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Volumn 147, Issue 1, 1999, Pages 195-204

Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier

Author keywords

Claudin; Clostridium perfringens enterotoxin; Epithelial barrier; Freezefracture; Tight junction

Indexed keywords

CLAUDIN; ENTEROTOXIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 0033523773     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.1.195     Document Type: Article
Times cited : (563)

References (42)
  • 1
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson, J.M., and C.M. Van Itallie. 1995. Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269:G467-G475.
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 3
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda, M.S., J.A. Whitney, C. Flores, S. Gonzalez, M. Cereijido, and K. Matter. 1996. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J. Cell Biol. 134:1031-1049.
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 4
    • 0025999560 scopus 로고
    • Isolation and characterization of transcripts induced by androgen withdrawal and apoptotic cell death in the rat ventral prostate
    • Bricht, M.M., and R.L. Miesfeld. 1991. Isolation and characterization of transcripts induced by androgen withdrawal and apoptotic cell death in the rat ventral prostate. Mol. Endocrinol. 5:1381-1388.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1381-1388
    • Bricht, M.M.1    Miesfeld, R.L.2
  • 5
    • 0030748172 scopus 로고    scopus 로고
    • COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos
    • Chen, Y.-H., C. Merzdorf, D.L. Paul, and D.A. Goodenough. 1997. COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos. J. Cell Biol. 138:891-899.
    • (1997) J. Cell Biol. , vol.138 , pp. 891-899
    • Chen, Y.-H.1    Merzdorf, C.2    Paul, D.L.3    Goodenough, D.A.4
  • 6
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M.G., and G.E. Palade. 1963. Junctional complexes in various epithelia. J. Cell Biol. 17:375-412.
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 7
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto, K. 1995. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Sci. 108:3443-3449.
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 8
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures
    • Furuse, M., K. Fujimoto, N. Sato, T. Hirase, Sa. Tsukita, and Sh. Tsukita. 1996. Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures. J. Cell Sci. 109:429-435.
    • (1996) J. Cell Sci. , vol.109 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, Sa.5    Tsukita, Sh.6
  • 9
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse, M., K. Fujita, T. Hiiragi, K. Fujimoto, and Sh. Tsukita. 1998a. Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141:1539-1550.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, Sh.5
  • 11
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse, M., H. Sasaki, K. Fujimoto, and Sh. Tsukita. 1998b. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143:391-401.
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, Sh.4
  • 12
    • 0342332387 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse, M., H. Sasaki, and Sh. Tsukita. 1999. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J. Cell Biol. 20:429-435.
    • (1999) J. Cell Biol. , vol.20 , pp. 429-435
    • Furuse, M.1    Sasaki, H.2    Tsukita, Sh.3
  • 14
    • 0023612699 scopus 로고
    • Structure, biochemistry, and assembly of epithelial tight junctions
    • Gumbiner, B. 1987. Structure, biochemistry, and assembly of epithelial tight junctions. Am. J. Physiol. 253:C749-C758.
    • (1987) Am. J. Physiol. , vol.253
    • Gumbiner, B.1
  • 15
    • 0027715358 scopus 로고
    • Breaking through the tight junction barrier
    • Gumbiner, B. 1993. Breaking through the tight junction barrier. J. Cell Biol. 123:1631-1633.
    • (1993) J. Cell Biol. , vol.123 , pp. 1631-1633
    • Gumbiner, B.1
  • 16
    • 0025914629 scopus 로고
    • Localization of the receptor-binding region of Clostridium perfringens enterotoxin utilizing cloned toxin fragments and synthetic peptides
    • Hanna, P.C., T.A. Mietzner, G.K. Schoolnik, and B.A. McClane. 1991. Localization of the receptor-binding region of Clostridium perfringens enterotoxin utilizing cloned toxin fragments and synthetic peptides. J. Biol. Chem. 17: 11037-11043.
    • (1991) J. Biol. Chem. , vol.17 , pp. 11037-11043
    • Hanna, P.C.1    Mietzner, T.A.2    Schoolnik, G.K.3    McClane, B.A.4
  • 17
    • 0026762963 scopus 로고
    • Mapping of functional regions of Clostridium perfringens type A enterotoxin
    • Hanna, P.C., E.H. Wieckowski, T.A. Mietzner, and B.A. McClane. 1992. Mapping of functional regions of Clostridium perfringens type A enterotoxin. Infect. Immun. 60:2110-2114.
    • (1992) Infect. Immun. , vol.60 , pp. 2110-2114
    • Hanna, P.C.1    Wieckowski, E.H.2    Mietzner, T.A.3    McClane, B.A.4
  • 18
    • 0032950502 scopus 로고    scopus 로고
    • Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues: Application of a novel fixation protocol using trichloroacetic acids (TCA) as a fixative
    • Hayashi, K., S. Yonemura, T. Matsui, Sa, Tsukita, and Sh. Tsukita. 1999. Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues: Application of a novel fixation protocol using trichloroacetic acids (TCA) as a fixative. J. Cell Sci. 112:1149-1158.
    • (1999) J. Cell Sci. , vol.112 , pp. 1149-1158
    • Hayashi, K.1    Yonemura, S.2    Matsui, T.3    Tsukita, S.4    Tsukita, Sh.5
  • 19
    • 0023493360 scopus 로고
    • Isolation and function of a Clostridium perfringens enterotoxin fragment
    • Horiguchi, Y., T. Akai, and G. Sakaguchi. 1987. Isolation and function of a Clostridium perfringens enterotoxin fragment. Infect. Immun. 55:2912-2915.
    • (1987) Infect. Immun. , vol.55 , pp. 2912-2915
    • Horiguchi, Y.1    Akai, T.2    Sakaguchi, G.3
  • 20
    • 0022640280 scopus 로고
    • Production and characterization of monoclonal antibodies to Clostridium perfringens enterotoxin
    • Horiguchi, Y., T. Uemura, Y. Kamata, S. Kozaki, and G. Sakaguchi. 1986. Production and characterization of monoclonal antibodies to Clostridium perfringens enterotoxin. Infect. Immun. 52:31-35.
    • (1986) Infect. Immun. , vol.52 , pp. 31-35
    • Horiguchi, Y.1    Uemura, T.2    Kamata, Y.3    Kozaki, S.4    Sakaguchi, G.5
  • 21
    • 0030846016 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin
    • Katahira, J., N. Inoue, Y. Horiguchi, M. Matsuda, and N. Sugimoto. 1997a. Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin. J. Cell Biol. 136:1239-1247.
    • (1997) J. Cell Biol. , vol.136 , pp. 1239-1247
    • Katahira, J.1    Inoue, N.2    Horiguchi, Y.3    Matsuda, M.4    Sugimoto, N.5
  • 22
    • 0030716491 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo
    • Katahira, J., H. Sugiyama, N. Inoue, Y. Horiguchi, M. Matsuda, and N. Sugimoto. 1997b. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. J. Biol. Chem. 272: 26652-26658.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26652-26658
    • Katahira, J.1    Sugiyama, H.2    Inoue, N.3    Horiguchi, Y.4    Matsuda, M.5    Sugimoto, N.6
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 2642614521 scopus 로고    scopus 로고
    • Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration
    • Martin-Padura, I., S. Lostaglio, M. Schneemann, L. Williams, M. Romano, P. Fruscella, C. Panzeri, A. Stoppacciaro, L. Ruco, A. Villa, et al. 1998. Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration. J. Cell Biol. 142:117-127.
    • (1998) J. Cell Biol. , vol.142 , pp. 117-127
    • Martin-Padura, I.1    Lostaglio, S.2    Schneemann, M.3    Williams, L.4    Romano, M.5    Fruscella, P.6    Panzeri, C.7    Stoppacciaro, A.8    Ruco, L.9    Villa, A.10
  • 25
    • 0018570524 scopus 로고
    • Calcium-independent and dependent steps in action of Clostridium perfringens enterotoxin on hela and vero cells
    • Matsuda, M., and N. Sugimoto. 1979. Calcium-independent and dependent steps in action of Clostridium perfringens enterotoxin on hela and vero cells. Biochem. Biophys. Res. Commun. 91:629-636.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 629-636
    • Matsuda, M.1    Sugimoto, N.2
  • 26
    • 0031886504 scopus 로고    scopus 로고
    • Biogenesis of tight junctions: The C-terminal domain of occludin mediates basolateral targeting
    • Matter, K., and M.S. Balda. 1998. Biogenesis of tight junctions: the C-terminal domain of occludin mediates basolateral targeting. J. Cell Sci. 111:511-519.
    • (1998) J. Cell Sci. , vol.111 , pp. 511-519
    • Matter, K.1    Balda, M.S.2
  • 28
    • 0019445849 scopus 로고
    • Protective effects of osmotic stabilizers on morphological and permeability alterations induced in Vero cells by Clostridium perfringens enterotoxin
    • McClane, B.A., and J.L. McDonel. 1981. Protective effects of osmotic stabilizers on morphological and permeability alterations induced in Vero cells by Clostridium perfringens enterotoxin. Biochim. Biophys. Acta. 641:401-409.
    • (1981) Biochim. Biophys. Acta. , vol.641 , pp. 401-409
    • McClane, B.A.1    McDonel, J.L.2
  • 29
    • 0023871271 scopus 로고
    • Divalent cation involvement in the action of Clostridium perfringens type A enterotoxin
    • McClane, B.A., A.P. Wnek, K.I. Hulkower, and P.C. Hanna. 1988. Divalent cation involvement in the action of Clostridium perfringens type A enterotoxin. J. Biol. Chem. 263:2423-2435.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2423-2435
    • McClane, B.A.1    Wnek, A.P.2    Hulkower, K.I.3    Hanna, P.C.4
  • 30
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita, K., M. Furuse, K. Fujimoto, and Sh. Tsukita. 1999a. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc. Natl. Acad. Sci. USA. 96:511-516.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, Sh.4
  • 31
    • 0033519348 scopus 로고    scopus 로고
    • Claudin-11/OSP-based tight junctions in myelinated sheaths of oligodendrocytes and Sertoli cells in testis
    • Morita, K., H. Sasaki, K. Fujimoto, M. Furuse, and Sh. Tsukita. 1999b. Claudin-11/OSP-based tight junctions in myelinated sheaths of oligodendrocytes and Sertoli cells in testis. J. Cell Biol. 145:579-588.
    • (1999) J. Cell Biol. , vol.145 , pp. 579-588
    • Morita, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, Sh.5
  • 32
    • 0031798631 scopus 로고    scopus 로고
    • Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes
    • Moroi, S., M. Saitou, K. Fujimoto, A. Sakakibara, M. Furuse, O. Yoshida, and Sh. Tsukita. 1998. Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes. Am. J. Physiol. 274:C1708-C1717.
    • (1998) Am. J. Physiol. , vol.274
    • Moroi, S.1    Saitou, M.2    Fujimoto, K.3    Sakakibara, A.4    Furuse, M.5    Yoshida, O.6    Tsukita, Sh.7
  • 33
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou, M., K. Fujimoto, Y. Doi, M. Itoh, T. Fujimoto, M. Furuse, H. Takano, T. Noda, and Sh. Tsukita. 1998. Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J. Cell Biol. 141:397-408.
    • (1998) J. Cell Biol. , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, Sh.9
  • 34
    • 0015713004 scopus 로고
    • Simplified method for purification of Clostridium perfringens type A enterotoxin
    • Sakaguchi, G., T. Uemura, and H. Riemann. 1973. Simplified method for purification of Clostridium perfringens type A enterotoxin. Appl. Microbiol. 27: 762-767.
    • (1973) Appl. Microbiol. , vol.27 , pp. 762-767
    • Sakaguchi, G.1    Uemura, T.2    Riemann, H.3
  • 35
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara, A., M. Furuse, M. Saitou, Y. Ando-Akatsuka, and Sh. Tsukita. 1997. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137:1393-1401.
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, Sh.5
  • 36
    • 0026752739 scopus 로고
    • Structure, function, and regulation of cellular tight junctions
    • Schneeberger, E.E., and R.D. Lynch. 1992. Structure, function, and regulation of cellular tight junctions. Am. J. Physiol. 262:L647-L661.
    • (1992) Am. J. Physiol. , vol.262
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 37
    • 0015846194 scopus 로고
    • Further observations on the fine structure of freeze-cleaved tight junctions
    • Staehelin, L.A. 1973. Further observations on the fine structure of freeze-cleaved tight junctions. J. Cell Sci. 13:763-786.
    • (1973) J. Cell Sci. , vol.13 , pp. 763-786
    • Staehelin, L.A.1
  • 38
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehelin, L.A. 1974. Structure and function of intercellular junctions. Int. Rev. Cytol. 39:191-283.
    • (1974) Int. Rev. Cytol. , vol.39 , pp. 191-283
    • Staehelin, L.A.1
  • 39
    • 0024211161 scopus 로고
    • Tight junction structure and ZO-1 constant are identical in two strains of Madin-Darby Canine Kidney cells which differ in transepithelial resistance
    • Stevenson, B.R., J.M. Anderson, D.A. Goodenough, and M.S. Mooseker. 1988. Tight junction structure and ZO-1 constant are identical in two strains of Madin-Darby Canine Kidney cells which differ in transepithelial resistance. J. Cell Biol. 107:2401-2408.
    • (1988) J. Cell Biol. , vol.107 , pp. 2401-2408
    • Stevenson, B.R.1    Anderson, J.M.2    Goodenough, D.A.3    Mooseker, M.S.4
  • 40
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight junction strands: Leading or supporting players?
    • Tsukita, Sh., and M. Furuse. 1999. Occludin and claudins in tight junction strands: leading or supporting players? Trend. Cell Biol. 9:268-273.
    • (1999) Trend. Cell Biol. , vol.9 , pp. 268-273
    • Tsukita, Sh.1    Furuse, M.2
  • 41
    • 0028246186 scopus 로고
    • Modulation of tight junction structure in blood-brain barrier endothelial cells. Effects of tissue culture, second messengers and cocultured astrocytes
    • Wolburg, H., J. Neuhaus, U. Kniesel, B. Krauss, E.-M. Schmid, M. Öcalan, C. Farrell, and W. Risau. 1994. Modulation of tight junction structure in blood-brain barrier endothelial cells. Effects of tissue culture, second messengers and cocultured astrocytes. J. Cell Sci. 107:1347-1357.
    • (1994) J. Cell Sci. , vol.107 , pp. 1347-1357
    • Wolburg, H.1    Neuhaus, J.2    Kniesel, U.3    Krauss, B.4    Schmid, E.-M.5    Öcalan, M.6    Farrell, C.7    Risau, W.8
  • 42
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong, V., and B.M. Gumbiner. 1997. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136:399-409.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2


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