메뉴 건너뛰기




Volumn 10, Issue 6, 1999, Pages 1337-1345

Transmembrane proteins in the tight junction barrier

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; MEMBRANE PROTEIN; OCCLUDIN;

EID: 0033061321     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (254)

References (80)
  • 1
    • 0001964701 scopus 로고
    • Evolution of ideas on the tight junction
    • eduted bt Cereijido M, Boca Raton, CRC Press
    • Cereijido M: Evolution of ideas on the tight junction. In: Tight Junctions, eduted bt Cereijido M, Boca Raton, CRC Press, 1992, P 1
    • (1992) Tight Junctions , pp. 1
    • Cereijido, M.1
  • 2
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson JM, Van Itallie CM: Tight junctions and the molecular basis for regulation of paracellular permeability. Am J Physiol 269: G467-G475, 1995
    • (1995) Am J Physiol , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 3
  • 4
    • 0030447993 scopus 로고    scopus 로고
    • Molecular dissection of tight junctions
    • Tsukita S, Furuse M, Itoh M: Molecular dissection of tight junctions. Cell Struct Funct 21: 381-385, 1996
    • (1996) Cell Struct Funct , vol.21 , pp. 381-385
    • Tsukita, S.1    Furuse, M.2    Itoh, M.3
  • 5
    • 0031944250 scopus 로고    scopus 로고
    • Molecular architecture of tight junctions
    • Mitic L, Anderson JM: Molecular architecture of tight junctions. Annu Rev Physiol 60: 121-141, 1998
    • (1998) Annu Rev Physiol , vol.60 , pp. 121-141
    • Mitic, L.1    Anderson, J.M.2
  • 6
    • 85095943964 scopus 로고
    • Barrier function of epithelia
    • Powell DW: Barrier function of epithelia. Am J Physiol 241: G275-G288, 1981
    • (1981) Am J Physiol , vol.241
    • Powell, D.W.1
  • 7
    • 0031944543 scopus 로고    scopus 로고
    • Routes and mechanism of fluid transport by epithelia
    • Spring KR: Routes and mechanism of fluid transport by epithelia. Annu Rev Physiol 60: 105-119, 1998
    • (1998) Annu Rev Physiol , vol.60 , pp. 105-119
    • Spring, K.R.1
  • 8
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker BM, Nigam SK: Molecular structure and assembly of the tight junction. Am J Physiol 274: F1-F9, 1998
    • (1998) Am J Physiol , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 9
    • 0031918158 scopus 로고    scopus 로고
    • Role of tight junctions in establishing and maintaining cell polarity
    • Cerijido M, Valdes J, Shoshani L, Contreras RG: Role of tight junctions in establishing and maintaining cell polarity. Annu Rev Physiol 60: 161-177, 1998
    • (1998) Annu Rev Physiol , vol.60 , pp. 161-177
    • Cerijido, M.1    Valdes, J.2    Shoshani, L.3    Contreras, R.G.4
  • 10
    • 0032102036 scopus 로고    scopus 로고
    • Molecular analyses of tight junction physiology: Insights and paradoxes
    • Yap AS, Mullin JM, Stevenson BR: Molecular analyses of tight junction physiology: Insights and paradoxes. J Membr Biol 163: 159-167, 1998
    • (1998) J Membr Biol , vol.163 , pp. 159-167
    • Yap, A.S.1    Mullin, J.M.2    Stevenson, B.R.3
  • 11
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara JL: Regulation of the movement of solutes across tight junctions. Annu Rev Physiol 60: 143-159, 1998
    • (1998) Annu Rev Physiol , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 12
    • 0025827433 scopus 로고
    • Ischemia-induced loss of epithelial polarity: Potential role of the actin cytoskeleton
    • Molitoris BA: Ischemia-induced loss of epithelial polarity: Potential role of the actin cytoskeleton. Am J Physiol 260: F769-F778, 1991
    • (1991) Am J Physiol , vol.260
    • Molitoris, B.A.1
  • 13
    • 0024439472 scopus 로고
    • Ischemic-induced loss of epithelial polarity: Role of the tight junction
    • Molitoris BA, Falk SA, Dahl R: Ischemic-induced loss of epithelial polarity: Role of the tight junction. J Clin Invest 84: 1334-1339, 1989
    • (1989) J Clin Invest , vol.84 , pp. 1334-1339
    • Molitoris, B.A.1    Falk, S.A.2    Dahl, R.3
  • 14
    • 0026179295 scopus 로고
    • New insights into the cell biology of ischemic acute renal failure
    • Molitoris BA: New insights into the cell biology of ischemic acute renal failure. J Am Soc Nephrol 1: 1263-1270, 1991
    • (1991) J Am Soc Nephrol , vol.1 , pp. 1263-1270
    • Molitoris, B.A.1
  • 15
    • 0025761170 scopus 로고
    • The cell biology of ischemic renal injury
    • Weinberg JM: The cell biology of ischemic renal injury. Kidney Int 39: 476-500, 1991
    • (1991) Kidney Int , vol.39 , pp. 476-500
    • Weinberg, J.M.1
  • 16
    • 0001901261 scopus 로고
    • Tight junction permeability to ions and water
    • edited by Cereijido M, Boca Raton, CRC Press
    • Reuss L: Tight junction permeability to ions and water. In: Tight Junctions, edited by Cereijido M, Boca Raton, CRC Press, 1991, p 49
    • (1991) Tight Junctions , pp. 49
    • Reuss, L.1
  • 17
    • 0023510866 scopus 로고
    • The structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara JL, Pappenheimer JR: The structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J Membr Biol 100: 149-164, 1987
    • (1987) J Membr Biol , vol.100 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 18
    • 0031425656 scopus 로고    scopus 로고
    • Measurement of paracellular epithelial conductivity by conductance scanning
    • Gitter AH, Bertog M, Schulzke J-D, Fromm M: Measurement of paracellular epithelial conductivity by conductance scanning. Pflügers Arch 434: 830-840, 1997
    • (1997) Pflügers Arch , vol.434 , pp. 830-840
    • Gitter, A.H.1    Bertog, M.2    Schulzke, J.-D.3    Fromm, M.4
  • 19
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leady" epithelia
    • Claude P, Goodenough DA: Fracture faces of zonulae occludentes from "tight" and "leady" epithelia. J Cell Biol 58: 390-400, 1973
    • (1973) J Cell Biol , vol.58 , pp. 390-400
    • Claude, P.1    Goodenough, D.A.2
  • 21
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the zonula occludens
    • Claude P: Morphological factors influencing transepithelial permeability: A model for the resistance of the zonula occludens. J Membr Biol 39: 219-232, 1978
    • (1978) J Membr Biol , vol.39 , pp. 219-232
    • Claude, P.1
  • 23
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • Van Itallie CM, Anderson JM: Occludin confers adhesiveness when expressed in fibroblasts. J Cell Sci 110: 1113-1121, 1997
    • (1997) J Cell Sci , vol.110 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 24
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins: Application to the immunogold labeling of intracellular junctional complexes
    • Fujimoto K: Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins: Application to the immunogold labeling of intracellular junctional complexes. J Cell Sci 108: 3443-3449, 1995
    • (1995) J Cell Sci , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 25
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A, Furuse M, Saitou M, Ando-Akatsuka Y, Tsukita S: Possible involvement of phosphorylation of occludin in tight junction formation. J Cell Biol 137: 1393-1401, 1997
    • (1997) J Cell Biol , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 27
    • 0028926288 scopus 로고
    • Basolateral but not apical application of protease results in a rapid rise of transepithelial electrical resistance and formation of aberrant tight junction strands in MDCK cells
    • Lynch RD, Tkachuk-Ross LJ, McCormack JM, McCarthy KM, Rogers RA, Schneeberger EE: Basolateral but not apical application of protease results in a rapid rise of transepithelial electrical resistance and formation of aberrant tight junction strands in MDCK cells. Eur J Cell Biol 66: 257-267, 1995
    • (1995) Eur J Cell Biol , vol.66 , pp. 257-267
    • Lynch, R.D.1    Tkachuk-Ross, L.J.2    McCormack, J.M.3    McCarthy, K.M.4    Rogers, R.A.5    Schneeberger, E.E.6
  • 28
    • 0030748172 scopus 로고    scopus 로고
    • COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos
    • Chen Y, Merzdorf C, Paul DL, Goodenough DA: COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos. J Cell Biol 138: 891-899, 1997
    • (1997) J Cell Biol , vol.138 , pp. 891-899
    • Chen, Y.1    Merzdorf, C.2    Paul, D.L.3    Goodenough, D.A.4
  • 29
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda MS, Whitney JA, Flores C, Gonzalez S, Cereijido M, Matter K: Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 134: 1031-1049, 1996
    • (1996) J Cell Biol , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 31
    • 0031047483 scopus 로고    scopus 로고
    • Synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong V, Gumbiner B: Synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J Cell Biol 136: 399-409, 1997
    • (1997) J Cell Biol , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.2
  • 32
    • 0027339375 scopus 로고
    • Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions
    • Mandel LJ, Bacallao R, Zampighi G: Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions. Nature 361: 552-555, 1993
    • (1993) Nature , vol.361 , pp. 552-555
    • Mandel, L.J.1    Bacallao, R.2    Zampighi, G.3
  • 33
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou M, Fujimoto K, Doi Y, Itoh M, Fujimoto T, Furuse M, Takano H, Noda T, Tsukita S: Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J Cell Biol 141: 397-408, 1998
    • (1998) J Cell Biol , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, S.9
  • 34
    • 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: Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 141: 1539-1550, 1998
    • (1998) J Cell Biol , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 35
    • 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: Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA 96: 511-516, 1999
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 36
    • 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: A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 143: 391-401, 1998
    • (1998) J Cell Biol , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 37
    • 85121065241 scopus 로고
    • Altered expression and localization of the tight junction proteins occludin and ZO-1 after common bile duct ligation
    • Fallon MB, Brecher A, Balda MS, Matter K, Anderson JM: Altered expression and localization of the tight junction proteins occludin and ZO-1 after common bile duct ligation. Am J Physiol 260: C1057-C1062, 1995
    • (1995) Am J Physiol , vol.260
    • Fallon, M.B.1    Brecher, A.2    Balda, M.S.3    Matter, K.4    Anderson, J.M.5
  • 39
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong Y, Saitoh T, Minase T, Sawada N, Enomoto K, Mori M: Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J Cell Biol 120: 477-483, 1993
    • (1993) J Cell Biol , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, T.3    Sawada, N.4    Enomoto, K.5    Mori, M.6
  • 40
    • 0027748945 scopus 로고
    • Hepatocyte tight junctions in health and disease
    • edited by Boyer JL, Philadelphia, Saunders
    • Anderson JM: Hepatocyte tight junctions in health and disease. In: Progress in Liver Diseases, edited by Boyer JL, Philadelphia, Saunders, 1993, p 45
    • (1993) Progress in Liver Diseases , pp. 45
    • Anderson, J.M.1
  • 41
    • 0030846016 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin
    • Katahira J, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N: Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin. J Cell Biol 136: 1239-1247, 1997
    • (1997) J Cell Biol , vol.136 , pp. 1239-1247
    • Katahira, J.1    Inoue, N.2    Horiguchi, Y.3    Matsuda, M.4    Sugimoto, N.5
  • 42
    • 0028226528 scopus 로고
    • Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes
    • McClane BA: Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes. Toxicology 87: 43-67, 1994
    • (1994) Toxicology , vol.87 , pp. 43-67
    • McClane, B.A.1
  • 43
    • 0029833675 scopus 로고    scopus 로고
    • Isolation and characterization of a novel oligo dendrocyte-specific protein
    • Bronstein JM, Popper P, Micevych PD, Fraber DB: Isolation and characterization of a novel oligo dendrocyte-specific protein. Neurology 47: 778, 1996
    • (1996) Neurology , vol.47 , pp. 778
    • Bronstein, J.M.1    Popper, P.2    Micevych, P.D.3    Fraber, D.B.4
  • 46
    • 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, Silicano JD, Mooseker M, Goodenough DA: 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: 755-766, 1986
    • (1986) J Cell Biol , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Silicano, J.D.2    Mooseker, M.3    Goodenough, D.A.4
  • 47
    • 0026345292 scopus 로고
    • Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D: Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc Natl Acad Sci USA 88: 3460-3464, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 48
    • 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: 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: 949-961, 1994
    • (1994) J Cell Biol , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 49
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein superfamily found at the tight junction, interacts with ZO-1 and occludin
    • Haskins J, Gu L, Wittchen ES, Hibbard J, Stevenson BR: ZO-3, a novel member of the MAGUK protein superfamily found at the tight junction, interacts with ZO-1 and occludin. J Cell Biol 141: 199-208, 1998
    • (1998) J Cell Biol , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 51
  • 52
    • 0029862538 scopus 로고    scopus 로고
    • Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis
    • Denker BM, Saha C, Khawaja S, Nigam SK: Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis. J Biol Chem 271: 25750-25753, 1996
    • (1996) J Biol Chem , vol.271 , pp. 25750-25753
    • Denker, B.M.1    Saha, C.2    Khawaja, S.3    Nigam, S.K.4
  • 53
    • 0029883798 scopus 로고    scopus 로고
    • Identification of isoforms of G proteins and PKC that colocalize with tight junctions
    • Dodane V, Kachar B: Identification of isoforms of G proteins and PKC that colocalize with tight junctions. J Membr Biol 149: 199-209, 1996
    • (1996) J Membr Biol , vol.149 , pp. 199-209
    • Dodane, V.1    Kachar, B.2
  • 54
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff KK, Yeaman C, Anandasabapathy N, Hsu S-C, Rodriguez-Boulan E, Scheller RH, Nelson WJ: Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93: 731-740, 1998
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.-C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 55
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita S, Oishi K, Akiyama T, Yamanashi Y, Yamamoto T: Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J Cell Biol 113: 867-879, 1991
    • (1991) J Cell Biol , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5
  • 56
    • 0030590868 scopus 로고    scopus 로고
    • The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain
    • Balda MS, Anderson JM, Matter K: The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain. FEBS Lett 399: 326-332, 1996
    • (1996) FEBS Lett , vol.399 , pp. 326-332
    • Balda, M.S.1    Anderson, J.M.2    Matter, K.3
  • 57
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker BM, Nigam SK: Molecular structure and assembly of the tight junction. Am J Physiol 274: F1-F9, 1998
    • (1998) Am J Physiol , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 58
    • 0028110309 scopus 로고
    • Direct association between occludin and ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M, Itoh M, Hirase T, Nagafuchi F, Yonemura S, Tsukita S: Direct association between occludin and ZO-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol 127: 1617-1626, 1994
    • (1994) J Cell Biol , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, F.4    Yonemura, S.5    Tsukita, S.6
  • 59
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions
    • Willott E, Balda MS, Fanning AS, Jameson B, Van Itallie C, Anderson JM: The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions. Proc Natl Acad Sci USA 90: 7834-7838, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7834-7838
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jameson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 61
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning AS, Jameson B, Jesaitis LA, Anderson JM: The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273: 29745-29753, 1998
    • (1998) J Biol Chem , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 62
    • 24444459854 scopus 로고    scopus 로고
    • Interaction with ZO-1 organizes connexin-occludin chimeras at tight junctions
    • Mitic L, Schneeberger EE, Fanning AS, Anderson JM: Interaction with ZO-1 organizes connexin-occludin chimeras at tight junctions [Abstract]. Mol Biol Cell 8: 205a, 1997
    • (1997) Mol Biol Cell , vol.8
    • Mitic, L.1    Schneeberger, E.E.2    Fanning, A.S.3    Anderson, J.M.4
  • 63
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dehar S, Hannigan GE: Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr Opin Cell Biol 8: 657-669, 1996
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 657-669
    • Dehar, S.1    Hannigan, G.E.2
  • 64
    • 0023176321 scopus 로고
    • Intestinal absorptive cell tight junctions are linked to cytoskeleton
    • Madara JL: Intestinal absorptive cell tight junctions are linked to cytoskeleton. Am J Physiol 253: C171-C175, 1987
    • (1987) Am J Physiol , vol.253
    • Madara, J.L.1
  • 65
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based adhesion through its direct binding to a catenin and actin filaments
    • Itoh M, Nagafuchi A, Moroi S, Tsukita S: Involvement of ZO-1 in cadherin-based adhesion through its direct binding to a catenin and actin filaments. J Cell Biol 138: 181-192, 1997
    • (1997) J Cell Biol , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 66
    • 0031018236 scopus 로고    scopus 로고
    • Dynamics of connexins, E-cadherin, and a-catenin on cell membranes during gap junction formation
    • Fugimoto K, Nagafuchi A, Tsukita S, Kuraoka A, Ohokuma A, Shibata Y: Dynamics of connexins, E-cadherin, and a-catenin on cell membranes during gap junction formation. J Cell Sci 110: 311-322, 1997
    • (1997) J Cell Sci , vol.110 , pp. 311-322
    • Fugimoto, K.1    Nagafuchi, A.2    Tsukita, S.3    Kuraoka, A.4    Ohokuma, A.5    Shibata, Y.6
  • 68
    • 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: 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: 2125-2136, 1986
    • (1986) J Cell Biol , vol.102 , pp. 2125-2136
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 69
    • 0029851720 scopus 로고    scopus 로고
    • Modulation of the junctional integrity by low or high concentrations of cytochalasin B and dihydrocytochalasin B is associated with distinct changes in F-actin and ZO-1
    • Nybom P, Magnusson KE: Modulation of the junctional integrity by low or high concentrations of cytochalasin B and dihydrocytochalasin B is associated with distinct changes in F-actin and ZO-1. Biosci Rep 16: 313-326, 1996
    • (1996) Biosci Rep , vol.16 , pp. 313-326
    • Nybom, P.1    Magnusson, K.E.2
  • 70
    • 0028289263 scopus 로고
    • Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells
    • Stevenson BR, Begg DA: Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells. J Cell Sci 107: 367-375, 1994
    • (1994) J Cell Sci , vol.107 , pp. 367-375
    • Stevenson, B.R.1    Begg, D.A.2
  • 71
    • 0028609124 scopus 로고
    • ATP depletion: A novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton
    • Bacallao R, Garfinkel A, Monke S, Zampighi G, Mandel LJ: ATP depletion: A novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton. J Cell Sci 107: 3301-3313, 1994
    • (1994) J Cell Sci , vol.107 , pp. 3301-3313
    • Bacallao, R.1    Garfinkel, A.2    Monke, S.3    Zampighi, G.4    Mandel, L.J.5
  • 72
    • 0030946064 scopus 로고    scopus 로고
    • Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly
    • Tsukamoto T, Nigam SK: Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly. J Biol Chem 272: 16133-16139, 1997
    • (1997) J Biol Chem , vol.272 , pp. 16133-16139
    • Tsukamoto, T.1    Nigam, S.K.2
  • 75
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA, and Rac1 small GTPases
    • Jou T-S, Schneeberger EE, Nelson WJ. Structural and functional regulation of tight junctions by RhoA, and Rac1 small GTPases. J Cell Biol 142: 101-115, 1998
    • (1998) J Cell Biol , vol.142 , pp. 101-115
    • Jou, T.-S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 76
    • 0020368721 scopus 로고
    • 2+-calmodulin dependent phosphorylation of myosin, and its role in brush border contraction in vitro
    • 2+-calmodulin dependent phosphorylation of myosin, and its role in brush border contraction in vitro. J Cell Biol 95: 943-959, 1982
    • (1982) J Cell Biol , vol.95 , pp. 943-959
    • Keller, T.C.S.1    Mooseker, M.S.2
  • 77
    • 0023520885 scopus 로고
    • Physiological regulation of transepithelial impedance in the intestinal mucosa of rats and hamsters
    • Pappenheimer JR: Physiological regulation of transepithelial impedance in the intestinal mucosa of rats and hamsters. J Membr Biol 100: 136-148, 1987
    • (1987) J Membr Biol , vol.100 , pp. 136-148
    • Pappenheimer, J.R.1
  • 78
    • 0029148427 scopus 로고
    • Physiological regulation of intestinal epithelial tight junctions as a consequence of Na(+)-coupled nutrient transport
    • Turner JR, Madara JL: Physiological regulation of intestinal epithelial tight junctions as a consequence of Na(+)-coupled nutrient transport. Gastroenterology 109: 1391-1396, 1995
    • (1995) Gastroenterology , vol.109 , pp. 1391-1396
    • Turner, J.R.1    Madara, J.L.2
  • 79


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.