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Volumn 73, Issue , 2011, Pages 283-309

Tight junction pore and leak pathways: A dynamic duo

Author keywords

barrier function; claudin; occluding; paracellular permeability; ZO 1

Indexed keywords

PROTEIN ZO1;

EID: 79951775751     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev-physiol-012110-142150     Document Type: Article
Times cited : (695)

References (145)
  • 1
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M, Palade G. 1963. Junctional complexes in various epithelia. J. Cell Biol. 17:375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.1    Palade, G.2
  • 2
    • 0014782467 scopus 로고
    • A fine structural analysis of intercellular junctions in the mouse liver
    • Goodenough DA, Revel JP. 1970. A fine structural analysis of intercellular junctions in the mouse liver. J. Cell Biol. 45:272-90
    • (1970) J. Cell Biol. , vol.45 , pp. 272-290
    • Goodenough, D.A.1    Revel, J.P.2
  • 3
    • 0015384702 scopus 로고
    • Permeable junctional complexes.The movement of lanthanum across rabbit gallbladder and intestine
    • Machen TE, Erlij D, Wooding FB. 1972. Permeable junctional complexes.The movement of lanthanum across rabbit gallbladder and intestine. J. Cell Biol. 54:302-12
    • (1972) J. Cell Biol. , vol.54 , pp. 302-312
    • MacHen, T.E.1    Erlij, D.2    Wooding, F.B.3
  • 4
    • 0014129424 scopus 로고
    • Standing-gradient osmotic flow. A mechanism for coupling of water and solute transport in epithelia
    • Diamond JM, Bossert WH. 1967. Standing-gradient osmotic flow. A mechanism for coupling of water and solute transport in epithelia. J. Gen. Physiol. 50:2061-83
    • (1967) J. Gen. Physiol. , vol.50 , pp. 2061-2083
    • Diamond, J.M.1    Bossert, W.H.2
  • 5
    • 0021884317 scopus 로고
    • Vibrating probe analysis of teleost opercular epithelium: Correlation between active transport and leak pathways of individual chloride cells
    • DOI 10.1007/BF01872003
    • Foskett JK, Machen TE. 1985. Vibrating probe analysis of teleost opercular epithelium: correlation between active transport and leak pathways of individual chloride cells. J. Membr. Biol. 85:25-35 (Pubitemid 15033396)
    • (1985) Journal of Membrane Biology , vol.85 , Issue.1 , pp. 25-35
    • Foskett, J.K.1    Machen, T.E.2
  • 6
    • 0014456576 scopus 로고
    • Freeze-etch appearance of the tight junctions in the epithelium of small and large intestine of mice
    • Staehelin LA, Mukherjee TM, Williams AW. 1969. Freeze-etch appearance of the tight junctions in the epithelium of small and large intestine of mice. Protoplasma 67:165-84
    • (1969) Protoplasma , vol.67 , pp. 165-184
    • Staehelin, L.A.1    Mukherjee, T.M.2    Williams, A.W.3
  • 7
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia
    • Claude P, Goodenough DA. 1973. Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia. J. Cell Biol. 58:390-400
    • (1973) J. Cell Biol. , vol.58 , pp. 390-400
    • Claude, P.1    Goodenough, D.A.2
  • 8
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the Zonula occludens
    • Claude P. 1978. Morphological factors influencing transepithelial permeability: amodel for the resistance of the zonula occludens. J. Membr. Biol. 39:219-32 (Pubitemid 8298689)
    • (1978) Journal of Membrane Biology , vol.39 , Issue.2-3 , pp. 219-232
    • Claude, P.1
  • 9
    • 0021895463 scopus 로고
    • Passive water flows driven across the isolated rabbit ileum by osmotic, hydrostatic and electrical gradients
    • Naftalin RJ, Tripathi S. 1985. Passive water flows driven across the isolated rabbit ileum by osmotic, hydrostatic and electrical gradients. J. Physiol. 360:27-50 (Pubitemid 15133982)
    • (1985) Journal of Physiology , vol.VOL. 360 , pp. 27-50
    • Naftalin, R.J.1    Tripathi, S.2
  • 10
    • 0033774567 scopus 로고    scopus 로고
    • Permeability of the rat small intestinal epithelium along the villuscrypt axis: Effects of glucose transport
    • Fihn BM, Sjoqvist A, Jodal M. 2000. Permeability of the rat small intestinal epithelium along the villuscrypt axis: effects of glucose transport. Gastroenterology 119:1029-36
    • (2000) Gastroenterology , vol.119 , pp. 1029-36
    • Fihn, B.M.1    Sjoqvist, A.2    Jodal, M.3
  • 11
    • 0021251275 scopus 로고
    • Partitioning of paracellular conductance along the ileal crypt-villus axis: A hypothesis based on structural analysis with detailed consideration of tight junction structure-function relationships
    • Marcial MA, Carlson SL, Madara JL. 1984. Partitioning of paracellular conductance along the ileal crypt-villus axis: a hypothesis based on structural analysis with detailed consideration of tight junction structure-function relationships. J. Membr. Biol. 80:59-70 (Pubitemid 14063669)
    • (1984) Journal of Membrane Biology , vol.80 , Issue.1 , pp. 59-70
    • Marcial, M.A.1    Carlson, S.L.2    Madara, J.L.3
  • 13
    • 29244455602 scopus 로고    scopus 로고
    • Interferon-γ selectively increases epithelial permeability to large molecules by activating different populations of paracellular pores
    • DOI 10.1242/jcs.02630
    • Watson CJ, Hoare CJ, Garrod DR, Carlson GL, Warhurst G. 2005. Interferon-gamma selectively increases epithelial permeability to large molecules by activating different populations of paracellular pores. J. Cell Sci. 118:5221-30 (Pubitemid 41819585)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5221-5230
    • Watson, C.J.1    Hoare, C.J.2    Garrod, D.R.3    Carlson, G.L.4    Warhurst, G.5
  • 15
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • Van Itallie CM, Fanning AS, Bridges A, Anderson JM. 2009. ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton. Mol. Biol. Cell 20:3930-40
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3930-40
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 16
    • 77950588683 scopus 로고    scopus 로고
    • Epithelial myosin light chain kinase activation induces mucosal interleukin-13 expression to alter tight junction ion selectivity
    • Weber CR, Raleigh DR, Su L, Shen L, Sullivan EA, et al. 2010. Epithelial myosin light chain kinase activation induces mucosal interleukin-13 expression to alter tight junction ion selectivity. J. Biol. Chem. 285:12037-46
    • (2010) J. Biol. Chem. , vol.285 , pp. 12037-46
    • Weber, C.R.1    Raleigh, D.R.2    Su, L.3    Shen, L.4    Sullivan, E.A.5
  • 17
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (Zonula Occludens) in a variety of epithelia
    • DOI 10.1083/jcb.103.3.755
    • StevensonBR, Siliciano JD, Mooseker MS, Goodenough DA. 1986. Identification ofZO-1: a highmolecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103:755-66 (Pubitemid 17177325)
    • (1986) Journal of Cell Biology , vol.103 , Issue.3 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3
  • 19
    • 8544277305 scopus 로고    scopus 로고
    • JACOP, a novel plaque protein localizing at the apical junctional complex with sequence similarity to cingulin
    • DOI 10.1074/jbc.M402616200
    • Ohnishi H, Nakahara T, Furuse K, Sasaki H, Tsukita S, Furuse M. 2004. JACOP, a novel plaque protein localizing at the apical junctional complex with sequence similarity to cingulin. J. Biol. Chem. 279:46014-22 (Pubitemid 39491595)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 46014-46022
    • Ohnishi, H.1    Nakahara, T.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Furuse, M.6
  • 20
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis LA, Goodenough DA. 1994. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J. Cell Biol. 124:949-61 (Pubitemid 24109397)
    • (1994) Journal of Cell Biology , vol.124 , Issue.6 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 22
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • DOI 10.1074/jbc.M002450200
    • Nusrat A, Chen JA, Foley CS, Liang TW, Tom J, et al. 2000. The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction. J. Biol. Chem. 275:29816-22 (Pubitemid 32043866)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29816-29822
    • Nusrat, A.1    Chen, J.A.2    Foley, C.S.3    Liang, T.W.4    Tom, J.5    Cromwell, M.6    Quan, C.7    Mrsny, R.J.8
  • 23
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • DOI 10.1083/jcb.127.6.1617
    • Furuse M, Itoh M, Hirase T, Nagafuchi A, Yonemura S, Tsukita S. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127:1617-26 (Pubitemid 24380900)
    • (1994) Journal of Cell Biology , vol.127 , Issue.6 I , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagaftichi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 24
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • Van Itallie CM, Anderson JM. 1997. Occludin confers adhesiveness when expressed in fibroblasts. J. Cell Sci. 110:1113-21 (Pubitemid 27232281)
    • (1997) Journal of Cell Science , vol.110 , Issue.9 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 26
    • 0033635344 scopus 로고    scopus 로고
    • Complex phenotype of mice lacking occludin, a component of tight junction strands
    • Saitou M, Furuse M, Sasaki H, Schulzke JD, FrommM, et al. 2000. Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol. Biol. Cell 11:4131-42
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4131-42
    • Saitou, M.1    Furuse, M.2    Sasaki, H.3    Schulzke, J.D.4    Fromm, M.5
  • 28
    • 77955992054 scopus 로고    scopus 로고
    • Occludin is required for cytokine-induced tight junction barrier regulation
    • Van Itallie CM, Fanning AS, Holmes J, Anderson JM. 2010. Occludin is required for cytokine-induced tight junction barrier regulation. J. Cell Sci. 123:2844-52
    • (2010) J. Cell Sci. , vol.123 , pp. 2844-52
    • Van Itallie, C.M.1    Fanning, A.S.2    Holmes, J.3    Anderson, J.M.4
  • 29
    • 77950585581 scopus 로고    scopus 로고
    • Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo
    • Marchiando AM, Shen L, Graham WV, Weber CR, Schwarz BT, et al. 2010. Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo. J. Cell Biol. 189:111-26
    • (2010) J. Cell Biol. , vol.189 , pp. 111-26
    • Marchiando, A.M.1    Shen, L.2    Graham, W.V.3    Weber, C.R.4    Schwarz, B.T.5
  • 30
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • DOI 10.1083/jcb.141.7.1539
    • Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S. 1998. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141:1539-50 (Pubitemid 28309169)
    • (1998) Journal of Cell Biology , vol.141 , Issue.7 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 31
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • DOI 10.1083/jcb.143.2.391
    • Furuse M, Sasaki H, Fujimoto K, Tsukita S. 1998. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143:391-401 (Pubitemid 28487858)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 32
    • 33646792959 scopus 로고    scopus 로고
    • Claudin profiling in the mouse during postnatal intestinal development and along the gastrointestinal tract reveals complex expression patterns
    • Holmes JL, Van Itallie CM, Rasmussen JE, Anderson JM. 2006. Claudin profiling in the mouse during postnatal intestinal development and along the gastrointestinal tract reveals complex expression patterns. Gene Expr. Patterns 6:581-88
    • (2006) Gene Expr. Patterns , vol.6 , pp. 581-88
    • Holmes, J.L.1    Van Itallie, C.M.2    Rasmussen, J.E.3    Anderson, J.M.4
  • 36
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio OR, Van Itallie C, Rahner C, Anderson JM. 2003. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell Physiol. 284:1346-54
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284 , pp. 1346-54
    • Colegio, O.R.1    Van Itallie, C.2    Rahner, C.3    Anderson, J.M.4
  • 37
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anionselective epithelial lines by expression of different claudins
    • Van Itallie CM, Fanning AS, Anderson JM. 2003. Reversal of charge selectivity in cation or anionselective epithelial lines by expression of different claudins. Am. J. Physiol. Ren. Physiol. 285:1078-84
    • (2003) Am. J. Physiol. Ren. Physiol. , vol.285 , pp. 1078-84
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 38
    • 0037930880 scopus 로고    scopus 로고
    • Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation
    • DOI 10.1074/jbc.M213286200
    • Yu AS, Enck AH, Lencer WI, Schneeberger EE. 2003. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J. Biol. Chem. 278:17350-59 (Pubitemid 36799620)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 17350-17359
    • Yu, A.S.L.1    Enck, A.H.2    Lencer, W.I.3    Schneeberger, E.E.4
  • 42
    • 60549090106 scopus 로고    scopus 로고
    • Molecular basis for cation selectivity in claudin-2-based paracellular pores: Identification of an electrostatic interaction site
    • Yu AS, Cheng MH, Angelow S, Gunzel D, Kanzawa SA, et al. 2009. Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site. J. Gen. Physiol. 133:111-27
    • (2009) J. Gen. Physiol. , vol.133 , pp. 111-27
    • Yu, A.S.1    Cheng, M.H.2    Angelow, S.3    Gunzel, D.4    Kanzawa, S.A.5
  • 43
  • 45
    • 0020058236 scopus 로고
    • Evidence for the lipidic nature of tight junction strands
    • DOI 10.1038/296464a0
    • Kachar B, Reese TS. 1982. Evidence for the lipidic nature of tight junction strands. Nature 296:464-66 (Pubitemid 12108535)
    • (1982) Nature , vol.296 , Issue.5856 , pp. 464-466
    • Kachar, B.1    Reese, T.S.2
  • 46
    • 0020079785 scopus 로고
    • On tight-junction structure
    • Pinto da Silva P, Kachar B. 1982. On tight-junction structure. Cell 28:441-50 (Pubitemid 12111918)
    • (1982) Cell , vol.28 , Issue.3 , pp. 441-450
    • Pinto Da Silva, P.1    Kachar, B.2
  • 50
    • 77953021608 scopus 로고    scopus 로고
    • Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules
    • Piehl C, Piontek J, Cording J, Wolburg H, Blasig IE. 2010. Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules. Cell Mol. Life Sci. 7:2131-40
    • (2010) Cell Mol. Life Sci. , vol.7 , pp. 2131-40
    • Piehl, C.1    Piontek, J.2    Cording, J.3    Wolburg, H.4    Blasig, I.E.5
  • 52
    • 38049166110 scopus 로고    scopus 로고
    • Formation of tight junction: Determinants of homophilic interaction between classic claudins
    • Piontek J, Winkler L, Wolburg H, Muller SL, Zuleger N, et al. 2008. Formation of tight junction: determinants of homophilic interaction between classic claudins. FASEB J. 22:146-58
    • (2008) FASEB J. , vol.22 , pp. 146-58
    • Piontek, J.1    Winkler, L.2    Wolburg, H.3    Muller, S.L.4    Zuleger, N.5
  • 54
    • 0033523773 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier
    • DOI 10.1083/jcb.147.1.195
    • Sonoda N, Furuse M, Sasaki H, Yonemura S, Katahira J, et al. 1999. Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands. Evidence for direct involvement of claudins in tight junction barrier. J. Cell Biol. 147:195-204 (Pubitemid 30211807)
    • (1999) Journal of Cell Biology , vol.147 , Issue.1 , pp. 195-204
    • Sonoda, N.1    Furuse, M.2    Sasaki, H.3    Yonemura, S.4    Katahira, J.5    Horiguchi, Y.6    Tsukita, S.7
  • 55
    • 0035013499 scopus 로고    scopus 로고
    • Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability
    • Van Itallie C, Rahner C, Anderson JM. 2001. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J. Clin. Investig. 107:1319-27 (Pubitemid 32494549)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.10 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 56
    • 33845995125 scopus 로고    scopus 로고
    • Changes in expression and distribution of claudin 2, 5 and 8 lead to discontinuous tight junctions and barrier dysfunction in active Crohn's disease
    • DOI 10.1136/gut.2006.094375
    • Zeissig S, Burgel N, Gunzel D, Richter J, Mankertz J, et al. 2007. Changes in expression and distribution of claudin 2, 5 and 8 lead to discontinuous tight junctions and barrier dysfunction in activeCrohn's disease. Gut 56:61-72 (Pubitemid 46044890)
    • (2007) Gut , vol.56 , Issue.1 , pp. 61-72
    • Zeissig, S.1    Burgel, N.2    Gunzel, D.3    Richter, J.4    Mankertz, J.5    Wahnschaffe, U.6    Kroesen, A.J.7    Zeitz, M.8    Fromm, M.9    Schulzke, J.-D.10
  • 58
    • 67650553423 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3
    • Winkler L, Gehring C, Wenzel A, Muller SL, Piehl C, et al. 2009. Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3. J. Biol. Chem. 284:18863-72
    • (2009) J. Biol. Chem. , vol.284 , pp. 18863-72
    • Winkler, L.1    Gehring, C.2    Wenzel, A.3    Muller, S.L.4    Piehl, C.5
  • 59
    • 73449142169 scopus 로고    scopus 로고
    • Identification of a claudin-4 residue important for mediating the host cell binding and action of Clostridium perfringens enterotoxin
    • Robertson SL, Smedley JG 3rd, McClane BA. 2010. Identification of a claudin-4 residue important for mediating the host cell binding and action of Clostridium perfringens enterotoxin. Infect. Immun. 78:505-17
    • (2010) Infect. Immun. , vol.78 , pp. 505-17
    • Robertson, S.L.1    Smedley III, J.G.2    McClane, B.A.3
  • 60
    • 34547921509 scopus 로고    scopus 로고
    • Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2
    • DOI 10.1007/s00232-007-9014-3
    • Angelow S, Schneeberger EE, Yu AS. 2007. Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2. J. Membr. Biol. 215:147-59 (Pubitemid 47282681)
    • (2007) Journal of Membrane Biology , vol.215 , Issue.2-3 , pp. 147-159
    • Angelow, S.1    Schneeberger, E.E.2    Yu, A.S.L.3
  • 61
    • 70350399482 scopus 로고    scopus 로고
    • Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis
    • Angelow S, YuAS. 2009. Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis. J. Biol. Chem. 284:29205-17
    • (2009) J. Biol. Chem. , vol.284 , pp. 29205-17
    • Angelow, S.1    Yu, A.S.2
  • 64
    • 77952756845 scopus 로고    scopus 로고
    • Molecular basis of the core structure of tight junctions
    • Furuse M. 2010. Molecular basis of the core structure of tight junctions. Cold Spring Harb. Perspect. Biol. 2:a002907
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Furuse, M.1
  • 65
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • DOI 10.1083/jcb.200711165
    • Shen L, Weber CR, Turner JR. 2008. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J. Cell Biol. 181:683-95 (Pubitemid 351717514)
    • (2008) Journal of Cell Biology , vol.181 , Issue.4 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3
  • 66
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse M, Sasaki H, Tsukita S. 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
  • 67
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • DOI 10.1083/jcb.147.6.1351
    • Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. 1999. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147:1351-63 (Pubitemid 30012818)
    • (1999) Journal of Cell Biology , vol.147 , Issue.6 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 70
    • 77950663681 scopus 로고    scopus 로고
    • Tight junction-associated MARVEL proteins marvelD3, tricellulin, and occludin have distinct but overlapping functions
    • Raleigh DR, Marchiando AM, Zhang Y, Shen L, Sasaki H, et al. 2010. Tight junction-associated MARVEL proteins marvelD3, tricellulin, and occludin have distinct but overlapping functions. Mol. Biol. Cell 21:1200-13
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1200-1213
    • Raleigh, D.R.1    Marchiando, A.M.2    Zhang, Y.3    Shen, L.4    Sasaki, H.5
  • 71
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • DOI 10.1083/jcb.200510043
    • Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S. 2005. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 171:939-45 (Pubitemid 41815826)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Tsukita, S.6
  • 72
    • 0017045714 scopus 로고
    • Effect of plant cytokinins on microfilaments and tight junction permeability
    • DOI 10.1038/264666a0
    • Bentzel CJ, Hainau B, Edelman A, Anagnostopoulos T, Benedetti EL. 1976. Effect of plant cytokinins on microfilaments and tight junction permeability. Nature 264:666-68 (Pubitemid 8020874)
    • (1976) Nature , vol.264 , Issue.5587 , pp. 666-668
    • Bentzel, C.J.1    Hainau, B.2    Edelman, A.3
  • 73
    • 0019778344 scopus 로고
    • Regulation of epithelial tight junction permeability by cyclic AMP
    • Duffey ME, Hainau B, Ho S, Bentzel CJ. 1981. Regulation of epithelial tight junction permeability by cyclic AMP. Nature 294:451-53 (Pubitemid 12220252)
    • (1981) Nature , vol.294 , Issue.5840 , pp. 451-453
    • Duffey, M.E.1    Hainau, B.2    Ho, S.3    Bentzel, C.J.4
  • 74
    • 0016377478 scopus 로고
    • Intestinal conductance and permselectivity changes with theophylline and choleragen
    • PowellDW.1974. Intestinal conductance and permselectivity changes with theophylline and choleragen. Am. J. Physiol. 227:1436-43
    • (1974) Am. J. Physiol. , vol.227 , pp. 1436-43
    • Powell, D.W.1
  • 75
    • 0020582481 scopus 로고
    • Increases in guinea pig small intestinal transepithelial resistance induced by osmotic loads are accompanied by rapid alterations in absorptive-cell tight-junction structure
    • Madara JL. 1983. Increases in guinea pig small intestinal transepithelial resistance induced by osmotic loads are accompanied by rapid alterations in absorptive-cell tight-junction structure. J. Cell Biol. 97:125-36 (Pubitemid 13076523)
    • (1983) Journal of Cell Biology , vol.97 , Issue.1 , pp. 125-136
    • Madara, J.L.1
  • 76
    • 2142758644 scopus 로고    scopus 로고
    • Rab13 regulates PKA signaling during tight junction assembly
    • DOI 10.1083/jcb.200312118
    • Kohler K, LouvardD, Zahraoui A. 2004. Rab13 regulates PKA signaling during tight junction assembly. J. Cell Biol. 165:175-80 (Pubitemid 38544520)
    • (2004) Journal of Cell Biology , vol.165 , Issue.2 , pp. 175-180
    • Kohler, K.1    Louvard, D.2    Zahraoui, A.3
  • 78
    • 0019258703 scopus 로고
    • Occluding junctions and cytoskeletal components in a cultured transporting epithelium
    • DOI 10.1083/jcb.87.3.746
    • Meza I, Ibarra G, Sabanero M, Martinez-Palomo A, Cereijido M. 1980. Occluding junctions and cytoskeletal components in a cultured transporting epithelium. J. Cell Biol. 87:746-54 (Pubitemid 11161806)
    • (1980) Journal of Cell Biology , vol.87 , Issue.3 I , pp. 746-754
    • Meza, I.1    Ibarra, G.2    Sabanero, M.3
  • 79
    • 0022451875 scopus 로고
    • Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity
    • Madara JL, Barenberg D, Carlson S. 1986. Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity. J. Cell Biol. 102:2125-36 (Pubitemid 16052152)
    • (1986) Journal of Cell Biology , vol.102 , Issue.6 , pp. 2125-2136
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 80
    • 24344457031 scopus 로고    scopus 로고
    • Actin depolymerization disrupts tight junctions via Caveolae-mediated endocytosis
    • DOI 10.1091/mbc.E04-12-1089
    • Shen L, Turner JR. 2005. Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Mol. Biol. Cell 16:3919-36 (Pubitemid 41262867)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 3919-3936
    • Shen, L.1    Turner, J.R.2
  • 81
    • 2542424590 scopus 로고    scopus 로고
    • Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex
    • DOI 10.1091/mbc.E04-02-0163
    • Ivanov AI, McCall IC, ParkosCA, Nusrat A. 2004. Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol. Biol. Cell 15:2639-51 (Pubitemid 38691854)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.6 , pp. 2639-2651
    • Ivanov, A.I.1    McCall, I.C.2    Parkos, C.A.3    Nusrat, A.4
  • 83
    • 77952405774 scopus 로고    scopus 로고
    • Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules
    • Muto S, Hata M, Taniguchi J, Tsuruoka S, Moriwaki K, et al. 2010. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc. Natl. Acad. Sci. USA 107:8011-16
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8011-16
    • Muto, S.1    Hata, M.2    Taniguchi, J.3    Tsuruoka, S.4    Moriwaki, K.5
  • 84
    • 0030669302 scopus 로고    scopus 로고
    • Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation
    • Turner JR, Rill BK, Carlson SL, Carnes D, Kerner R, et al. 1997. Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation. Am. J. Physiol. Cell Physiol. 273:1378-85
    • (1997) Am. J. Physiol. Cell Physiol. , vol.273 , pp. 1378-85
    • Turner, J.R.1    Rill, B.K.2    Carlson, S.L.3    Carnes, D.4    Kerner, R.5
  • 85
    • 0023510866 scopus 로고
    • Structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara JL, Pappenheimer JR. 1987. Structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J. Membr. Biol. 100:149-64 (Pubitemid 18004072)
    • (1987) Journal of Membrane Biology , vol.100 , Issue.2 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 86
    • 0027763397 scopus 로고
    • Luminal nutrients alter tight-junction permeability in the rat jejunum: An in vivo perfusion model
    • Sadowski DC, Meddings JB. 1993. Luminal nutrients alter tight-junction permeability in the rat jejunum: an in vivo perfusion model. Can. J. Physiol. Pharmacol. 71:835-39 (Pubitemid 24053562)
    • (1993) Canadian Journal of Physiology and Pharmacology , vol.71 , Issue.10-11 , pp. 835-839
    • Sadowski, D.C.1    Meddings, J.B.2
  • 87
    • 0029148427 scopus 로고
    • Physiological regulation of intestinal epithelial tight junctions as a consequence of Na+-coupled nutrient transport
    • Turner JR, Madara JL. 1995. Physiological regulation of intestinal epithelial tight junctions as a consequence of Na+-coupled nutrient transport. Gastroenterology 109:1391-96
    • (1995) Gastroenterology , vol.109 , pp. 1391-96
    • Turner, J.R.1    Madara, J.L.2
  • 89
    • 0023521841 scopus 로고
    • Contribution of solvent drug through intercellular junctions to absorption of nutrients by the small intestine of the rat
    • Pappenheimer JR, Reiss KZ. 1987. Contribution of solvent drag through intercellular junctions to absorption of nutrients by the small intestine of the rat. J. Membr. Biol. 100:123-36 (Pubitemid 18004070)
    • (1987) Journal of Membrane Biology , vol.100 , Issue.2 , pp. 123-136
    • Pappenheimer, J.R.1    Reiss, K.Z.2
  • 90
    • 0024525147 scopus 로고
    • Intestinal glucose transport using perfused rat jejunum in vivo: Model analysis and derivation of corrected kinetic constants
    • Meddings JB, Westergaard H. 1989. Intestinal glucose transport using perfused rat jejunum in vivo: model analysis and derivation of corrected kinetic constants. Clin. Sci. 76:403-13 (Pubitemid 19104294)
    • (1989) Clinical Science , vol.76 , Issue.4 , pp. 403-413
    • Meddings, J.B.1    Westergaard, H.2
  • 91
    • 33749428028 scopus 로고    scopus 로고
    • Coordinated epithelial NHE3 inhibition and barrier dysfunction are required for TNF-mediated diarrhea in vivo
    • DOI 10.1172/JCI29218
    • Clayburgh DR, Musch MW, Leitges M, Fu YX, Turner JR. 2006. Coordinated epithelial NHE3 inhibition and barrier dysfunction are required for TNF-mediated diarrhea in vivo. J. Clin. Investig. 116:2682-94 (Pubitemid 44511632)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.10 , pp. 2682-2694
    • Clayburgh, D.R.1    Musch, M.W.2    Leitges, M.3    Fu, Y.-X.4    Turner, J.R.5
  • 92
    • 0035205240 scopus 로고    scopus 로고
    • NHE3-dependent cytoplasmic alkalinization is triggered by Na+-glucose cotransport in intestinal epithelia
    • Turner JR, Black ED. 2001. NHE3-dependent cytoplasmic alkalinization is triggered by Na+-glucose cotransport in intestinal epithelia. Am. J. Physiol. Cell Physiol. 281:1533-41
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281 , pp. 1533-41
    • Turner, J.R.1    Black, E.D.2
  • 95
    • 0025061063 scopus 로고
    • Effects of phlorizin and sodium on glucose-elicited alterations of cell junctions in intestinal epithelia
    • Atisook K, Carlson S, Madara JL. 1990. Effects of phlorizin and sodium on glucose-elicited alterations of cell junctions in intestinal epithelia. Am. J. Physiol. Cell Physiol. 258:77-85
    • (1990) Am. J. Physiol. Cell Physiol. , vol.258 , pp. 77-85
    • Atisook, K.1    Carlson, S.2    Madara, J.L.3
  • 100
    • 0019996563 scopus 로고
    • Intestinal permeability in children with Crohn's disease and coeliac disease
    • Pearson AD, Eastham EJ, Laker MF, Craft AW, Nelson R. 1982. Intestinal permeability in children with Crohn's disease and celiac disease. Br. Med. J. (Clin. Res. Ed.) 285:20-21 (Pubitemid 12080390)
    • (1982) British Medical Journal , vol.285 , Issue.6334 , pp. 20-21
    • Pearson, A.D.J.1    Eastham, E.J.2    Laker, M.F.3
  • 101
    • 0020643629 scopus 로고
    • Abnormal small intestine permeability to sugars in patients with Crohn's disease of the terminal ileum and colon
    • Ukabam SO, Clamp JR, Cooper BT. 1983. Abnormal small intestinal permeability to sugars in patients with Crohn's disease of the terminal ileum and colon. Digestion 27:70-74 (Pubitemid 13041629)
    • (1983) Digestion , vol.27 , Issue.2 , pp. 70-74
    • Ukabam, S.O.1    Clamp, J.R.2    Cooper, B.T.3
  • 102
    • 0022970442 scopus 로고
    • Increased intestinal permeability in patients with Crohn's disease and their relatives: A possible etiologic factor
    • Hollander D, Vadheim CM, Brettholz E, Petersen GM, Delahunty T, Rotter JI. 1986. Increased intestinal permeability in patients with Crohn's disease and their relatives. A possible etiologic factor. Ann. Intern. Med. 105:883-85 (Pubitemid 17201765)
    • (1986) Annals of Internal Medicine , vol.105 , Issue.6 , pp. 883-885
    • Hollander, D.1    Vadheim, C.M.2    Brettholz, E.3
  • 104
    • 0027217379 scopus 로고
    • Intestinal permeability and the prediction of relapse in Crohn's disease
    • DOI 10.1016/0140-6736(93)90882-H
    • Wyatt J, VogelsangH, Hubl W, Waldhoer T, Lochs H. 1993. Intestinal permeability and the prediction of relapse in Crohn's disease. Lancet 341:1437-39 (Pubitemid 23161445)
    • (1993) Lancet , vol.341 , Issue.8858 , pp. 1437-1439
    • Wyatt, J.1    Vogelsang, H.2    Hubl, W.3    Waldhoer, T.4    Lochs, H.5
  • 106
    • 58649090901 scopus 로고    scopus 로고
    • Targeted epithelial tight junction dysfunction causes immune activation and contributes to development of experimental colitis
    • Su L, Shen L, Clayburgh DR, Nalle SC, Sullivan EA, et al. 2009. Targeted epithelial tight junction dysfunction causes immune activation and contributes to development of experimental colitis. Gastroenterology 136:551-63
    • (2009) Gastroenterology , vol.136 , pp. 551-63
    • Su, L.1    Shen, L.2    Clayburgh, D.R.3    Nalle, S.C.4    Sullivan, E.A.5
  • 108
    • 58249085436 scopus 로고    scopus 로고
    • Reducing small intestinal permeability attenuates colitis in the IL10 gene-deficient mouse
    • Arrieta MC, Madsen K, Doyle J, Meddings J. 2009. Reducing small intestinal permeability attenuates colitis in the IL10 gene-deficient mouse. Gut 58:41-48
    • (2009) Gut , vol.58 , pp. 41-48
    • Arrieta, M.C.1    Madsen, K.2    Doyle, J.3    Meddings, J.4
  • 109
    • 33645049332 scopus 로고    scopus 로고
    • The primary defect in experimental ileitis originates from a nonhematopoietic source
    • OlsonTS, Reuter BK, Scott KG, MorrisMA, Wang XM, et al. 2006. The primary defect in experimental ileitis originates from a nonhematopoietic source. J. Exp. Med. 203:541-52
    • (2006) J. Exp. Med. , vol.203 , pp. 541-52
    • Olson, T.S.1    Reuter, B.K.2    Scott, K.G.3    Morris, M.A.4    Wang, X.M.5
  • 110
    • 0033228442 scopus 로고    scopus 로고
    • Interleukin-10 gene-deficient mice develop a primary intestinal permeability defect in response to enteric microflora
    • Madsen KL, Malfair D, Gray D, Doyle JS, Jewell LD, Fedorak RN. 1999. Interleukin-10 gene-deficient mice develop a primary intestinal permeability defect in response to enteric microflora. Inflamm. Bowel Dis. 5:262-70
    • (1999) Inflamm. Bowel Dis. , vol.5 , pp. 262-70
    • Madsen, K.L.1    Malfair, D.2    Gray, D.3    Doyle, J.S.4    Jewell, L.D.5    Fedorak, R.N.6
  • 111
    • 55449095474 scopus 로고    scopus 로고
    • A transient breach in the epithelial barrier leads to regulatory T-cell generation and resistance to experimental colitis
    • Boirivant M, Amendola A, Butera A, Sanchez M, Xu L, et al. 2008. A transient breach in the epithelial barrier leads to regulatory T-cell generation and resistance to experimental colitis. Gastroenterology 135:1612-23
    • (2008) Gastroenterology , vol.135 , pp. 1612-23
    • Boirivant, M.1    Amendola, A.2    Butera, A.3    Sanchez, M.4    Xu, L.5
  • 112
    • 50249086073 scopus 로고    scopus 로고
    • XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease
    • Kaser A, Lee AH, Franke A, Glickman JN, Zeissig S, et al. 2008. XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell 134:743-56
    • (2008) Cell , vol.134 , pp. 743-56
    • Kaser, A.1    Lee, A.H.2    Franke, A.3    Glickman, J.N.4    Zeissig, S.5
  • 113
    • 70350509805 scopus 로고    scopus 로고
    • Intestinal mucosal barrier function in health and disease
    • Turner JR. 2009. Intestinal mucosal barrier function in health and disease. Nat. Rev. Immunol. 9:799-809
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 799-809
    • Turner, J.R.1
  • 114
    • 0036678630 scopus 로고    scopus 로고
    • Anti-tumor necrosis factor treatment restores the gut barrier in Crohn's disease
    • Suenaert P, Bulteel V, Lemmens L, Noman M, Geypens B, et al. 2002. Anti-tumor necrosis factor treatment restores the gut barrier in Crohn's disease. Am. J. Gastroenterol. 97:2000-4
    • (2002) Am. J. Gastroenterol. , vol.97 , pp. 2000-4
    • Suenaert, P.1    Bulteel, V.2    Lemmens, L.3    Noman, M.4    Geypens, B.5
  • 116
    • 0032533897 scopus 로고    scopus 로고
    • Tumor necrosis factor-α production to lipopolysaccharide stimulation by donor cells predicts the severity of experimental acute graft-versus-host disease
    • Cooke KR, Hill GR, Crawford JM, Bungard D, Brinson YS, et al. 1998. Tumor necrosis factor-α production to lipopolysaccharide stimulation by donor cells predicts the severity of experimental acute graft-versus-host disease. J. Clin. Investig. 102:1882-91 (Pubitemid 28533836)
    • (1998) Journal of Clinical Investigation , vol.102 , Issue.10 , pp. 1882-1891
    • Cooke, K.R.1    Hill, G.R.2    Crawford, J.M.3    Bungard, D.4    Brinson, Y.S.5    Delmonte Jr., J.6    Ferrara, J.L.M.7
  • 117
    • 0033011210 scopus 로고    scopus 로고
    • Tumor necrosis factor inhibitor ameliorates murine intestinal graft- versus-host disease
    • BrownGR, Lindberg G, Meddings J, SilvaM, Beutler B, Thiele D. 1999. Tumor necrosis factor inhibitor ameliorates murine intestinal graft-versus-host disease. Gastroenterology 116:593-601 (Pubitemid 29106767)
    • (1999) Gastroenterology , vol.116 , Issue.3 , pp. 593-601
    • Brown, G.R.1    Lindberg, G.2    Meddings, J.3    Silva, M.4    Beutler, B.5    Thiele, D.6
  • 119
    • 0031898947 scopus 로고    scopus 로고
    • Autocrine regulation of epithelial permeability by hypoxia: Role for polarized release of tumor necrosis factor α
    • DOI 10.1016/S0016-5085(98)70579-7
    • Taylor CT, Dzus AL, Colgan SP. 1998. Autocrine regulation of epithelial permeability by hypoxia: role for polarized release of tumor necrosis factor α. Gastroenterology 114:657-68 (Pubitemid 28160400)
    • (1998) Gastroenterology , vol.114 , Issue.4 I , pp. 657-668
    • Taylor, C.T.1    Dzus, A.L.2    Colgan, S.P.3
  • 120
    • 0033818743 scopus 로고    scopus 로고
    • Leaks in the epithelial barrier caused by spontaneous and TNF-α-induced single-cell apoptosis
    • Gitter AH, Bendfeldt K, Schulzke JD, Fromm M. 2000. Leaks in the epithelial barrier caused by spontaneous and TNF-α-induced single-cell apoptosis. FASEB J. 14:1749-53
    • (2000) FASEB J. , vol.14 , pp. 1749-53
    • Gitter, A.H.1    Bendfeldt, K.2    Schulzke, J.D.3    Fromm, M.4
  • 121
    • 0036305854 scopus 로고    scopus 로고
    • A membrane-permeant peptide that inhibits MLC kinase restores barrier function in in vitro models of intestinal disease
    • DOI 10.1053/gast.2002.34235
    • Zolotarevsky Y, Hecht G, Koutsouris A, Gonzalez DE, Quan C, et al. 2002. A membrane-permeant peptide that inhibits MLC kinase restores barrier function in in vitro models of intestinal disease. Gastroenterology 123:163-72 (Pubitemid 34747537)
    • (2002) Gastroenterology , vol.123 , Issue.1 , pp. 163-172
    • Zolotarevsky, Y.1    Hecht, G.2    Koutsouris, A.3    Gonzalez, D.E.4    Quan, C.5    Tom, J.6    Mrsny, R.J.7    Turner, J.R.8
  • 122
    • 13844308129 scopus 로고    scopus 로고
    • Mechanism of TNF-α modulation of Caco-2 intestinal epithelial tight junction barrier: Role of myosin light-chain kinase protein expression
    • Ma TY, Boivin MA, Ye D, Pedram A, Said HM. 2005. Mechanism of TNF-α modulation of Caco-2 intestinal epithelial tight junction barrier: role of myosin light-chain kinase protein expression. Am. J. Physiol. Gastrointest. Liver Physiol. 288:422-30
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.288 , pp. 422-30
    • Ma, T.Y.1    Boivin, M.A.2    Ye, D.3    Pedram, A.4    Said, H.M.5
  • 123
    • 13244298599 scopus 로고    scopus 로고
    • Interferon-γ and tumor necrosis factor-α synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression
    • Wang F, Graham WV, Wang Y, Witkowski ED, Schwarz BT, Turner JR. 2005. Interferon-γand tumor necrosis factor-α synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression. Am. J. Pathol. 166:409-19 (Pubitemid 40189038)
    • (2005) American Journal of Pathology , vol.166 , Issue.2 , pp. 409-419
    • Wang, F.1    Graham, W.V.2    Wang, Y.3    Witkowski, E.D.4    Schwarz, B.T.5    Turner, J.R.6
  • 124
    • 20444481707 scopus 로고    scopus 로고
    • Interferon-γ induces internalization of epithelial tight junction proteins via a macropinocytosis-like process
    • DOI 10.1096/fj.04-3260com
    • Bruewer M, Utech M, Ivanov AI, Hopkins AM, Parkos CA, Nusrat A. 2005. Interferon-γ induces internalization of epithelial tight junction proteins via amacropinocytosis-like process. FASEB J. 19:923-33 (Pubitemid 40827713)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 923-933
    • Bruewer, M.1    Utech, M.2    Ivanov, A.I.3    Hopkins, A.M.4    Parkos, C.A.5    Nusrat, A.6
  • 125
  • 126
    • 34250190636 scopus 로고    scopus 로고
    • LIGHT Signals Directly to Intestinal Epithelia to Cause Barrier Dysfunction via Cytoskeletal and Endocytic Mechanisms
    • DOI 10.1053/j.gastro.2007.02.052, PII S0016508507004118
    • Schwarz BT, Wang F, Shen L, Clayburgh DR, Su L, et al. 2007. LIGHT signals directly to intestinal epithelia to cause barrier dysfunction via cytoskeletal and endocytic mechanisms. Gastroenterology 132:2383-94 (Pubitemid 46900820)
    • (2007) Gastroenterology , vol.132 , Issue.7 , pp. 2383-2394
    • Schwarz, B.T.1    Wang, F.2    Shen, L.3    Clayburgh, D.R.4    Su, L.5    Wang, Y.6    Fu, Y.7    Turner, J.R.8
  • 127
    • 0036850908 scopus 로고    scopus 로고
    • Oxazolone colitis, a Th2 colitis model resembling ulcerative colitis, is mediated by IL-13-producing NK-T cells
    • DOI 10.1016/S1074-7613(02)00453-3
    • Heller F, Fuss IJ, Nieuwenhuis EE, Blumberg RS, Strober W. 2002. Oxazolone colitis, a Th2 colitis model resembling ulcerative colitis, is mediated by IL-13-producing NK-T cells. Immunity 17:629-38 (Pubitemid 35351508)
    • (2002) Immunity , vol.17 , Issue.5 , pp. 629-638
    • Heller, F.1    Fuss, I.J.2    Nieuwenhuis, E.E.3    Blumberg, R.S.4    Strober, W.5
  • 129
    • 33846065117 scopus 로고    scopus 로고
    • Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells
    • DOI 10.1091/mbc.E06-05-0471
    • Capaldo CT, Macara IG. 2007. Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells. Mol. Biol. Cell 18:189-200 (Pubitemid 46066720)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.1 , pp. 189-200
    • Capaldo, C.T.1    Macara, I.G.2
  • 130
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • DOI 10.1016/j.cell.2005.09.020, PII S0092867405009748
    • Yamada S, Pokutta S, Drees F, Weis WI, NelsonWJ. 2005. Deconstructing the cadherin-catenin-actin complex. Cell 123:889-901 (Pubitemid 41721034)
    • (2005) Cell , vol.123 , Issue.5 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 131
    • 0033766722 scopus 로고    scopus 로고
    • Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells
    • McCarthy KM, Francis SA, McCormack JM, Lai J, Rogers RA, et al. 2000. Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells. J. Cell Sci. 113(Pt. 19):3387-98
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 19 , pp. 3387-3398
    • McCarthy, K.M.1    Francis, S.A.2    McCormack, J.M.3    Lai, J.4    Rogers, R.A.5
  • 132
    • 4043156987 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli infection leads to appearance of aberrant tight junctions strands in the lateral membrane of intestinal epithelial cells
    • DOI 10.1111/j.1462-5822.2004.00404.x
    • Muza-Moons MM, Schneeberger EE, Hecht GA. 2004. Enteropathogenic Escherichia coli infection leads to appearance of aberrant tight junctions strands in the lateral membrane of intestinal epithelial cells. Cell Microbiol. 6:783-93 (Pubitemid 39077384)
    • (2004) Cellular Microbiology , vol.6 , Issue.8 , pp. 783-793
    • Muza-Moons, M.M.1    Schneeberger, E.E.2    Hecht, G.A.3
  • 133
    • 77952391850 scopus 로고    scopus 로고
    • MLCK-dependent exchange and actin binding region-dependent anchoring of ZO-1 regulate tight junction barrier function
    • Yu D, Marchiando AM, Weber CR, Raleigh DR, Wang Y, et al. 2010. MLCK-dependent exchange and actin binding region-dependent anchoring of ZO-1 regulate tight junction barrier function. Proc. Natl. Acad. Sci. USA 107:8237-41
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8237-8241
    • Yu, D.1    Marchiando, A.M.2    Weber, C.R.3    Raleigh, D.R.4    Wang, Y.5
  • 134
    • 0036832157 scopus 로고    scopus 로고
    • Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1
    • Fanning AS, Ma TY, Anderson JM. 2002. Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1. FASEB J. 16:1835-37
    • (2002) FASEB J. , vol.16 , pp. 1835-37
    • Fanning, A.S.1    Ma, T.Y.2    Anderson, J.M.3
  • 137
    • 0035897412 scopus 로고    scopus 로고
    • Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells
    • DOI 10.1083/jcb.153.2.263
    • Furuse M, Furuse K, Sasaki H, Tsukita S. 2001. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J. Cell Biol. 153:263-72 (Pubitemid 34280213)
    • (2001) Journal of Cell Biology , vol.153 , Issue.2 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 138
    • 21644461890 scopus 로고    scopus 로고
    • + conductance in LLC-PK1 cells
    • DOI 10.1242/jcs.02406
    • Alexandre MD, Lu Q, Chen YH. 2005. Overexpression of claudin-7 decreases the paracellular Cl conductance and increases the paracellular Na+ conductance in LLC-PK1 cells. J. Cell Sci. 118:2683-93 (Pubitemid 40932893)
    • (2005) Journal of Cell Science , vol.118 , Issue.12 , pp. 2683-2693
    • Alexandre, M.D.1    Lu, Q.2    Chen, Y.-H.3
  • 139
    • 33645843051 scopus 로고    scopus 로고
    • Claudin-8modulates paracellular permeability to acidic and basic ions in MDCK II cells
    • Angelow S, Kim KJ, Yu AS. 2006. Claudin-8modulates paracellular permeability to acidic and basic ions in MDCK II cells. J. Physiol. 571:15-26
    • (2006) J. Physiol. , vol.571 , pp. 15-26
    • Angelow, S.1    Kim, K.J.2    Yu, A.S.3
  • 141
    • 17844408453 scopus 로고    scopus 로고
    • Palmitoylation of claudins is required for efficient tight-junction localization
    • DOI 10.1242/jcs.01735
    • Van Itallie CM, Gambling TM, Carson JL, Anderson JM. 2005. Palmitoylation of claudins is required for efficient tight-junction localization. J. Cell Sci. 118:1427-36 (Pubitemid 40585123)
    • (2005) Journal of Cell Science , vol.118 , Issue.7 , pp. 1427-1436
    • Van Itallie, C.M.1    Gambling, T.M.2    Carson, J.L.3    Anderson, J.M.4
  • 142
    • 52649123158 scopus 로고    scopus 로고
    • Claudin-1 and claudin-2 expression is elevated in inflammatory bowel disease and may contribute to early neoplastic transformation
    • Weber CR, Nalle SC, Tretiakova M, Rubin DT, Turner JR. 2008. Claudin-1 and claudin-2 expression is elevated in inflammatory bowel disease and may contribute to early neoplastic transformation. Lab. Investig. 88:1110-20
    • (2008) Lab. Investig. , vol.88 , pp. 1110-20
    • Weber, C.R.1    Nalle, S.C.2    Tretiakova, M.3    Rubin, D.T.4    Turner, J.R.5
  • 143
    • 2942659788 scopus 로고    scopus 로고
    • The cytoplasmic tails of claudins can influence tight junction barrier properties through effects on protein stability
    • DOI 10.1007/s00232-004-0673-z
    • Van Itallie CM, Colegio OR, Anderson JM. 2004. The cytoplasmic tails of claudins can influence tight junction barrier properties through effects on protein stability. J. Membr. Biol. 199:29-38 (Pubitemid 38766424)
    • (2004) Journal of Membrane Biology , vol.199 , Issue.1 , pp. 29-38
    • Van Itallie, C.M.1    Colegio, O.R.2    Anderson, J.M.3
  • 144
    • 0037304386 scopus 로고    scopus 로고
    • Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4
    • DOI 10.1110/ps.0233903
    • Mitic LL, Unger VM, Anderson JM. 2003. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Sci. 12: 218-27 (Pubitemid 36120334)
    • (2003) Protein Science , vol.12 , Issue.2 , pp. 218-227
    • Mitic, L.L.1    Unger, V.M.2    Anderson, J.M.3
  • 145
    • 79951799165 scopus 로고    scopus 로고
    • Casein kinase 2 (CK2) phosphorylates occludin at Ser408 to increase intra-tight junction diffusion and reduce paracellular barrier function
    • (Abstr.)
    • Raleigh DR, Marchiando AM, Boe D, Wang Y, Shen L, Turner JR. 2010. Casein kinase 2 (CK2) phosphorylates occludin at Ser408 to increase intra-tight junction diffusion and reduce paracellular barrier function. FASEB J. 24:1004.6 (Abstr.)
    • (2010) FASEB J. , vol.24 , pp. 10046
    • Raleigh, D.R.1    Marchiando, A.M.2    Boe, D.3    Wang, Y.4    Shen, L.5    Turner, J.R.6


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