Tesh, V.L.4
  • 87
    • 0037373313 scopus 로고    scopus 로고
    • Shiga toxin 1 triggers a ribotoxic stress response leading to p38 and JNK activation and induction of apoptosis in intestinal epithelial cells
    • Smith, W.E.; Kane, A.V.; Campbell, S.T.; Acheson, D.W.K.; Cochran, B.H.; Thorpe, C.M. Shiga toxin 1 triggers a ribotoxic stress response leading to p38 and JNK activation and induction of apoptosis in intestinal epithelial cells. Infect. Immun. 2003, 71, 1497-1504.
    • (2003) Infect. Immun , vol.71 , pp. 1497-1504
    • Smith, W.E.1    Kane, A.V.2    Campbell, S.T.3    Acheson, D.W.K.4    Cochran, B.H.5    Thorpe, C.M.6
  • 88
    • 0036141198 scopus 로고    scopus 로고
    • Shiga toxin 1-induced activation of c-Jun NH(2)-terminal kinase and p38 in the human monocytic cell line THP-1: Possible involvement in the production of TNF-alpha
    • Foster, G.H.; Tesh, V.L. Shiga toxin 1-induced activation of c-Jun NH(2)-terminal kinase and p38 in the human monocytic cell line THP-1: Possible involvement in the production of TNF-alpha. J. Leukoc. Biol.2002, 71, 107-114.
    • (2002) J. Leukoc. Biol , vol.71 , pp. 107-114
    • Foster, G.H.1    Tesh, V.L.2
  • 89
    • 0041589432 scopus 로고    scopus 로고
    • Role of double-stranded RNA-activated protein kinase R (PKR) in deoxynivalenol-induced ribotoxic stress response
    • Zhou, H.R.; Lau, A.S.; Pestka, J.J. Role of double-stranded RNA-activated protein kinase R (PKR) in deoxynivalenol-induced ribotoxic stress response. Toxicol. Sci. 2003, 74, 335-344.
    • (2003) Toxicol. Sci , vol.74 , pp. 335-344
    • Zhou, H.R.1    Lau, A.S.2    Pestka, J.J.3
  • 90
    • 45249123044 scopus 로고    scopus 로고
    • ZAK: A MAP3Kinase that transduces Shiga toxin- and ricin-induced proinflammatory cytokine expression
    • Jandhyala, D.M.; Ahluwalia, A.; Obrig, T.; Thorpe, C.M. ZAK: A MAP3Kinase that transduces Shiga toxin- and ricin-induced proinflammatory cytokine expression. Cell. Microbiol. 2008, 10, 1468-1477.
    • (2008) Cell. Microbiol , vol.10 , pp. 1468-1477
    • Jandhyala, D.M.1    Ahluwalia, A.2    Obrig, T.3    Thorpe, C.M.4
  • 91
    • 0035968287 scopus 로고    scopus 로고
    • Novel role for JNK as a stress-activated Bcl2 kinase
    • Deng, X.; Xiao, L.; Lang, W.; Gao, F.; Ruvolo, P.; May, W.S. Novel role for JNK as a stress-activated Bcl2 kinase. J. Biol. Chem. 2001, 276, 23681-23688.
    • (2001) J. Biol. Chem , vol.276 , pp. 23681-23688
    • Deng, X.1    Xiao, L.2    Lang, W.3    Gao, F.4    Ruvolo, P.5    May, W.S.6
  • 93
    • 23344441474 scopus 로고    scopus 로고
    • Shiga toxin 1 induces apoptosis in the human myelogenous leukemia cell line THP-1 by a caspase-8-dependent, tumor necrosis factor receptor-independent mechanism
    • Lee, S.-Y.; Cherla, R.P.; Caliskan, I.; Tesh, V.L. Shiga toxin 1 induces apoptosis in the human myelogenous leukemia cell line THP-1 by a caspase-8-dependent, tumor necrosis factor receptor-independent mechanism. Infect. Immun. 2005, 73, 5115-5126.
    • (2005) Infect. Immun , vol.73 , pp. 5115-5126
    • Lee, S.-Y.1    Cherla, R.P.2    Caliskan, I.3    Tesh, V.L.4
  • 94
    • 77949368508 scopus 로고    scopus 로고
    • Induction of apoptosis by Shiga toxins
    • Tesh, V.L. Induction of apoptosis by Shiga toxins. Future Microbiol. 2010, 5, 431-453.
    • (2010) Future Microbiol , vol.5 , pp. 431-453
    • Tesh, V.L.1
  • 95
    • 1642463408 scopus 로고    scopus 로고
    • Verotoxin activates mitogen-activated protein kinase in human peripheral blood monocytes: Role in apoptosis and proinflammatory cytokine release
    • Cameron, P.; Smith, S.J.; Giembycz, M.A.; Rotondo, D.; Plevin, R. Verotoxin activates mitogen-activated protein kinase in human peripheral blood monocytes: role in apoptosis and proinflammatory cytokine release. Br. J. Pharmacol. 2003, 140, 1320-1330.
    • (2003) Br. J. Pharmacol , vol.140 , pp. 1320-1330
    • Cameron, P.1    Smith, S.J.2    Giembycz, M.A.3    Rotondo, D.4    Plevin, R.5
  • 96
    • 14644423253 scopus 로고    scopus 로고
    • Comparative evaluation of apoptosis induced by Shiga toxin 1 and/or lipopolysaccharides in human monocytic and macrophage-like cells
    • Harrison, L.M.; Cherla, R.P.; van den Hoogen, C.; van Haaften, W.C.E.; Lee, S.-Y.; Tesh, V.L. Comparative evaluation of apoptosis induced by Shiga toxin 1 and/or lipopolysaccharides in human monocytic and macrophage-like cells. Microb. Pathog. 2005, 38, 63-76.
    • (2005) Microb. Pathog , vol.38 , pp. 63-76
    • Harrison, L.M.1    Cherla, R.P.2    van den Hoogen, C.3    van Haaften, W.C.E.4    Lee, S.-Y.5    Tesh, V.L.6
  • 98
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J.; Sambrook, J. Protein folding in the cell. Nature 1992, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 99
    • 0043093689 scopus 로고    scopus 로고
    • Getting a grip on non-native proteins
    • Stirling, P.C.; Lundin, V.F.; Leroux, M.R. Getting a grip on non-native proteins. EMBO Rep. 2003, 4, 565-570.
    • (2003) EMBO Rep , vol.4 , pp. 565-570
    • Stirling, P.C.1    Lundin, V.F.2    Leroux, M.R.3
  • 100
    • 0033953974 scopus 로고    scopus 로고
    • Protein folding in vivo: The importance of molecular chaperones
    • Feldman, D.E.; Frydman, J. Protein folding in vivo: The importance of molecular chaperones. Curr. Opin. Struct. Biol. 2000, 10, 26-33.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 26-33
    • Feldman, D.E.1    Frydman, J.2
  • 102
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L.; Helenius, A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 2003, 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 103
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D.; Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 2007, 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 104
    • 7444240833 scopus 로고    scopus 로고
    • The ER chaperone BiP is a master regulator of ER function
    • L.M. The ER chaperone BiP is a master regulator of ER function. Mt. Sinai J. Med. 2004, 71, 289-297.
    • (2004) Mt. Sinai J. Med , vol.71 , pp. 289-297
  • 105
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: A matter of life or death
    • Boyce, M.; Yuan, J. Cellular response to endoplasmic reticulum stress: A matter of life or death. Cell Death Differ. 2006, 13, 363-373.
    • (2006) Cell Death Differ , vol.13 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 106
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M.; Kaufman, R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 2005, 74, 739-789.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 107
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi, E.; Logue, S.E.; Gorman, A.M.; Samali, A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep. 2006, 7, 880-885.
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 108
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H.; Matsui, T.; Yamamoto, A.; Okada, T.; Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107, 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 109
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M.; Zeng, H.; Urano, F.; Till, J. H.; Hubbard, S.R.; Harding, H.P.; Clark, S.G.; Ron, D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002, 415, 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 110
  • 111
    • 4444253303 scopus 로고    scopus 로고
    • Survival and apoptosis signals in ER stress: The role of protein kinases
    • Kadowaki, H.; Nishitoh, H.; Ichijo, H. Survival and apoptosis signals in ER stress: The role of protein kinases. J. Chem. Neuroanat. 2004, 28, 93-100.
    • (2004) J. Chem. Neuroanat , vol.28 , pp. 93-100
    • Kadowaki, H.1    Nishitoh, H.2    Ichijo, H.3
  • 113
    • 38849180895 scopus 로고    scopus 로고
    • Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells
    • Lee, S.-Y.; Lee, M.-S.; Cherla, R.P.; Tesh, V.L. Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells. Cell. Microbiol. 2008, 10, 770-780.
    • (2008) Cell. Microbiol , vol.10 , pp. 770-780
    • Lee, S.-Y.1    Lee, M.-S.2    Cherla, R.P.3    Tesh, V.L.4
  • 115
    • 8544283103 scopus 로고    scopus 로고
    • Chop is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi, H.; Wang, H.G. CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J. Biol. Chem. 2004, 279, 45495-45502.
    • (2004) J. Biol. Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 116
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough, K.D.; Martindale, J.L.; Klotz, L.O.; Aw, T.Y.; Holbrook, N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 2001, 21, 1249-1259.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 118
    • 48749112866 scopus 로고    scopus 로고
    • Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways
    • Wolfson, J.J.; May, K.L.; Thorpe, C.M.; Jandhyala, D.M.; Paton, J.C.; Paton, A.W. Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways. Cell. Microbiol. 2008, 10, 1775-1786.
    • (2008) Cell. Microbiol , vol.10 , pp. 1775-1786
    • Wolfson, J.J.1    May, K.L.2    Thorpe, C.M.3    Jandhyala, D.M.4    Paton, J.C.5    Paton, A.W.6
  • 119
    • 66149128432 scopus 로고    scopus 로고
    • Role of GRP78/BiP degradation and ER stress in deoxynivalenol-induced interleukin-6 upregulation in the macrophage
    • Shi, Y.; Porter, K.; Parameswaran, N.; Bae, H.K.; Pestka, J.J. Role of GRP78/BiP degradation and ER stress in deoxynivalenol-induced interleukin-6 upregulation in the macrophage. Toxicol. Sci. 2009, 109, 247-255.
    • (2009) Toxicol. Sci , vol.109 , pp. 247-255
    • Shi, Y.1    Porter, K.2    Parameswaran, N.3    Bae, H.K.4    Pestka, J.J.5
  • 120
    • 0031581060 scopus 로고    scopus 로고
    • The role of calcium in the regulation of apoptosis
    • McConkey, D.J.; Orrenius, S. The role of calcium in the regulation of apoptosis. Biochem. Biophys. Res. Commun. 1997, 239, 357-366.
    • (1997) Biochem. Biophys. Res. Commun , vol.239 , pp. 357-366
    • McConkey, D.J.1    Orrenius, S.2
  • 122
    • 0141754206 scopus 로고    scopus 로고
    • Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria
    • Filippin, L.; Magalhaes, P.J.; Di Benedetto, G.; Colella, M.; Pozzan, T. Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria. J. Biol. Chem. 2003, 278, 39224-39234.
    • (2003) J. Biol. Chem , vol.278 , pp. 39224-39234
    • Filippin, L.1    Magalhaes, P.J.2    di Benedetto, G.3    Colella, M.4    Pozzan, T.5
  • 123
    • 0036312001 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
    • Boya, P.; Cohen, I.; Zamzami, N.; Vieira, H.L.; Kroemer, G. Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization. Cell Death Differ. 2002, 9, 465-467.
    • (2002) Cell Death Differ , vol.9 , pp. 465-467
    • Boya, P.1    Cohen, I.2    Zamzami, N.3    Vieira, H.L.4    Kroemer, G.5
  • 125
    • 69049120323 scopus 로고    scopus 로고
    • Shiga toxin 1-induced proinflammatory cytokine production is regulated by the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin signaling pathway
    • Cherla, R.P.; Lee, S.-Y.; Mulder, R.A.; Lee, M.-S.; Tesh, V.L. Shiga toxin 1-induced proinflammatory cytokine production is regulated by the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin signaling pathway. Infect. Immun. 2009, 77, 3919-3931.
    • (2009) Infect. Immun , vol.77 , pp. 3919-3931
    • Cherla, R.P.1    Lee, S.-Y.2    Mulder, R.A.3    Lee, M.-S.4    Tesh, V.L.5
  • 126
    • 33847725556 scopus 로고    scopus 로고
    • Simultaneous induction of apoptotic and survival signaling pathways in macrophage-like THP-1 cells by Shiga toxin 1
    • Lee, S.-Y.; Cherla, R.P.; Tesh, V.L. Simultaneous induction of apoptotic and survival signaling pathways in macrophage-like THP-1 cells by Shiga toxin 1. Infect. Immun. 2007, 75, 1291-1302.
    • (2007) Infect. Immun , vol.75 , pp. 1291-1302
    • Lee, S.-Y.1    Cherla, R.P.2    Tesh, V.L.3
  • 127
    • 72449135276 scopus 로고    scopus 로고
    • Bcl-2 regulates the onset of Shiga toxin 1-induced apoptosis in THP-1 cells
    • Lee, M.-S.; Cherla, R.P.; Leyva-Illades, D.; Tesh, V.L. Bcl-2 regulates the onset of Shiga toxin 1-induced apoptosis in THP-1 cells. Infect. Immun. 2009, 77, 5233-5344.
    • (2009) Infect. Immun , vol.77 , pp. 5233-5344
    • Lee, M.-S.1    Cherla, R.P.2    Leyva-Illades, D.3    Tesh, V.L.4
  • 128
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R.J.; Strasser, A. The BCL-2 protein family: Opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol.2008, 9, 47-59.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 129
    • 68149154728 scopus 로고    scopus 로고
    • BH3-only proteins and their roles in programmed cell death
    • Giam, M.; Huang, D.C.; Bouillet, P. BH3-only proteins and their roles in programmed cell death. Oncogene 2008, 27 (Suppl. 1), S128-S136.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Giam, M.1    Huang, D.C.2    Bouillet, P.3
  • 130
    • 77955284279 scopus 로고    scopus 로고
    • Signaling through C/EBP homology protein and death receptor 5, and calpain activation differentially regulates THP-1 cell maturation-dependent apoptosis induced by Shiga toxin type 1
    • doi:10.1128/IAI.00342-10
    • Lee, M.-S.; Cherla, R.P.; Lentz, E.K.; Leyva-Illades, D.; Tesh V.L. Signaling through C/EBP homology protein and death receptor 5, and calpain activation differentially regulates THP-1 cell maturation-dependent apoptosis induced by Shiga toxin type 1. Infect. Immun. 2010, doi:10.1128/IAI.00342-10.
    • (2010) Infect. Immun
    • Lee, M.-S.1    Cherla, R.P.2    Lentz, E.K.3    Leyva-Illades, D.4    Tesh, V.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.