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Volumn 102, Issue 4, 1998, Pages 813-820

Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin

Author keywords

Gastric ulcer; Gastritis; Helicobacter pylori; Tight junctions; Vacuolating toxin

Indexed keywords

BACTERIAL TOXIN; OCCLUDIN; UVOMORULIN;

EID: 0032528956     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI2764     Document Type: Article
Times cited : (218)

References (50)
  • 1
    • 84920247287 scopus 로고
    • Unidentified curved bacilli on gastric epithelium in active chronic gastritis
    • Warren, J.R., and B.J. Marshall. 1483. Unidentified curved bacilli on gastric epithelium in active chronic gastritis. Lancet. 1:1273-1275.
    • (1483) Lancet , vol.1 , pp. 1273-1275
    • Warren, J.R.1    Marshall, B.J.2
  • 2
    • 0027441698 scopus 로고
    • Helicobacter pylori: Microbiology of a "slow" bacterial infection
    • Blaser, M.J. 1993. Helicobacter pylori: microbiology of a "slow" bacterial infection. Trends Microbiol. 1:255-259.
    • (1993) Trends Microbiol. , vol.1 , pp. 255-259
    • Blaser, M.J.1
  • 3
    • 0027176157 scopus 로고
    • An international association between Helicobacter pylori infection and gastric cancer
    • Eurogast Study Group. 1993. An international association between Helicobacter pylori infection and gastric cancer. Lancet. 341:1359-1362.
    • (1993) Lancet , vol.341 , pp. 1359-1362
  • 5
    • 0028860071 scopus 로고
    • Analysis of expression of CagA and VacA virulence factors in 43 strains of H. pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin
    • Xiang, Z., S. Censini, P.F. Bayeli, J.L. Telford, N. Figura, R. Rappuoli, and A. Covacci. 1995. Analysis of expression of CagA and VacA virulence factors in 43 strains of H. pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin. Infect. Immun. 63:94-98.
    • (1995) Infect. Immun. , vol.63 , pp. 94-98
    • Xiang, Z.1    Censini, S.2    Bayeli, P.F.3    Telford, J.L.4    Figura, N.5    Rappuoli, R.6    Covacci, A.7
  • 10
    • 0026739795 scopus 로고
    • Purification and characterization of the vacuolating toxin from Helicobacter pylori
    • Cover, T.L., and M.J. Blaser. 1992. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J. Biol Chem. 267:10570-10575.
    • (1992) J. Biol Chem. , vol.267 , pp. 10570-10575
    • Cover, T.L.1    Blaser, M.J.2
  • 11
    • 0027479881 scopus 로고
    • Effects of ATPase inhibitors on the response of HeLa cells to Helicobacter pylori vacuolating toxin
    • Cover, T.L., L.Y. Reddy, and M.J. Blaser. 1993. Effects of ATPase inhibitors on the response of HeLa cells to Helicobacter pylori vacuolating toxin. Infect. Immun. 61:1427-1431.
    • (1993) Infect. Immun. , vol.61 , pp. 1427-1431
    • Cover, T.L.1    Reddy, L.Y.2    Blaser, M.J.3
  • 16
  • 18
    • 0030764202 scopus 로고    scopus 로고
    • Effect of Helicobacter pylori vacuolating toxin on maturation and extracellular release of procathepsin D and on epidermal growth factor degradation
    • Satin, B., N. Norais, J.L. Telford, R. Rappuoli, M. Murgia, C. Montecucco, and E. Papini. 1997. Effect of Helicobacter pylori vacuolating toxin on maturation and extracellular release of procathepsin D and on epidermal growth factor degradation. J. Biol. Chem. 272:25022-25028.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25022-25028
    • Satin, B.1    Norais, N.2    Telford, J.L.3    Rappuoli, R.4    Murgia, M.5    Montecucco, C.6    Papini, E.7
  • 20
    • 0029923910 scopus 로고    scopus 로고
    • The vacuolating cytotoxin of Helicobacter pylori
    • Cover, T.L. 1997. The vacuolating cytotoxin of Helicobacter pylori. Mol. Microbiol. 20:241-246.
    • (1997) Mol. Microbiol. , vol.20 , pp. 241-246
    • Cover, T.L.1
  • 21
    • 0030809535 scopus 로고    scopus 로고
    • Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating toxin, reveals its pattern of assembly
    • Cover, T.L., P.I. Hanson, and J.E. Heuser. 1997. Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating toxin, reveals its pattern of assembly. J. Cell Biol. 138:759-769.
    • (1997) J. Cell Biol. , vol.138 , pp. 759-769
    • Cover, T.L.1    Hanson, P.I.2    Heuser, J.E.3
  • 24
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco, C., E. Papini, and O. Schiavo. 1994. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346:92-98.
    • (1994) FEBS Lett. , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, O.3
  • 25
    • 0029068244 scopus 로고
    • Apical, basal, and lateral cues for epithelial polarization
    • Eaton, S., and K. Simons. 1995. Apical, basal, and lateral cues for epithelial polarization. Cell. 82:5-8.
    • (1995) Cell , vol.82 , pp. 5-8
    • Eaton, S.1    Simons, K.2
  • 26
    • 0001367397 scopus 로고
    • Structure, biochemistry, and assembly of tight junctions
    • Gumbiner, B. 1987. Structure, biochemistry, and assembly of tight junctions. Am. J. Physiol. 253:C749-C758.
    • (1987) Am. J. Physiol. , vol.253
    • Gumbiner, B.1
  • 27
    • 0026469077 scopus 로고
    • Molecular and cellular basis of immune protection of mucosal surfaces
    • Kraehenbuhl, J.P., and M.R. Neutra. 1992. Molecular and cellular basis of immune protection of mucosal surfaces. Physiol. Rev. 72:853-879.
    • (1992) Physiol. Rev. , vol.72 , pp. 853-879
    • Kraehenbuhl, J.P.1    Neutra, M.R.2
  • 28
    • 0021751195 scopus 로고
    • Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line. MDCK
    • Fuller, S., C.H. von Bonsdorf, and K. Simons. 1984. Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line. MDCK. Cell. 38:65-77.
    • (1984) Cell , vol.38 , pp. 65-77
    • Fuller, S.1    Von Bonsdorf, C.H.2    Simons, K.3
  • 29
    • 0025616203 scopus 로고
    • Established intestinal cell lines as model systems for electrolyte transport studies
    • Dharmsathphorn, K., and J.L. Madara. 1990. Established intestinal cell lines as model systems for electrolyte transport studies. Methods Enzymol. 192: 354-389.
    • (1990) Methods Enzymol. , vol.192 , pp. 354-389
    • Dharmsathphorn, K.1    Madara, J.L.2
  • 30
    • 0023925328 scopus 로고
    • Epithelial polarity, villin expression, and enterocytic differentiation of cultured human colon carcinoma cells: A survey of twenty cell lines
    • Chantret, I., A. Barbat, E. Dussaulx, M.G. Brattain, and A. Zweibaum. 1988. Epithelial polarity, villin expression, and enterocytic differentiation of cultured human colon carcinoma cells: a survey of twenty cell lines. Cancer Res. 48:1936-1942.
    • (1988) Cancer Res. , vol.48 , pp. 1936-1942
    • Chantret, I.1    Barbat, A.2    Dussaulx, E.3    Brattain, M.G.4    Zweibaum, A.5
  • 31
    • 0028948118 scopus 로고
    • Thyroid hormone regulates stromelysin expression, protease secretion and the morphogenetic potential of normal polarized mammary epithelial cells
    • Lopez-Barahona, M., I. Fialka, J.M. Gonzalez-Sancho, M. Asuncion, M. Gonzalez, T. Iglesias, J. Bernal, H. Beug, and A. Munoz. 1995. Thyroid hormone regulates stromelysin expression, protease secretion and the morphogenetic potential of normal polarized mammary epithelial cells. EMBO J. 14: 1145-1155.
    • (1995) EMBO J. , vol.14 , pp. 1145-1155
    • Lopez-Barahona, M.1    Fialka, I.2    Gonzalez-Sancho, J.M.3    Asuncion, M.4    Gonzalez, M.5    Iglesias, T.6    Bernal, J.7    Beug, H.8    Munoz, A.9
  • 33
    • 0017233794 scopus 로고
    • Membrane flow during pinocytosis. A stereological analysis
    • Steinman, R.M., S.E. Brodie, and Z.A. Chon. 1976. Membrane flow during pinocytosis. A stereological analysis. J. Cell. Biol. 68:665-687.
    • (1976) J. Cell. Biol. , vol.68 , pp. 665-687
    • Steinman, R.M.1    Brodie, S.E.2    Chon, Z.A.3
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0019964095 scopus 로고
    • Ion fluxes and electrical characteristics of the short-circuited rat colon in vitro
    • Gazitua, S., and J.W. Robinson. 1982. Ion fluxes and electrical characteristics of the short-circuited rat colon in vitro. Pflugers Arch. 394:32-37.
    • (1982) Pflugers Arch. , vol.394 , pp. 32-37
    • Gazitua, S.1    Robinson, J.W.2
  • 37
    • 0025823864 scopus 로고
    • Essential role of urease in pathogenesis of gastritis induced by helicobacter pylori in gnotobiotic piglets
    • Eaton, K.A., C.L. Brooks, D.R. Morgan, and S. Krakowka. 1991. Essential role of urease in pathogenesis of gastritis induced by helicobacter pylori in gnotobiotic piglets. Infect. Immun. 59:2470-2475.
    • (1991) Infect. Immun. , vol.59 , pp. 2470-2475
    • Eaton, K.A.1    Brooks, C.L.2    Morgan, D.R.3    Krakowka, S.4
  • 38
    • 0025979283 scopus 로고
    • Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity
    • Labigne, A., V. Cussac, and P. Courcoux. 1991. Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity. J. Bacteriol. 173:1920-1931.
    • (1991) J. Bacteriol. , vol.173 , pp. 1920-1931
    • Labigne, A.1    Cussac, V.2    Courcoux, P.3
  • 39
    • 0028064605 scopus 로고
    • A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach
    • Tsuda, M., M. Karita, M.G. Morshed, K. Okita, and T. Nakazawa. 1994. A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach. Infect. Immun. 62:3586-3589.
    • (1994) Infect. Immun. , vol.62 , pp. 3586-3589
    • Tsuda, M.1    Karita, M.2    Morshed, M.G.3    Okita, K.4    Nakazawa, T.5
  • 40
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and Zonula Occludens-1 form a complex during stages in the assembly of tight junctions
    • Rajasekaran, A.K., M. Hojo, T. Huima, and E. Rodriguez-Boulan. 1996. Catenins and Zonula Occludens-1 form a complex during stages in the assembly of tight junctions. J. Cell. Biol. 132:451-463.
    • (1996) J. Cell. Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 41
    • 0024292731 scopus 로고
    • Tight junction dynamic: Is paracellular transport regulated?
    • Madara, J.L. 1988. Tight junction dynamic: is paracellular transport regulated? Cell. 53:497-498.
    • (1988) Cell , vol.53 , pp. 497-498
    • Madara, J.L.1
  • 42
    • 0026942033 scopus 로고
    • Endothelial cells: Adhesion and tight junctions
    • Rubin, L.L. 1992. Endothelial cells: adhesion and tight junctions. Curr. Opin. Cell Biol. 4:830-833.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 830-833
    • Rubin, L.L.1
  • 43
    • 0030669302 scopus 로고    scopus 로고
    • Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation
    • Turner, J.R., B.K. Rill, S.L. Carlson, D. Carnes, R. Kerner, R.J. Mrsny, and J.L. Madara. 1997. Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation. Am. J. Physiol. 173:C1378-C1385.
    • (1997) Am. J. Physiol. , vol.173
    • Turner, J.R.1    Rill, B.K.2    Carlson, S.L.3    Carnes, D.4    Kerner, R.5    Mrsny, R.J.6    Madara, J.L.7
  • 46
    • 0029822812 scopus 로고    scopus 로고
    • Binding and internalization of the Helicobacter pylori vacuolating cytotoxin by epithelial cells
    • Garner, J.A., and T.L. Cover. 1996. Binding and internalization of the Helicobacter pylori vacuolating cytotoxin by epithelial cells. Infect. Immun. 46: 4197-4203.
    • (1996) Infect. Immun. , vol.46 , pp. 4197-4203
    • Garner, J.A.1    Cover, T.L.2
  • 48
    • 0028200510 scopus 로고
    • Hydrogen ion concentration in the mucus layer on top of acid-stimulated and -inhibited rat gastric mucosa
    • Schade, C., G. Flemstrom, and L. Holm. 1994. Hydrogen ion concentration in the mucus layer on top of acid-stimulated and -inhibited rat gastric mucosa. Gastroenterology. 107:180-188.
    • (1994) Gastroenterology , vol.107 , pp. 180-188
    • Schade, C.1    Flemstrom, G.2    Holm, L.3
  • 49
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • Jabri, E., M.B. Carr, R.P. Hausinger, and P.A. Karplus. 1995. The crystal structure of urease from Klebsiella aerogenes. Science. 268:998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 50
    • 0028930318 scopus 로고
    • Helicobacter pylori nickel-transport gene nixA: Synthesis of catalytically active urease in Escherichia coli independent of growth conditions
    • Mobley, H.L.T., R.M. Garner, and P. Bauerfeind. 1995. Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. Mol. Microbiol. 16:97-109.
    • (1995) Mol. Microbiol. , vol.16 , pp. 97-109
    • Mobley, H.L.T.1    Garner, R.M.2    Bauerfeind, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.