메뉴 건너뛰기




Volumn 1257, Issue 1, 2012, Pages 77-84

Dynamic properties of the tight junction barrier

Author keywords

Claudin; FRAP; Occludin; Tight junction; ZO 1

Indexed keywords

CLAUDIN; CLAUDIN 16; INTERLEUKIN 13; SODIUM GLUCOSE COTRANSPORTER 1; TUMOR NECROSIS FACTOR ALPHA;

EID: 84861979056     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06528.x     Document Type: Article
Times cited : (85)

References (31)
  • 1
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia
    • Claude, P. & D.A. Goodenough. 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
  • 2
    • 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: a model for the resistance of the zonula occludens. J. Membr. Biol. 39: 219-232.
    • (1978) J. Membr. Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 3
    • 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 & S. Tsukita. 1998. 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, S.4
  • 4
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • Amasheh, S., N. Meiri, A.H. Gitter, et al. 2002. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J. Cell. Sci. 115: 4969-4976.
    • (2002) J. Cell. Sci. , vol.115 , pp. 4969-4976
    • Amasheh, S.1    Meiri, N.2    Gitter, A.H.3
  • 5
    • 79956202699 scopus 로고    scopus 로고
    • Occludin S408 phosphorylation regulates tight junction protein interactions and barrier function
    • Raleigh, D.R., D.M. Boe, D. Yu, et al. 2011. Occludin S408 phosphorylation regulates tight junction protein interactions and barrier function. J. Cell. Biol. 193: 565-582.
    • (2011) J. Cell. Biol. , vol.193 , pp. 565-582
    • Raleigh, D.R.1    Boe, D.M.2    Yu, D.3
  • 6
    • 0035013499 scopus 로고    scopus 로고
    • Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability
    • Van Itallie, C., C. Rahner & J.M. Anderson. 2001. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J. Clin. Invest. 107: 1319-1327.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 7
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5
    • Wen, H., D.D. Watry, M.C. Marcondes & H.S. Fox. 2004. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 24: 8408-8417.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8408-8417
    • Wen, H.1    Watry, D.D.2    Marcondes, M.C.3    Fox, H.S.4
  • 9
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio, O.R., C.V. Itallie, C. Rahner & J.M. Anderson. 2003. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell. Physiol. 284: C1346-C1354.
    • (2003) Am. J. Physiol. Cell. Physiol. , vol.284
    • Colegio, O.R.1    Itallie, C.V.2    Rahner, C.3    Anderson, J.M.4
  • 10
    • 0037304386 scopus 로고    scopus 로고
    • Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4
    • Mitic, L.L., V.M. Unger & J.M. Anderson. 2003. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Science: a publication of the Protein Society 12: 218-227.
    • (2003) Protein Science: a publication of the Protein Society , vol.12 , pp. 218-227
    • Mitic, L.L.1    Unger, V.M.2    Anderson, J.M.3
  • 11
    • 70350399482 scopus 로고    scopus 로고
    • Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis
    • Angelow, S. & A.S. Yu. 2009. Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis. J. Biol. Chem. 284: 29205-29217.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29205-29217
    • Angelow, S.1    Yu, A.S.2
  • 12
    • 79952800345 scopus 로고    scopus 로고
    • Claudin-2 forms homodimers and is a component of a high molecular weight protein complex
    • Van Itallie, C.M., L.L. Mitic & J.M. Anderson. 2011. Claudin-2 forms homodimers and is a component of a high molecular weight protein complex. J. Biol. Chem. 286: 3442-3450.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3442-3450
    • Van Itallie, C.M.1    Mitic, L.L.2    Anderson, J.M.3
  • 13
    • 38849149203 scopus 로고    scopus 로고
    • Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex
    • Hou, J., A. Renigunta, M. Konrad, et al. 2008. Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex. J. Clin. Invest. 118: 619-628.
    • (2008) J. Clin. Invest. , vol.118 , pp. 619-628
    • Hou, J.1    Renigunta, A.2    Konrad, M.3
  • 14
    • 70349326768 scopus 로고    scopus 로고
    • Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium
    • Hou, J., A. Renigunta, A.S. Gomes, et al. 2009. Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc. Natl. Acad. Sci. USA 106: 15350-15355.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15350-15355
    • Hou, J.1    Renigunta, A.2    Gomes, A.S.3
  • 15
    • 40549109907 scopus 로고    scopus 로고
    • The density of small tight junction pores varies among cell types and is increased by expression of claudin-2
    • Van Itallie, C.M., J. Holmes, A. Bridges, et al. 2008. The density of small tight junction pores varies among cell types and is increased by expression of claudin-2. J. Cell. Sci. 121: 298-305.
    • (2008) J. Cell. Sci. , vol.121 , pp. 298-305
    • Van Itallie, C.M.1    Holmes, J.2    Bridges, A.3
  • 16
    • 0034891627 scopus 로고    scopus 로고
    • Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers
    • Watson, C.J., M. Rowland & G. Warhurst. 2001. Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers. Am. J. Physiol. Cell. Physiol. 281: C388-C397.
    • (2001) Am. J. Physiol. Cell. Physiol. , vol.281
    • Watson, C.J.1    Rowland, M.2    Warhurst, G.3
  • 17
    • 60549090106 scopus 로고    scopus 로고
    • Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site
    • Yu, A.S., M.H. Cheng, S. Angelow, et al. 2009. Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site. J. Gen. Physiol. 133: 111-127.
    • (2009) J. Gen. Physiol. , vol.133 , pp. 111-127
    • Yu, A.S.1    Cheng, M.H.2    Angelow, S.3
  • 18
    • 19644375846 scopus 로고    scopus 로고
    • Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells
    • Yu, A.S., K.M. McCarthy, S.A. Francis, et al. 2005. Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells. Am. J. Physiol. Cell. Physiol. 288: C1231-C1241.
    • (2005) Am. J. Physiol. Cell. Physiol. , vol.288
    • Yu, A.S.1    McCarthy, K.M.2    Francis, S.A.3
  • 19
    • 69949110857 scopus 로고    scopus 로고
    • Tricellulin forms a barrier to macromolecules in tricellular tight junctions without affecting ion permeability
    • Krug, S.M., S. Amasheh, J.F. Richter, et al. 2009. Tricellulin forms a barrier to macromolecules in tricellular tight junctions without affecting ion permeability. Mol. Biol. Cell. 20: 3713-3724.
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 3713-3724
    • Krug, S.M.1    Amasheh, S.2    Richter, J.F.3
  • 20
    • 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, et al. 1997. Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation. Am. J. Physiol. 273: C1378-C1385.
    • (1997) Am. J. Physiol. , vol.273
    • Turner, J.R.1    Rill, B.K.2    Carlson, S.L.3
  • 21
    • 27744551342 scopus 로고    scopus 로고
    • Inflammatory processes have differential effects on claudins 2, 3, and 4 in colonic epithelial cells
    • Prasad, S., R. Mingrino, K. Kaukinen, et al. 2005. Inflammatory processes have differential effects on claudins 2, 3, and 4 in colonic epithelial cells. Lab. Invest. 85: 1139-1162.
    • (2005) Lab. Invest. , vol.85 , pp. 1139-1162
    • Prasad, S.1    Mingrino, R.2    Kaukinen, K.3
  • 22
    • 23244455992 scopus 로고    scopus 로고
    • Interleukin-13 Is the key effector Th2 cytokine in ulcerative colitis that affects epithelial tight junctions, apoptosis, and cell restitution
    • Heller, F., P. Florian, C. Bojarski, et al. 2005. Interleukin-13 Is the key effector Th2 cytokine in ulcerative colitis that affects epithelial tight junctions, apoptosis, and cell restitution. Gastroenterology 129: 550-564.
    • (2005) Gastroenterology , vol.129 , pp. 550-564
    • Heller, F.1    Florian, P.2    Bojarski, C.3
  • 23
    • 77950588683 scopus 로고    scopus 로고
    • Epithelial myosin light chain kinase activation induces mucosal interleukin-13 expression to alter tight junction ion selectivity
    • Weber, C.R., D.R. Raleigh, L. Su, et al. 2010. Epithelial myosin light chain kinase activation induces mucosal interleukin-13 expression to alter tight junction ion selectivity. J. Biol. Chem. 285: 12037-12046.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12037-12046
    • Weber, C.R.1    Raleigh, D.R.2    Su, L.3
  • 24
    • 13244298599 scopus 로고    scopus 로고
    • Interferongamma and tumor necrosis factor-alpha synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression
    • Wang, F., W.V. Graham, Y. Wang, et al. 2005. Interferongamma and tumor necrosis factor-alpha synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression. Am. J. Pathol. 166: 409-419.
    • (2005) Am. J. Pathol. , vol.166 , pp. 409-419
    • Wang, F.1    Graham, W.V.2    Wang, Y.3
  • 25
    • 77952391850 scopus 로고    scopus 로고
    • MLCK-dependent exchange and actin binding region-dependent anchoring of ZO-1 regulate tight junction barrier function
    • Yu, D., A.M. Marchiando, C.R. Weber, 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: 8237-8241.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8237-8241
    • Yu, D.1    Marchiando, A.M.2    Weber, C.R.3
  • 26
    • 0035897412 scopus 로고    scopus 로고
    • Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 intoMadin-Darby canine kidney I cells
    • Furuse, M., K. Furuse, H. Sasaki & S. Tsukita. 2001. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 intoMadin-Darby canine kidney I cells. J. Cell. Biol. 153: 263-272.
    • (2001) J. Cell. Biol. , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 27
    • 0023190873 scopus 로고
    • Analysis of absorptive cell occluding junction structure-function relationships in a state of enhanced junctional permeability
    • Marcial, M.A. & J.L. Madara. 1987. Analysis of absorptive cell occluding junction structure-function relationships in a state of enhanced junctional permeability. Lab. Invest. 56: 424-434.
    • (1987) Lab. Invest. , vol.56 , pp. 424-434
    • Marcial, M.A.1    Madara, J.L.2
  • 28
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • Van Itallie, C.M., A.S. Fanning, A. Bridges & J.M. Anderson. 2009. ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton. Mol. Biol. Cell. 20: 3930-3940.
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 3930-3940
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 29
    • 34447281675 scopus 로고    scopus 로고
    • Molecular basis of epithelial barrier regulation: from basic mechanisms to clinical application
    • Turner, J.R. 2006. Molecular basis of epithelial barrier regulation: from basic mechanisms to clinical application. Am. J. Pathol. 169: 1901-1909.
    • (2006) Am. J. Pathol. , vol.169 , pp. 1901-1909
    • Turner, J.R.1
  • 31
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • Shen, L., C.R. Weber & J.R. Turner. 2008. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J. Cell. Biol. 181: 683-695.
    • (2008) J. Cell. Biol. , vol.181 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.