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Volumn 68, Issue , 2006, Pages 403-429

Claudins and epithelial paracellular transport

Author keywords

Flux; Occludin; Permselectivity; Tight junction; Transepithelial electrical resistance

Indexed keywords

CLAUDIN; CLAUDIN 11; CLAUDIN 16; CLAUDIN 2; CLOSTRIDIUM PERFRINGENS ENTEROTOXIN; CYTOKINE; ENTEROTOXIN; MEMBRANE PROTEIN; OCCLUDIN; PDZ PROTEIN; PERIPHERAL MYELIN PROTEIN 22; PROTEIN MP20; PROTEIN MUPP1; PROTEIN PMP22; PROTEIN ZO1; PROTEIN ZO2; TRANSCRIPTION FACTOR GATA 4; TRANSCRIPTION FACTOR SNAIL; UNCLASSIFIED DRUG;

EID: 33645963995     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.68.040104.131404     Document Type: Review
Times cited : (977)

References (143)
  • 1
    • 0023715186 scopus 로고
    • The epithelial tight junction: Structure, function and preliminary biochemical characterization
    • Stevenson BR, Anderson JM, Bullivant S. 1988. The epithelial tight junction: Structure, function and preliminary biochemical characterization. Mol. Cell Biochem. 83(2):129-45
    • (1988) Mol. Cell Biochem. , vol.83 , Issue.2 , pp. 129-145
    • Stevenson, B.R.1    Anderson, J.M.2    Bullivant, S.3
  • 2
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the zonula occludens
    • 1a. Claude P. 1978. Morphological factors influencing transepithelial permeability: a model for the resistance of the zonula occludens. J. Membr. Biol. 39:219-32
    • (1978) J. Membr. Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 4
    • 3042856468 scopus 로고    scopus 로고
    • Barriers built on claudins
    • Turksen K, Troy TC. 2004. Barriers built on claudins. J. Cell Sci. 117:2435-47
    • (2004) J. Cell Sci. , vol.117 , pp. 2435-2447
    • Turksen, K.1    Troy, T.C.2
  • 5
    • 0035991935 scopus 로고    scopus 로고
    • Molecular complexity of vertebrate tight junctions
    • D'Atri F, Citi S. 2002. Molecular complexity of vertebrate tight junctions. Mol. Membr. Biol. 19:103-12
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 103-112
    • D'Atri, F.1    Citi, S.2
  • 7
    • 0033825953 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity
    • Cereijido M, Shoshani L, Contreras RG. 2000. Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity. Am. J. Physiol. Gastrointest. Liver Physiol. 279:G477-82
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Cereijido, M.1    Shoshani, L.2    Contreras, R.G.3
  • 8
    • 0019631483 scopus 로고
    • Barrier function of epithelia
    • Powell DW. 1981. Barrier function of epithelia. Am. J. Physiol. 241:G275-88
    • (1981) Am. J. Physiol. , vol.241
    • Powell, D.W.1
  • 9
    • 0002980757 scopus 로고    scopus 로고
    • Tight junction permeability to ions and water
    • ed. M Cereijido, JM Anderson. Boca Raton: CRC
    • Reuss L. 2001. Tight junction permeability to ions and water. In Tight Junctions, ed. M Cereijido, JM Anderson, pp. 61-88. Boca Raton: CRC
    • (2001) Tight Junctions , pp. 61-88
    • Reuss, L.1
  • 10
    • 10444264499 scopus 로고    scopus 로고
    • The molecular physiology of tight junction pores
    • Van Itallie CM, Anderson JM. 2004. The molecular physiology of tight junction pores. Physiology 19:331-38
    • (2004) Physiology , vol.19 , pp. 331-338
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 11
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins
    • Van Itallie CM, Fanning AS, Anderson JM. 2003. Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am. J. Physiol. Renal Physiol. 285:F1078-84
    • (2003) Am. J. Physiol. Renal Physiol. , vol.285
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 12
    • 0033672942 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: Nutrients, cytokines, and immune cells
    • Nusrat A, Turner JR, Madara JL. 2000. Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: nutrients, cytokines, and immune cells. Am. J. Physiol. Gastrointest. Liver Physiol. 279:G851-57
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Nusrat, A.1    Turner, J.R.2    Madara, J.L.3
  • 13
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara JL. 1998. Regulation of the movement of solutes across tight junctions. Annu. Rev. Physiol. 60:143-59
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 14
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high-molecular-weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson BR, Siliciano JD, Mooseker MS, Goodenough DA. 1986. Identification of ZO-1: A high-molecular-weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103:755-66
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 15
    • 0037342777 scopus 로고    scopus 로고
    • Paracellular ion channel at the tight junction
    • Tang VW, Goodenough DA. 2003. Paracellular ion channel at the tight junction. Biophys. J. 84:1660-73
    • (2003) Biophys. J. , vol.84 , pp. 1660-1673
    • Tang, V.W.1    Goodenough, D.A.2
  • 16
    • 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, 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
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 17
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, Tsukita S. 1999. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc. Natl. Acad. Sci. USA 96:511-16
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 20
    • 7644230747 scopus 로고    scopus 로고
    • Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: A tight junction disease
    • Hadj-Rabia S, Baala L, Vabres P, Hamel-Teillac D, Jacquemin E, et al. 2004. Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease. Gastroenterology 127:1386-90
    • (2004) Gastroenterology , vol.127 , pp. 1386-1390
    • Hadj-Rabia, S.1    Baala, L.2    Vabres, P.3    Hamel-Teillac, D.4    Jacquemin, E.5
  • 21
    • 17744380785 scopus 로고    scopus 로고
    • Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29
    • Wilcox ER, Burton QL, Naz S, Riazuddin S, Smith TN, et al. 2001. Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29. Cell 104:165-72
    • (2001) Cell , vol.104 , pp. 165-172
    • Wilcox, E.R.1    Burton, Q.L.2    Naz, S.3    Riazuddin, S.4    Smith, T.N.5
  • 23
    • 22144499164 scopus 로고    scopus 로고
    • Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer
    • Dhawan P, Singh AB, Deane NG, No Y, Shiou SR, et al. 2005. Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer. J. Clin. Invest. 115:1765-76
    • (2005) J. Clin. Invest. , vol.115 , pp. 1765-1776
    • Dhawan, P.1    Singh, A.B.2    Deane, N.G.3    No, Y.4    Shiou, S.R.5
  • 24
    • 0027744129 scopus 로고
    • Occludin-a novel integral membrane-protein localizing at tight junctions
    • Furuse M, Hirase T, Itoh M, Nagafuchi A, Yonemura S, et al. 1993. Occludin-a novel integral membrane-protein localizing at tight junctions. J. Cell Biol. 123:1777-88
    • (1993) J. Cell Biol. , vol.123 , pp. 1777-1788
    • Furuse, M.1    Hirase, T.2    Itoh, M.3    Nagafuchi, A.4    Yonemura, S.5
  • 25
    • 0141644213 scopus 로고    scopus 로고
    • The JAM family of junctional adhesion molecules
    • Bazzoni G. 2003. The JAM family of junctional adhesion molecules. Curr. Opin. Cell Biol. 15:525-30
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 525-530
    • Bazzoni, G.1
  • 27
    • 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, Fromm M, 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. 4131-4142
    • Saitou, M.1    Furuse, M.2    Sasaki, H.3    Schulzke, J.D.4    Fromm, M.5
  • 28
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • 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
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 29
    • 0033598188 scopus 로고    scopus 로고
    • 2+-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions
    • 2+-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions. Curr. Biol. 9:1035-38
    • (1999) Curr. Biol. , vol.9 , pp. 1035-1038
    • Kubota, K.1    Furuse, M.2    Sasaki, H.3    Sonoda, N.4    Fujita, K.5
  • 30
    • 3543049587 scopus 로고    scopus 로고
    • Extensive expansion of the claudin gene family in the teleost fish, Fugu rubripes
    • Loh YH, Christoffels A, Brenner S, Hunziker W, Venkatesh B. 2004. Extensive expansion of the claudin gene family in the teleost fish, Fugu rubripes. Genome Res. 14:1248-57
    • (2004) Genome Res. , vol.14 , pp. 1248-1257
    • Loh, Y.H.1    Christoffels, A.2    Brenner, S.3    Hunziker, W.4    Venkatesh, B.5
  • 32
    • 21844456631 scopus 로고    scopus 로고
    • The zebrafish gene claudinj is essential for normal ear function and important for the formation of the otoliths
    • Hardison AL, Lichten L, Banerjee-Basu S, Becker TS, Burgess SM. 2005. The zebrafish gene claudinj is essential for normal ear function and important for the formation of the otoliths. Mech. Dev. 122:949-58
    • (2005) Mech. Dev. , vol.122 , pp. 949-958
    • Hardison, A.L.1    Lichten, L.2    Banerjee-Basu, S.3    Becker, T.S.4    Burgess, S.M.5
  • 33
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, et al. 2005. High-throughput mapping of a dynamic signaling network in mammalian cells. Science 307:1621-25
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodiles, M.1    Brown, K.R.2    Ozdamar, B.3    Bose, R.4    Liu, Z.5
  • 35
    • 0034617463 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein
    • Fujita K, Katahira J, Horiguchi Y, Sonoda N, Furuse M, Tsukita S. 2000. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett. 476:258-61
    • (2000) FEBS Lett. , vol.476 , pp. 258-261
    • Fujita, K.1    Katahira, J.2    Horiguchi, Y.3    Sonoda, N.4    Furuse, M.5    Tsukita, S.6
  • 36
    • 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
    • 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
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 37
    • 0037304386 scopus 로고    scopus 로고
    • Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4
    • 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
    • (2003) Protein Sci. , vol.12 , pp. 218-227
    • Mitic, L.L.1    Unger, V.M.2    Anderson, J.M.3
  • 38
    • 0029156287 scopus 로고
    • Purification and oligomeric state of the major lens fiber cell membrane proteins
    • Jarvis LJ, Louis CF. 1995. Purification and oligomeric state of the major lens fiber cell membrane proteins. Curr. Eye Res. 14:799-808
    • (1995) Curr. Eye Res. , vol.14 , pp. 799-808
    • Jarvis, L.J.1    Louis, C.F.2
  • 39
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S. 2002. Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J. Biol. Chem. 277:455-61
    • (2002) J. Biol. Chem. , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 40
    • 1542778870 scopus 로고    scopus 로고
    • Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells
    • Jeansonne B, Lu Q, Goodenough DA, Chen YH. 2003. Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells. Cell Mol. Biol. 49:13-21
    • (2003) Cell Mol. Biol. , vol.49 , pp. 13-21
    • Jeansonne, B.1    Lu, Q.2    Goodenough, D.A.3    Chen, Y.H.4
  • 41
    • 0037178864 scopus 로고    scopus 로고
    • The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • Roh MH, Liu CJ, Laurinec S, Margolis B. 2002. The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J. Biol. Chem. 277:27501-9
    • (2002) J. Biol. Chem. , vol.277 , pp. 27501-27509
    • Roh, M.H.1    Liu, C.J.2    Laurinec, S.3    Margolis, B.4
  • 42
    • 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. 113:3387-98
    • (2000) J. Cell Sci. , vol.113 , pp. 3387-3398
    • McCarthy, K.M.1    Francis, S.A.2    McCormack, J.M.3    Lai, J.4    Rogers, R.A.5
  • 43
    • 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
  • 44
    • 3543024486 scopus 로고    scopus 로고
    • The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions
    • Ruffer C, Gerke V. 2004. The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions. Eur. J. Cell Biol. 83:135-44
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 135-144
    • Ruffer, C.1    Gerke, V.2
  • 45
    • 17844408453 scopus 로고    scopus 로고
    • Palmitoylation of claudins is required for efficient tight-junction localization
    • 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
    • (2005) J. Cell Sci. , vol.118 , pp. 1427-1436
    • Van Itallie, C.M.1    Gambling, T.M.2    Carson, J.L.3    Anderson, J.M.4
  • 46
    • 2942659788 scopus 로고    scopus 로고
    • The cytoplasmic tails of claudius can influence tight junction barrier properties through effects on protein stability
    • Van Itallie CM, Colegio OR, Anderson JM. 2004. The cytoplasmic tails of claudius can influence tight junction barrier properties through effects on protein stability. J. Membr. Biol. 199:29-38
    • (2004) J. Membr. Biol. , vol.199 , pp. 29-38
    • Van Itallie, C.M.1    Colegio, O.R.2    Anderson, J.M.3
  • 47
    • 0001636804 scopus 로고    scopus 로고
    • CNS myelin and sertoli cell tight junction strands are absent in Osp/claudin-11 null mice
    • Gow A, Southwood CM, Li JS, Pariali M, Riordan GP, et al. 1999. CNS myelin and sertoli cell tight junction strands are absent in Osp/claudin-11 null mice. Cell 99:649-59
    • (1999) Cell , vol.99 , pp. 649-659
    • Gow, A.1    Southwood, C.M.2    Li, J.S.3    Pariali, M.4    Riordan, G.P.5
  • 48
    • 0345967824 scopus 로고    scopus 로고
    • Involvement of nectin-activated Cdc42 small G protein in organization of adherens and tight junctions in Madin-Darby canine kidney cells
    • Fukuhara A, Shimizu K, Kawakatsu T, Fukuhara T, Takai Y. 2003. Involvement of nectin-activated Cdc42 small G protein in organization of adherens and tight junctions in Madin-Darby canine kidney cells. J. Biol. Chem. 278:51885-93
    • (2003) J. Biol. Chem. , vol.278 , pp. 51885-51893
    • Fukuhara, A.1    Shimizu, K.2    Kawakatsu, T.3    Fukuhara, T.4    Takai, Y.5
  • 49
    • 0034796342 scopus 로고    scopus 로고
    • Claudin-6: A novel tight junction molecule is developmentally regulated in mouse embryonic epithelium
    • Turksen K, Troy TC. 2001. Claudin-6: A novel tight junction molecule is developmentally regulated in mouse embryonic epithelium. Dev. Dyn. 222:292-300
    • (2001) Dev. Dyn. , vol.222 , pp. 292-300
    • Turksen, K.1    Troy, T.C.2
  • 50
    • 0035991412 scopus 로고    scopus 로고
    • The renal segmental distribution of claudins changes with development
    • Reyes JL, Lamas M, Martin D, Namorado MD, Islas S, et al. 2002. The renal segmental distribution of claudins changes with development. Kidney Int. 62:476-87
    • (2002) Kidney Int. , vol.62 , pp. 476-487
    • Reyes, J.L.1    Lamas, M.2    Martin, D.3    Namorado, M.D.4    Islas, S.5
  • 51
    • 0036208599 scopus 로고    scopus 로고
    • Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments
    • Kiuchi-Saishin Y, Gotoh S, Furuse M, Takasuga A, Tano Y, Tsukita S. 2002. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 13:875-86
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 875-886
    • Kiuchi-Saishin, Y.1    Gotoh, S.2    Furuse, M.3    Takasuga, A.4    Tano, Y.5    Tsukita, S.6
  • 52
    • 0141920729 scopus 로고    scopus 로고
    • The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila
    • Behr M, Riedel D, Schuh R. 2003. The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila. Dev. Cell 5:611-20
    • (2003) Dev. Cell , vol.5 , pp. 611-620
    • Behr, M.1    Riedel, D.2    Schuh, R.3
  • 53
    • 0035674837 scopus 로고    scopus 로고
    • Epithelial cell polarity and cell junctions in Drosophila
    • Tepass U, Tanentzapf G, Ward R, Fehon R. 2001. Epithelial cell polarity and cell junctions in Drosophila. Annu. Rev. Genet. 35:747-84
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 747-784
    • Tepass, U.1    Tanentzapf, G.2    Ward, R.3    Fehon, R.4
  • 54
    • 1642458089 scopus 로고    scopus 로고
    • Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control
    • Wu VM, Schulte J, Hirschi A, Tepass U, Beitel GJ. 2004. Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control. J. Cell Biol. 164:313-23
    • (2004) J. Cell Biol. , vol.164 , pp. 313-323
    • Wu, V.M.1    Schulte, J.2    Hirschi, A.3    Tepass, U.4    Beitel, G.J.5
  • 55
    • 0038679606 scopus 로고    scopus 로고
    • Claudins in Caenorhabditis elegans: Their distribution and barrier function in the epithelium
    • Asano A, Asano K, Sasaki H, Furuse M, Tsukita S. 2003. Claudins in Caenorhabditis elegans: their distribution and barrier function in the epithelium. Curr. Biol. 13:1042-46
    • (2003) Curr. Biol. , vol.13 , pp. 1042-1046
    • Asano, A.1    Asano, K.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 56
    • 22144499164 scopus 로고    scopus 로고
    • Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer
    • 54a. Dhawan P, Singh AB, Deane NG, No Y, Shiou SR, et al. 2005. Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer. J. Clin. Invest. 115:1765-76
    • (2005) J. Clin. Invest. , vol.115 , pp. 1765-1776
    • Dhawan, P.1    Singh, A.B.2    Deane, N.G.3    No, Y.4    Shiou, S.R.5
  • 58
    • 0033631414 scopus 로고    scopus 로고
    • The peripheral myelin protein 22 and epithelial membrane protein family
    • Jetten AM, Suter U. 2000. The peripheral myelin protein 22 and epithelial membrane protein family. Prog. Nucleic Acid. Res. Mol. Biol. 64:97-129
    • (2000) Prog. Nucleic Acid. Res. Mol. Biol. , vol.64 , pp. 97-129
    • Jetten, A.M.1    Suter, U.2
  • 60
    • 0031557714 scopus 로고    scopus 로고
    • Identification of a mutation in the MP19 gene, Lim2, in the cataractous mouse mutant To3
    • Steele EC Jr, Kerscher S, Lyon MF, Glenister PH, Favor J, et al. 1997. Identification of a mutation in the MP19 gene, Lim2, in the cataractous mouse mutant To3. Mol. Vis. 3:5
    • (1997) Mol. Vis. , vol.3 , pp. 5
    • Steele Jr., E.C.1    Kerscher, S.2    Lyon, M.F.3    Glenister, P.H.4    Favor, J.5
  • 61
    • 0141757144 scopus 로고    scopus 로고
    • Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier
    • Grey AC, Jacobs MD, Gonen T, Kistler J, Donaldson PJ. 2003. Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier. Exp. Eye Res. 77:567-74
    • (2003) Exp. Eye Res. , vol.77 , pp. 567-574
    • Grey, A.C.1    Jacobs, M.D.2    Gonen, T.3    Kistler, J.4    Donaldson, P.J.5
  • 62
    • 0033739691 scopus 로고    scopus 로고
    • Function of tetraspan proteins in the myelin sheath
    • Bronstein JM. 2000. Function of tetraspan proteins in the myelin sheath. Curr. Opin. Neurobiol. 10:552-57
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 552-557
    • Bronstein, J.M.1
  • 63
    • 0034493505 scopus 로고    scopus 로고
    • Exposure at the cell surface is required for Gas3/PMP22 to regulate both cell death and cell spreading: Implication for the Charcot-Marie-Tooth type 1A and Dejerine-Sottas diseases
    • Brancolini C, Edomi P, Marzinotto S, Schneider C. 2000. Exposure at the cell surface is required for Gas3/PMP22 to regulate both cell death and cell spreading: Implication for the Charcot-Marie-Tooth type 1A and Dejerine-Sottas diseases. Mol. Biol. Cell 11:2901-14
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2901-2914
    • Brancolini, C.1    Edomi, P.2    Marzinotto, S.3    Schneider, C.4
  • 64
    • 2642522146 scopus 로고    scopus 로고
    • The temporospatial expression of peripheral myelin protein 22 at the developing blood-nerve and blood-brain barriers
    • Roux KJ, Amici SA, Notterpek L. 2004. The temporospatial expression of peripheral myelin protein 22 at the developing blood-nerve and blood-brain barriers. J. Comp. Neurol. 474:578-88
    • (2004) J. Comp. Neurol. , vol.474 , pp. 578-588
    • Roux, K.J.1    Amici, S.A.2    Notterpek, L.3
  • 65
    • 14844320521 scopus 로고    scopus 로고
    • Modulation of epithelial morphology, monolayer permeability, and cell migration by growth arrest specific 3/peripheral myelin protein 22
    • Roux KJ, Amici SA, Fletcher BS, Notterpek L. 2005. Modulation of epithelial morphology, monolayer permeability, and cell migration by growth arrest specific 3/peripheral myelin protein 22. Mol. Biol. Cell 16:1142-51
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1142-1151
    • Roux, K.J.1    Amici, S.A.2    Fletcher, B.S.3    Notterpek, L.4
  • 66
    • 0037174931 scopus 로고    scopus 로고
    • The tetraspan protein epithelial membrane protein-2 interacts with beta1 integrins and regulates adhesion
    • Wadehra M, Iyer R, Goodglick L, Braun J. 2002. The tetraspan protein epithelial membrane protein-2 interacts with beta1 integrins and regulates adhesion. J. Biol. Chem. 277:41094-100
    • (2002) J. Biol. Chem. , vol.277 , pp. 41094-41100
    • Wadehra, M.1    Iyer, R.2    Goodglick, L.3    Braun, J.4
  • 67
    • 0037072748 scopus 로고    scopus 로고
    • Epithelial membrane proteins induce membrane blebbing and interact with the P2X(7) receptor C terminus
    • Wilson HL, Wilson SA, Surprenant A, North RA. 2002. Epithelial membrane proteins induce membrane blebbing and interact with the P2X(7) receptor C terminus. J. Biol. Chem. 277:34017-23
    • (2002) J. Biol. Chem. , vol.277 , pp. 34017-34023
    • Wilson, H.L.1    Wilson, S.A.2    Surprenant, A.3    North, R.A.4
  • 69
    • 1542317582 scopus 로고    scopus 로고
    • Dynamic interaction of stargazin-like TARPs with cycling AMPA receptors at synapses
    • Tomita S, Fukata M, Nicoll RA, Bredt DS. 2004. Dynamic interaction of stargazin-like TARPs with cycling AMPA receptors at synapses. Science 303:1508-11
    • (2004) Science , vol.303 , pp. 1508-1511
    • Tomita, S.1    Fukata, M.2    Nicoll, R.A.3    Bredt, D.S.4
  • 70
    • 21244498977 scopus 로고    scopus 로고
    • The alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate receptor trafficking regulator "stargazin" is related to the claudin family of proteins by its ability to mediate cell-cell adhesion
    • Price MG, Davis CF, Deng F, Burgess DL. 2005. The alpha-amino-3-hydroxyl- 5-methyl-4-isoxazolepropionate receptor trafficking regulator "stargazin" is related to the claudin family of proteins by its ability to mediate cell-cell adhesion. J. Biol. Chem. 280:19711-20
    • (2005) J. Biol. Chem. , vol.280 , pp. 19711-19720
    • Price, M.G.1    Davis, C.F.2    Deng, F.3    Burgess, D.L.4
  • 71
    • 0034891627 scopus 로고    scopus 로고
    • Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers
    • Watson CJ, Rowland M, Warhurst G. 2001. Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers. Am. J. Physiol. Cell Physiol. 281:C388-97
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Watson, C.J.1    Rowland, M.2    Warhurst, G.3
  • 72
    • 0018172932 scopus 로고
    • Channels in epithelial cell membranes and junctions
    • Diamond JM. 1978. Channels in epithelial cell membranes and junctions. Fed. Proc. 37:2639-44
    • (1978) Fed. Proc. , vol.37 , pp. 2639-2644
    • Diamond, J.M.1
  • 73
    • 0020084411 scopus 로고
    • Single-file diffusion multi-ion mechanism of permeation in paracellular epithelial channels
    • Salas PJI, Moreno JH. 1982. Single-file diffusion multi-ion mechanism of permeation in paracellular epithelial channels. J. Membr. Biol. 64:103-12
    • (1982) J. Membr. Biol. , vol.64 , pp. 103-112
    • Salas, P.J.I.1    Moreno, J.H.2
  • 74
    • 0036316397 scopus 로고    scopus 로고
    • Endothelial barriers: From hypothetical pores to membrane proteins
    • Firth JA. 2002. Endothelial barriers: from hypothetical pores to membrane proteins. J. Anat. 200:541-48
    • (2002) J. Anat. , vol.200 , pp. 541-548
    • Firth, J.A.1
  • 75
    • 0037648580 scopus 로고    scopus 로고
    • Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice
    • Nitta T, Hata M, Gotoh S, Seo Y, Sasaki H, et al. 2003. Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice. J. Cell Biol. 161:653-60
    • (2003) J. Cell Biol. , vol.161 , pp. 653-660
    • Nitta, T.1    Hata, M.2    Gotoh, S.3    Seo, Y.4    Sasaki, H.5
  • 78
    • 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
    • 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
    • (2001) J. Cell Biol. , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 79
    • 0035129369 scopus 로고    scopus 로고
    • Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut
    • Rahner C, Mitic LL, Anderson JM. 2001. Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. Gastroenterology 120:411-22
    • (2001) Gastroenterology , vol.120 , pp. 411-422
    • Rahner, C.1    Mitic, L.L.2    Anderson, J.M.3
  • 80
    • 0038617335 scopus 로고    scopus 로고
    • Functional analysis of tight junctions
    • Matter K, Balda MS. 2003. Functional analysis of tight junctions. Methods 30:228-34
    • (2003) Methods , vol.30 , pp. 228-234
    • Matter, K.1    Balda, M.S.2
  • 81
    • 0032102036 scopus 로고    scopus 로고
    • Molecular analyses of tight junction physiology: Insights and paradoxes
    • Yap AS, Mullin JM, Stevenson BR. 1998. Molecular analyses of tight junction physiology: insights and paradoxes. J. Membr. Biol. 163:159-67
    • (1998) J. Membr. Biol. , vol.163 , pp. 159-167
    • Yap, A.S.1    Mullin, J.M.2    Stevenson, B.R.3
  • 84
    • 8744310611 scopus 로고    scopus 로고
    • Compartmentalization established by claudin-11-based tight junctions in stria vascularis is required for hearing through generation of endocochlear potential
    • Kitajiri SI, Miyamoto T, Mineharu A, Sonoda N, Furuse K, et al. 2004. Compartmentalization established by claudin-11-based tight junctions in stria vascularis is required for hearing through generation of endocochlear potential. J. Cell Sci. 117:5087-96
    • (2004) J. Cell Sci. , vol.117 , pp. 5087-5096
    • Kitajiri, S.I.1    Miyamoto, T.2    Mineharu, A.3    Sonoda, N.4    Furuse, K.5
  • 85
    • 10744222330 scopus 로고    scopus 로고
    • Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration
    • Ben Yosef T, Belyantseva IA, Saunders TL, Hughes ED, Kawamoto K, et al. 2003. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum. Mol. Genet. 12:2049-61
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2049-2061
    • Ben Yosef, T.1    Belyantseva, I.A.2    Saunders, T.L.3    Hughes, E.D.4    Kawamoto, K.5
  • 86
    • 21044437802 scopus 로고    scopus 로고
    • Tight junctions in Schwann cells of peripheral myelinated axons: A lesson from claudin-19-deficient mice
    • Miyamoto T, Morita K, Takemoto D, Takeuchi K, Kitano Y, et al. 2005. Tight junctions in Schwann cells of peripheral myelinated axons: a lesson from claudin-19-deficient mice. J. Cell Biol. 169:527-38
    • (2005) J. Cell Biol. , vol.169 , pp. 527-538
    • Miyamoto, T.1    Morita, K.2    Takemoto, D.3    Takeuchi, K.4    Kitano, Y.5
  • 87
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice
    • Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, et al. 2002. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J. Cell Biol. 156:1099-111
    • (2002) J. Cell Biol. , vol.156 , pp. 1099-1111
    • Furuse, M.1    Hata, M.2    Furuse, K.3    Yoshida, Y.4    Haratake, A.5
  • 88
    • 0036336486 scopus 로고    scopus 로고
    • Permeability barrier dysfunction in transgenic mice overexpressing claudin 6
    • Turksen K, Troy TC. 2002. Permeability barrier dysfunction in transgenic mice overexpressing claudin 6. Development 129:1775-84
    • (2002) Development , vol.129 , pp. 1775-1784
    • Turksen, K.1    Troy, T.C.2
  • 89
    • 0033554314 scopus 로고    scopus 로고
    • Human nerve pathology caused by different mutational mechanisms of the PMP22 gene
    • Gabreels-Festen A, Wetering RV. 1999. Human nerve pathology caused by different mutational mechanisms of the PMP22 gene. Ann. NY Acad. Sci. 883:336-43
    • (1999) Ann. NY Acad. Sci. , vol.883 , pp. 336-343
    • Gabreels-Festen, A.1    Wetering, R.V.2
  • 90
    • 0037994064 scopus 로고    scopus 로고
    • Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT
    • Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, et al. 2003. Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat. Genet. 34:91-96
    • (2003) Nat. Genet. , vol.34 , pp. 91-96
    • Carlton, V.E.1    Harris, B.Z.2    Puffenberger, E.G.3    Batta, A.K.4    Knisely, A.S.5
  • 91
    • 17544399838 scopus 로고    scopus 로고
    • A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting
    • Muller D, Kausalya PJ, Claverie-Martin F, Meij IC, Eggert P, et al. 2003. A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting. Am. J. Hum. Genet. 73:1293-301
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 1293-1301
    • Muller, D.1    Kausalya, P.J.2    Claverie-Martin, F.3    Meij, I.C.4    Eggert, P.5
  • 92
    • 20344365338 scopus 로고    scopus 로고
    • Different mechanisms preclude mutant CLDN14 proteins from forming tight junctions in vitro
    • Wattenhofer M, Reymond A, Falciola V, Charollais A, Caille D, et al. 2005. Different mechanisms preclude mutant CLDN14 proteins from forming tight junctions in vitro. Hum. Mutat. 25:543-49
    • (2005) Hum. Mutat. , vol.25 , pp. 543-549
    • Wattenhofer, M.1    Reymond, A.2    Falciola, V.3    Charollais, A.4    Caille, D.5
  • 93
    • 0036010110 scopus 로고    scopus 로고
    • A new deletion mutation in bovine Claudin-16 (CL-16) deficiency and diagnosis
    • Hirano T, Hirotsune S, Sasaki S, Kikuchi T, Sugimoto Y. 2002. A new deletion mutation in bovine Claudin-16 (CL-16) deficiency and diagnosis. Animal Genet. 33:118-22
    • (2002) Animal Genet. , vol.33 , pp. 118-122
    • Hirano, T.1    Hirotsune, S.2    Sasaki, S.3    Kikuchi, T.4    Sugimoto, Y.5
  • 94
    • 0028200520 scopus 로고
    • Sodium-glucose co-transport and epithelial permeability
    • Madara JL. 1994. Sodium-glucose co-transport and epithelial permeability. Gastroenterology 107:319-320
    • (1994) Gastroenterology , vol.107 , pp. 319-320
    • Madara, J.L.1
  • 96
    • 0142026252 scopus 로고    scopus 로고
    • Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways
    • Ishizaki T, Chiba H, Kojima T, Fujibe M, Soma T, et al. 2003. Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways. Exp. Cell Res. 290:275-88
    • (2003) Exp. Cell Res. , vol.290 , pp. 275-288
    • Ishizaki, T.1    Chiba, H.2    Kojima, T.3    Fujibe, M.4    Soma, T.5
  • 97
    • 1642543216 scopus 로고    scopus 로고
    • Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions
    • Fujibe M, Chiba H, Kojima T, Soma T, Wada T, et al. 2004. Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions. Exp. Cell Res. 295:36-47
    • (2004) Exp. Cell Res. , vol.295 , pp. 36-47
    • Fujibe, M.1    Chiba, H.2    Kojima, T.3    Soma, T.4    Wada, T.5
  • 98
    • 11144354175 scopus 로고    scopus 로고
    • Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins
    • Yamauchi K, Rai T, Kobayashi K, Sohara E, Suzuki T, et al. 2004. Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins. Proc. Natl. Acad. Sci. USA 101:4690-94
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4690-4694
    • Yamauchi, K.1    Rai, T.2    Kobayashi, K.3    Sohara, E.4    Suzuki, T.5
  • 100
    • 22544434673 scopus 로고    scopus 로고
    • Phosphorylation of claudin-3 at threonine 192 by PKA regulates tight junction barrier function in ovarian cancer cells
    • D'Souza T, Agarwal R, Morin PJ. 2005. Phosphorylation of claudin-3 at threonine 192 by PKA regulates tight junction barrier function in ovarian cancer cells. J. Biol. Chem. 280:26233-40
    • (2005) J. Biol. Chem. , vol.280 , pp. 26233-26240
    • D'Souza, T.1    Agarwal, R.2    Morin, P.J.3
  • 101
    • 1842426940 scopus 로고    scopus 로고
    • A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells
    • Matsuda M, Kubo A, Furuse M, Tsukita S. 2004. A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells. J. Cell Sci. 117:1247-57
    • (2004) J. Cell Sci. , vol.117 , pp. 1247-1257
    • Matsuda, M.1    Kubo, A.2    Furuse, M.3    Tsukita, S.4
  • 102
    • 13844312631 scopus 로고    scopus 로고
    • The epithelium in inflammatory bowel disease: Potential role of endocytosis of junctional proteins in barrier disruption
    • Ivanov AI, Nusrat A, Parkos CA. 2004. The epithelium in inflammatory bowel disease: potential role of endocytosis of junctional proteins in barrier disruption. Novartis. Found. Symp. 263:115-24
    • (2004) Novartis. Found. Symp. , vol.263 , pp. 115-124
    • Ivanov, A.I.1    Nusrat, A.2    Parkos, C.A.3
  • 103
    • 0033816938 scopus 로고    scopus 로고
    • Role of the peripheral myelin protein 22 N-linked glycan in oligomer stability
    • Ryan MC, Notterpek L, Tobler AR, Liu N, Shooter EM. 2000. Role of the peripheral myelin protein 22 N-linked glycan in oligomer stability. J. Neurochem. 75:1465-74
    • (2000) J. Neurochem. , vol.75 , pp. 1465-1474
    • Ryan, M.C.1    Notterpek, L.2    Tobler, A.R.3    Liu, N.4    Shooter, E.M.5
  • 104
    • 0037129361 scopus 로고    scopus 로고
    • Identification of genes associated with head and neck carcinogenesis by cDNA microarray comparison between matched primary normal epithelial and squamous carcinoma cells
    • Al Moustafa AE, Alaoui-Jamali MA, Batist G, Hernandez-Perez M, Serruya C, et al. 2002. Identification of genes associated with head and neck carcinogenesis by cDNA microarray comparison between matched primary normal epithelial and squamous carcinoma cells. Oncogene 21:2634-40
    • (2002) Oncogene , vol.21 , pp. 2634-2640
    • Al Moustafa, A.E.1    Alaoui-Jamali, M.A.2    Batist, G.3    Hernandez-Perez, M.4    Serruya, C.5
  • 106
    • 0038106228 scopus 로고    scopus 로고
    • Regulation of tight junctions during the epithelium-mesenchyme transition: Direct repression of the gene expression of claudins/occludin by Snail
    • Ikenouchi J, Matsuda M, Furuse M, Tsukita S. 2003. Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail. J. Cell Sci. 116:1959-67
    • (2003) J. Cell Sci. , vol.116 , pp. 1959-1967
    • Ikenouchi, J.1    Matsuda, M.2    Furuse, M.3    Tsukita, S.4
  • 107
    • 2342431153 scopus 로고    scopus 로고
    • The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation
    • Ohkubo T, Ozawa M. 2004. The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation. J. Cell Sci. 117:1675-85
    • (2004) J. Cell Sci. , vol.117 , pp. 1675-1685
    • Ohkubo, T.1    Ozawa, M.2
  • 108
    • 25444439289 scopus 로고    scopus 로고
    • Inducible expression of Snail selectively increases paracellular ion permeability and differentially modulates tight junction proteins
    • Carrozzino F, Soulie P, Huber D, Mensi N, Orci L, et al. 2005. Inducible expression of Snail selectively increases paracellular ion permeability and differentially modulates tight junction proteins. Am. J. Physiol. Cell Physiol. 289:1002-14
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289 , pp. 1002-1014
    • Carrozzino, F.1    Soulie, P.2    Huber, D.3    Mensi, N.4    Orci, L.5
  • 109
    • 14744270867 scopus 로고    scopus 로고
    • Differential expression of claudin-2 along the human intestine: Implication of GATA-4 in the maintenance of claudin-2 in differentiating cells
    • Escaffit F, Boudreau F, Beaulieu JF. 2005. Differential expression of claudin-2 along the human intestine: Implication of GATA-4 in the maintenance of claudin-2 in differentiating cells. J. Cell. Physiol. 203:15-26
    • (2005) J. Cell. Physiol. , vol.203 , pp. 15-26
    • Escaffit, F.1    Boudreau, F.2    Beaulieu, J.F.3
  • 110
    • 0034787457 scopus 로고    scopus 로고
    • Claudin-18, a novel downstream target gene for the T/EBP/NKX2.1 homeodomain transcription factor, encodes lung- And stomach-specific isoforms through alternative splicing
    • Niimi T, Nagashima K, Ward JM, Minoo P, Zimonjic DB, et al. 2001. Claudin-18, a novel downstream target gene for the T/EBP/NKX2.1 homeodomain transcription factor, encodes lung- and stomach-specific isoforms through alternative splicing. Mol. Cell Biol. 21:7380-90
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7380-7390
    • Niimi, T.1    Nagashima, K.2    Ward, J.M.3    Minoo, P.4    Zimonjic, D.B.5
  • 111
    • 13544266585 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells
    • Lipschutz JH, Li S, Arisco A, Balkovetz DF. 2005. Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells. J. Biol. Chem. 280:3780-88
    • (2005) J. Biol. Chem. , vol.280 , pp. 3780-3788
    • Lipschutz, J.H.1    Li, S.2    Arisco, A.3    Balkovetz, D.F.4
  • 112
    • 2142813761 scopus 로고    scopus 로고
    • A porous defense: The leaky epithelial barrier in intestinal disease
    • Clayburgh DR, Shen L, Turner JR. 2004. A porous defense: The leaky epithelial barrier in intestinal disease. Lab. Invest. 84:282-91
    • (2004) Lab. Invest. , vol.84 , pp. 282-291
    • Clayburgh, D.R.1    Shen, L.2    Turner, J.R.3
  • 114
    • 0034733782 scopus 로고    scopus 로고
    • Modulation of tight junction structure and function by cytokines
    • Walsh SV, Hopkins AM, Nusrat A. 2000. Modulation of tight junction structure and function by cytokines. Adv. Drug Deliv. Rev. 41:303-13
    • (2000) Adv. Drug Deliv. Rev. , vol.41 , pp. 303-313
    • Walsh, S.V.1    Hopkins, A.M.2    Nusrat, A.3
  • 115
    • 0034128634 scopus 로고    scopus 로고
    • Claudins regulate the intestinal barrier in response to immune mediators
    • Kinugasa T, Sakaguchi T, Gu XB, Reinecker HC. 2000. Claudins regulate the intestinal barrier in response to immune mediators. Gastroenterology 118:1001-11
    • (2000) Gastroenterology , vol.118 , pp. 1001-1011
    • Kinugasa, T.1    Sakaguchi, T.2    Gu, X.B.3    Reinecker, H.C.4
  • 116
    • 0027293439 scopus 로고
    • Is small intestinal permeability really increased in relatives of patients with Crohn's disease?
    • May GR, Sutherland LR, Meddings JB. 1993. Is small intestinal permeability really increased in relatives of patients with Crohn's disease? Gastroenterology 104:1627-32
    • (1993) Gastroenterology , vol.104 , pp. 1627-1632
    • May, G.R.1    Sutherland, L.R.2    Meddings, J.B.3
  • 117
    • 0032958705 scopus 로고    scopus 로고
    • Altered tight junction structure contributes to the impaired epithelial barrier function in ulcerative colitis
    • Schmitz H, Barmeyer C, Fromm M, Runkel N, Foss HD, et al. 1999. Altered tight junction structure contributes to the impaired epithelial barrier function in ulcerative colitis. Gastroenterology 116:301-9
    • (1999) Gastroenterology , vol.116 , pp. 301-309
    • Schmitz, H.1    Barmeyer, C.2    Fromm, M.3    Runkel, N.4    Foss, H.D.5
  • 118
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong V, Gumbiner BM. 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
  • 119
    • 0034508690 scopus 로고    scopus 로고
    • Human zonulin, a potential modulator of intestinal tight junctions
    • Wang W, Uzzau S, Goldblum SE, Fasano A. 2000. Human zonulin, a potential modulator of intestinal tight junctions. J. Cell Sci. 113(Pt. 24):4435-40
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 24 , pp. 4435-4440
    • Wang, W.1    Uzzau, S.2    Goldblum, S.E.3    Fasano, A.4
  • 121
    • 0034868507 scopus 로고    scopus 로고
    • The complex interactions between Clostridium perfringens enterotoxin and epithelial tight junctions
    • McClane BA. 2001. The complex interactions between Clostridium perfringens enterotoxin and epithelial tight junctions. Toxicon 39:1781-91
    • (2001) Toxicon , vol.39 , pp. 1781-1791
    • McClane, B.A.1
  • 122
    • 0034837388 scopus 로고    scopus 로고
    • Claudin-4: A new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin
    • Michl P, Buchholz M, Rolke M, Kunsch S, Lohr M, et al. 2001. Claudin-4: A new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin. Gastroenterology 121:678-84
    • (2001) Gastroenterology , vol.121 , pp. 678-684
    • Michl, P.1    Buchholz, M.2    Rolke, M.3    Kunsch, S.4    Lohr, M.5
  • 123
    • 20144375357 scopus 로고    scopus 로고
    • Treatment of chemotherapy-resistant human ovarian cancer xenografts in C,B-17/SCID mice by intraperitoneal administration of Clostridium perfringens enterotoxin
    • Santin AD, Cane S, Bellone S, Palmieri M, Siegel ER, et al. 2005. Treatment of chemotherapy-resistant human ovarian cancer xenografts in C,B-17/SCID mice by intraperitoneal administration of Clostridium perfringens enterotoxin. Cancer Res. 65:4334-42
    • (2005) Cancer Res. , vol.65 , pp. 4334-4342
    • Santin, A.D.1    Cane, S.2    Bellone, S.3    Palmieri, M.4    Siegel, E.R.5
  • 124
    • 22944461756 scopus 로고    scopus 로고
    • Role of N-terminal amino acids in the absorption-enhancing effects of the C-terminal fragment of Clostridium perfringens enterotoxin
    • Masuyama A, Kondoh M, Seguchi H, Takahashi A, Harada M, et al. 2005. Role of N-terminal amino acids in the absorption-enhancing effects of the C-terminal fragment of Clostridium perfringens enterotoxin. J. Pharmacol. Exp. Ther. 314:789-95
    • (2005) J. Pharmacol. Exp. Ther. , vol.314 , pp. 789-795
    • Masuyama, A.1    Kondoh, M.2    Seguchi, H.3    Takahashi, A.4    Harada, M.5
  • 125
    • 0033376599 scopus 로고    scopus 로고
    • Claudin-1 contributes to the epithelial barrier function in MDCK cells
    • Inai T, Kobayashi J, Shibata Y. 1999. Claudin-1 contributes to the epithelial barrier function in MDCK cells. Eur. J. Cell Biol. 78:849-55
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 849-855
    • Inai, T.1    Kobayashi, J.2    Shibata, Y.3
  • 126
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • Amasheh S, Meiri N, Gitter AH, Schoneberg T, Mankertz J, et al. 2002. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J. Cell Sci. 115:4969-76
    • (2002) J. Cell Sci. , vol.115 , pp. 4969-4976
    • Amasheh, S.1    Meiri, N.2    Gitter, A.H.3    Schoneberg, T.4    Mankertz, J.5
  • 127
    • 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. Invest. 107:1319-27
    • (2001) J. Clin. Invest. , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 128
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: Role of the first extracellular domain of claudin-5
    • Wen HJ, Watry DD, Marcondes MCG, Fox HS. 2004. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell Biol. 24:8408-17
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8408-8417
    • Wen, H.J.1    Watry, D.D.2    Marcondes, M.C.G.3    Fox, H.S.4
  • 130
    • 0037930880 scopus 로고    scopus 로고
    • Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation
    • 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
    • (2003) J. Biol. Chem. , vol.278 , pp. 17350-17359
    • Yu, A.S.1    Enck, A.H.2    Lencer, W.I.3    Schneeberger, E.E.4
  • 131
    • 0034068924 scopus 로고    scopus 로고
    • Null mutation of PCLN-1/claudin-16 results in bovine chronic interstitial nephritis
    • Hirano T, Kobayashi N, Itoh T, Takasuga A, Nakamaru T, et al. 2000. Null mutation of PCLN-1/claudin-16 results in bovine chronic interstitial nephritis. Genome Res. 10:659-63
    • (2000) Genome Res. , vol.10 , pp. 659-663
    • Hirano, T.1    Kobayashi, N.2    Itoh, T.3    Takasuga, A.4    Nakamaru, T.5
  • 132
    • 2342446235 scopus 로고    scopus 로고
    • Membrane-associated HB-EGF modulates HGF-induced cellular responses in MDCK cells
    • Singh AB, Tsukada T, Zent R, Harris RC. 2004. Membrane-associated HB-EGF modulates HGF-induced cellular responses in MDCK cells. J. Cell Sci. 117:1365-79
    • (2004) J. Cell Sci. , vol.117 , pp. 1365-1379
    • Singh, A.B.1    Tsukada, T.2    Zent, R.3    Harris, R.C.4
  • 133
    • 0035242434 scopus 로고    scopus 로고
    • Retinoid X receptor α and retinoic acid receptor γ mediate expression of genes encoding tight-junction proteins and barrier function in F9 cells during visceral endodermal differentiation
    • Kubota H, Chiba H, Takakuwa Y, Osanai M, Tobioka H, et al. 2001. Retinoid X receptor α and retinoic acid receptor γ mediate expression of genes encoding tight-junction proteins and barrier function in F9 cells during visceral endodermal differentiation. Exp. Cell Res. 263:163-72
    • (2001) Exp. Cell Res. , vol.263 , pp. 163-172
    • Kubota, H.1    Chiba, H.2    Takakuwa, Y.3    Osanai, M.4    Tobioka, H.5
  • 134
    • 0037077248 scopus 로고    scopus 로고
    • Cloning of the human claudin-2 5′-flanking region revealed a TATA-less promoter with conserved binding sites in mouse and human for caudal-related homeodomain proteins and hepatocyte nuclear factor-1 α
    • Sakaguchi T, Gu XB, Golden HM, Suh ER, Rhoads DB, Reinecker HC. 2002. Cloning of the human claudin-2 5′-flanking region revealed a TATA-less promoter with conserved binding sites in mouse and human for caudal-related homeodomain proteins and hepatocyte nuclear factor-1 α. J. Biol. Chem. 277:21361-70
    • (2002) J. Biol. Chem. , vol.277 , pp. 21361-21370
    • Sakaguchi, T.1    Gu, X.B.2    Golden, H.M.3    Suh, E.R.4    Rhoads, D.B.5    Reinecker, H.C.6
  • 135
    • 0037621983 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor (HNF)-4α triggers formation of functional tight junctions and establishment of polarized epithelial morphology in F9 embryonal carcinoma cells
    • Chiba H, Gotoh T, Kojima T, Satohisa S, Kikuchi K, et al. 2003. Hepatocyte nuclear factor (HNF)-4α triggers formation of functional tight junctions and establishment of polarized epithelial morphology in F9 embryonal carcinoma cells. Exp. Cell Res. 286:288-97
    • (2003) Exp. Cell Res. , vol.286 , pp. 288-297
    • Chiba, H.1    Gotoh, T.2    Kojima, T.3    Satohisa, S.4    Kikuchi, K.5
  • 136
    • 10044248760 scopus 로고    scopus 로고
    • Sp1 site is crucial for the mouse claudin-19 gene expression in the kidney cells
    • Luk JM, Tong MK, Mok BW, Tam PC, Yeung WS, Lee KF. 2004. Sp1 site is crucial for the mouse claudin-19 gene expression in the kidney cells. FEBS Lett. 578:251-56
    • (2004) FEBS Lett. , vol.578 , pp. 251-256
    • Luk, J.M.1    Tong, M.K.2    Mok, B.W.3    Tam, P.C.4    Yeung, W.S.5    Lee, K.F.6
  • 137
    • 12144249206 scopus 로고    scopus 로고
    • The human paracellin-1 gene (hPCLN-1): Renal epithelial cell-specific expression and regulation
    • Efrati E, Arsentiev-Rozenfeld J, Zelikovic I. 2005. The human paracellin-1 gene (hPCLN-1): renal epithelial cell-specific expression and regulation. Am. J. Physiol. Renal Physiol. 288:F272-83
    • (2005) Am. J. Physiol. Renal Physiol. , vol.288
    • Efrati, E.1    Arsentiev-Rozenfeld, J.2    Zelikovic, I.3
  • 138
    • 24944459847 scopus 로고    scopus 로고
    • Signaling mechanisms of HIV-1 Tat-induced alterations of claudin-5 expression in brain endothelial cells
    • Andras IE, Pu H, Ti an J, Deli MA, Nath A, et al. 2005. Signaling mechanisms of HIV-1 Tat-induced alterations of claudin-5 expression in brain endothelial cells. J. Cereb. Blood Flow Metab. 25:1159-70
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 1159-1170
    • Andras, I.E.1    Pu, H.2    Ti An, J.3    Deli, M.A.4    Nath, A.5
  • 139
    • 4444335486 scopus 로고    scopus 로고
    • IL-1β regulates expression of Cx32, occludin, and claudin-2 of rat hepatocytes via distinct signal transduction pathways
    • Yamamoto T, Kojima T, Murata M, Takano K, Go M, et al. 2004. IL-1β regulates expression of Cx32, occludin, and claudin-2 of rat hepatocytes via distinct signal transduction pathways. Exp. Cell Res. 299:427-41
    • (2004) Exp. Cell Res. , vol.299 , pp. 427-441
    • Yamamoto, T.1    Kojima, T.2    Murata, M.3    Takano, K.4    Go, M.5
  • 140
    • 2942557164 scopus 로고    scopus 로고
    • Modulation of gene expression by hypoxia in human umbilical cord vein endothelial cells: A transcriptomic and proteomic study
    • Scheurer SB, Rybak JN, Rosli C, Neri D, Elia G. 2004. Modulation of gene expression by hypoxia in human umbilical cord vein endothelial cells: A transcriptomic and proteomic study. Proteomics 4:1737-60
    • (2004) Proteomics , vol.4 , pp. 1737-1760
    • Scheurer, S.B.1    Rybak, J.N.2    Rosli, C.3    Neri, D.4    Elia, G.5
  • 141
    • 10744230052 scopus 로고    scopus 로고
    • Modification of the transcriptomic response to renal ischemia/reperfusion injury by lipoxin analog
    • Kieran NE, Doran PP, Connolly SB, Greenan MC, Higgins DF, et al. 2003. Modification of the transcriptomic response to renal ischemia/reperfusion injury by lipoxin analog. Kidney Int. 64:480-92
    • (2003) Kidney Int. , vol.64 , pp. 480-492
    • Kieran, N.E.1    Doran, P.P.2    Connolly, S.B.3    Greenan, M.C.4    Higgins, D.F.5
  • 142
    • 0141957168 scopus 로고    scopus 로고
    • Proinflammatory cytokines cause NO*-dependent and -independent changes in expression and localization of tight junction proteins in intestinal epithelial cells
    • Han X, Fink MP, Delude RL. 2003. Proinflammatory cytokines cause NO*-dependent and -independent changes in expression and localization of tight junction proteins in intestinal epithelial cells. Shock 19:229-37
    • (2003) Shock , vol.19 , pp. 229-237
    • Han, X.1    Fink, M.P.2    Delude, R.L.3
  • 143
    • 0036510402 scopus 로고    scopus 로고
    • Molecular regulation of urothelial renewal and host defenses during infection with uropathogenic Escherichia coli
    • Mysorekar IU, Mulvey MA, Hultgren SJ, Gordon JI. 2002. Molecular regulation of urothelial renewal and host defenses during infection with uropathogenic Escherichia coli. J. Biol. Chem. 277:7412-19
    • (2002) J. Biol. Chem. , vol.277 , pp. 7412-7419
    • Mysorekar, I.U.1    Mulvey, M.A.2    Hultgren, S.J.3    Gordon, J.I.4


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