메뉴 건너뛰기




Volumn 76, Issue 12, 2008, Pages 5677-5685

Evidence that membrane rafts are not required for the action of Clostridium perfringens enterotoxin

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CLAUDIN 4; ENTEROTOXIN; METHYL BETA CYCLODEXTRIN; OCCLUDIN;

EID: 57349151474     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00854-08     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • Abrami, L., S. H. Leppla, and F. G. van der Goot. 2006. Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. J. Cell Biol. 172:309-320.
    • (2006) J. Cell Biol , vol.172 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    van der Goot, F.G.3
  • 2
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • Abrami, L., and F. G. van Der Goot. 1999. Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J. Cell Biol. 147:175-184.
    • (1999) J. Cell Biol , vol.147 , pp. 175-184
    • Abrami, L.1    van Der Goot, F.G.2
  • 3
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:111-136.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 4
    • 0042905943 scopus 로고    scopus 로고
    • Death pathways activated in CaCo-2 cells by Clostridium perfringens enterotoxin
    • Chakrabarti, G., X. Zhou, and B. A. McClane. 2003. Death pathways activated in CaCo-2 cells by Clostridium perfringens enterotoxin. Infect. Immun. 71:4260-4270.
    • (2003) Infect. Immun , vol.71 , pp. 4260-4270
    • Chakrabarti, G.1    Zhou, X.2    McClane, B.A.3
  • 5
    • 34447565868 scopus 로고    scopus 로고
    • Differential incorporation of docosahexaenoic acid into distinct cholesterol-rich membrane raft domains
    • Duraisamy, Y., D. Lambert, C. A. O'Neill, and P. J. Padfield. 2007. Differential incorporation of docosahexaenoic acid into distinct cholesterol-rich membrane raft domains. Biochem. Biophys. Res. Commun. 360:885-890.
    • (2007) Biochem. Biophys. Res. Commun , vol.360 , pp. 885-890
    • Duraisamy, Y.1    Lambert, D.2    O'Neill, C.A.3    Padfield, P.J.4
  • 6
    • 0032840311 scopus 로고    scopus 로고
    • Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance
    • Francis, S. A., J. M. Kelly, J. McCormack, R. A. Rogers, J. Lai, E. E. Schneeberger, and R. D. Lynch. 1999. Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance. Eur. J. Cell Biol. 78:473-484.
    • (1999) Eur. J. Cell Biol , vol.78 , pp. 473-484
    • Francis, S.A.1    Kelly, J.M.2    McCormack, J.3    Rogers, R.A.4    Lai, J.5    Schneeberger, E.E.6    Lynch, R.D.7
  • 7
    • 0034617463 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein
    • Fujita, K., J. Katahira, Y. Horiguchi, N. Sonoda, M. Furuse, and S. Tsukita. 2000. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett. 476:258-261.
    • (2000) FEBS Lett , vol.476 , pp. 258-261
    • Fujita, K.1    Katahira, J.2    Horiguchi, Y.3    Sonoda, N.4    Furuse, M.5    Tsukita, S.6
  • 8
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse, M., H. Sasaki, and S. Tsukita. 1999. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J. Cell Biol. 147:891-903.
    • (1999) J. Cell Biol , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 9
    • 23844478566 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin listeriolysin O aggregates rafts via oligomerization
    • Gekara, N. O., T. Jacobs, T. Chakraborty, and S. Weiss. 2005. The cholesterol-dependent cytolysin listeriolysin O aggregates rafts via oligomerization. Cell. Microbiol. 7:1345-1356.
    • (2005) Cell. Microbiol , vol.7 , pp. 1345-1356
    • Gekara, N.O.1    Jacobs, T.2    Chakraborty, T.3    Weiss, S.4
  • 10
    • 44349126582 scopus 로고    scopus 로고
    • A novel splice variant of occludin deleted in exon 9 and its role in cell apoptosis and invasion
    • Gu, J. M., S. O. Lim, Y. M. Park, and G. Jung. 2008. A novel splice variant of occludin deleted in exon 9 and its role in cell apoptosis and invasion. FEBS J. 275:3145-3156.
    • (2008) FEBS J , vol.275 , pp. 3145-3156
    • Gu, J.M.1    Lim, S.O.2    Park, Y.M.3    Jung, G.4
  • 11
    • 1842588541 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin
    • Hale, M. L., J. C. Marvaud, M. R. Popoff, and B. G. Stiles. 2004. Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin. Infect. Immun. 72:2186-2193.
    • (2004) Infect. Immun , vol.72 , pp. 2186-2193
    • Hale, M.L.1    Marvaud, J.C.2    Popoff, M.R.3    Stiles, B.G.4
  • 12
    • 0032808735 scopus 로고    scopus 로고
    • Cationic currents induced by Clostridium perfringens type A enterotoxin in human intestinal CaCO-2 cells
    • Hardy, S. P., M. Denmead, N. Parekh, and P. E. Granum. 1999. Cationic currents induced by Clostridium perfringens type A enterotoxin in human intestinal CaCO-2 cells. J. Med. Microbiol. 48:235-243.
    • (1999) J. Med. Microbiol , vol.48 , pp. 235-243
    • Hardy, S.P.1    Denmead, M.2    Parekh, N.3    Granum, P.E.4
  • 13
    • 34547116657 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium regulates intercellular junction proteins and facilitates transepithelial neutrophil and bacterial passage
    • Kohler, H., T. Sakaguchi, B. P. Hurley, B. J. Kase, H. C. Reinecker, and B. A. McCormick. 2007. Salmonella enterica serovar Typhimurium regulates intercellular junction proteins and facilitates transepithelial neutrophil and bacterial passage. Am. J. Physiol. Gastrointest. Liver Physiol. 293:G178-G187.
    • (2007) Am. J. Physiol. Gastrointest. Liver Physiol , vol.293
    • Kohler, H.1    Sakaguchi, T.2    Hurley, B.P.3    Kase, B.J.4    Reinecker, H.C.5    McCormick, B.A.6
  • 15
    • 17644421069 scopus 로고    scopus 로고
    • Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins
    • Lambert, D., C. A. O'Neill, and P. J. Padfield. 2005. Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins. Biochem. J. 387:553-560.
    • (2005) Biochem. J , vol.387 , pp. 553-560
    • Lambert, D.1    O'Neill, C.A.2    Padfield, P.J.3
  • 17
    • 33750959086 scopus 로고    scopus 로고
    • Surveillance for foodborne-disease outbreaks - United States, 1998-2002
    • Lynch, M., J. Painter, R. Woodruff, and C. Braden. 2006. Surveillance for foodborne-disease outbreaks - United States, 1998-2002. MMWR Surveill. Summ. 55:1-34.
    • (2006) MMWR Surveill. Summ , vol.55 , pp. 1-34
    • Lynch, M.1    Painter, J.2    Woodruff, R.3    Braden, C.4
  • 18
    • 34250800879 scopus 로고    scopus 로고
    • Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin
    • Lynch, R. D., S. A. Francis, K. M. McCarthy, E. Casas, C. Thiele, and E. E. Schneeberger. 2007. Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin. Exp. Cell Res. 313:2597-2610.
    • (2007) Exp. Cell Res , vol.313 , pp. 2597-2610
    • Lynch, R.D.1    Francis, S.A.2    McCarthy, K.M.3    Casas, E.4    Thiele, C.5    Schneeberger, E.E.6
  • 19
    • 0028226528 scopus 로고
    • Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes
    • McClane, B. A. 1994. Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes. Toxicology 87:43-67.
    • (1994) Toxicology , vol.87 , pp. 43-67
    • McClane, B.A.1
  • 20
    • 0025032332 scopus 로고
    • Studies of Clostridium perfringens enterotoxin action at different temperatures demonstrate a correlation between complex formation and cytotoxicity
    • McClane, B. A., and A. P. Wnek. 1990. Studies of Clostridium perfringens enterotoxin action at different temperatures demonstrate a correlation between complex formation and cytotoxicity. Infect. Immun. 58:3109-3115.
    • (1990) Infect. Immun , vol.58 , pp. 3109-3115
    • McClane, B.A.1    Wnek, A.P.2
  • 21
    • 0024264146 scopus 로고
    • Production, purification, and assay of Clostridium perfringens enterotoxin
    • McDonel, J. L., and B. A. McClane. 1988. Production, purification, and assay of Clostridium perfringens enterotoxin. Methods Enzymol. 165:94-103.
    • (1988) Methods Enzymol , vol.165 , pp. 94-103
    • McDonel, J.L.1    McClane, B.A.2
  • 22
    • 0037130957 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of Madin-Darby canine kidney cells and rat synaptosomes
    • Miyata, S., J. Minami, E. Tamai, O. Matsushita, S. Shimamoto, and A. Okabe. 2002. Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of Madin-Darby canine kidney cells and rat synaptosomes. J. Biol. Chem. 277:39463-39468.
    • (2002) J. Biol. Chem , vol.277 , pp. 39463-39468
    • Miyata, S.1    Minami, J.2    Tamai, E.3    Matsushita, O.4    Shimamoto, S.5    Okabe, A.6
  • 23
    • 0141703462 scopus 로고    scopus 로고
    • Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells
    • Nagahama, M., S. Hayashi, S. Morimitsu, and J. Sakurai. 2003. Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells. J. Biol. Chem. 278:36934-36941.
    • (2003) J. Biol. Chem , vol.278 , pp. 36934-36941
    • Nagahama, M.1    Hayashi, S.2    Morimitsu, S.3    Sakurai, J.4
  • 26
    • 33746085241 scopus 로고    scopus 로고
    • Pike, L. J. 2006. Rafts defined: a report on the Keystone Symposium on lipid rafts and cell function. J. Lipid Res. 47:1597-1598.
    • Pike, L. J. 2006. Rafts defined: a report on the Keystone Symposium on lipid rafts and cell function. J. Lipid Res. 47:1597-1598.
  • 27
    • 34848838008 scopus 로고    scopus 로고
    • Compositional and stoichiometric analysis of Clostridium perfringens enterotoxin complexes in Caco-2 cells and claudin 4 fibroblast transfectants
    • Robertson, S. L., J. G. Smedley III, U. Singh, G. Chakrabarti, C. M. Van Itallie, J. M. Anderson, and B. A. McClane. 2007. Compositional and stoichiometric analysis of Clostridium perfringens enterotoxin complexes in Caco-2 cells and claudin 4 fibroblast transfectants. Cell. Microbiol. 9:2734-2755.
    • (2007) Cell. Microbiol , vol.9 , pp. 2734-2755
    • Robertson, S.L.1    Smedley III, J.G.2    Singh, U.3    Chakrabarti, G.4    Van Itallie, C.M.5    Anderson, J.M.6    McClane, B.A.7
  • 28
    • 0035823597 scopus 로고    scopus 로고
    • Comparative biochemical and immunocytochemical studies reveal differences in the effects of Clostridium perfringens enterotoxin on polarized CaCo-2 cells versus Vero cells
    • Singh, U., L. L. Mitic, E. U. Wieckowski, J. M. Anderson, and B. A. McClane. 2001. Comparative biochemical and immunocytochemical studies reveal differences in the effects of Clostridium perfringens enterotoxin on polarized CaCo-2 cells versus Vero cells. J. Biol. Chem. 276:33402-33412.
    • (2001) J. Biol. Chem , vol.276 , pp. 33402-33412
    • Singh, U.1    Mitic, L.L.2    Wieckowski, E.U.3    Anderson, J.M.4    McClane, B.A.5
  • 29
    • 0034674563 scopus 로고    scopus 로고
    • CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin
    • Singh, U., C. M. Van Itallie, L. L. Mitic, J. M. Anderson, and B. A. McClane. 2000. CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin. J. Biol. Chem. 275:18407-18417.
    • (2000) J. Biol. Chem , vol.275 , pp. 18407-18417
    • Singh, U.1    Van Itallie, C.M.2    Mitic, L.L.3    Anderson, J.M.4    McClane, B.A.5
  • 30
    • 34248398456 scopus 로고    scopus 로고
    • Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxin
    • Smedley, J. G., III, F. A. Uzal, and B. A. McClane. 2007. Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxin. Infect. Immun. 75:2381-2390.
    • (2007) Infect. Immun , vol.75 , pp. 2381-2390
    • Smedley III, J.G.1    Uzal, F.A.2    McClane, B.A.3
  • 31
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley, S. J., and H. R. Saibil. 2006. The mechanism of pore formation by bacterial toxins. Curr. Opin. Struct. Biol. 16:230-236.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 35
    • 0028768185 scopus 로고
    • Evidence that an approximately 50-kDa mammalian plasma membrane protein with receptor-like properties mediates the amphiphilicity of specifically bound Clostridium perfringens enterotoxin
    • Wieckowski, E. U., A. P. Wnek, and B. A. McClane. 1994. Evidence that an approximately 50-kDa mammalian plasma membrane protein with receptor-like properties mediates the amphiphilicity of specifically bound Clostridium perfringens enterotoxin. J. Biol. Chem. 269:10838- 10848.
    • (1994) J. Biol. Chem , vol.269 , pp. 10838-10848
    • Wieckowski, E.U.1    Wnek, A.P.2    McClane, B.A.3
  • 36
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Wong, V. 1997. Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273:C1859-C1867.
    • (1997) Am. J. Physiol , vol.273
    • Wong, V.1
  • 37
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J. A., and R. J. Collier. 2007. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76:243-265.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.