메뉴 건너뛰기




Volumn 60, Issue , 1998, Pages 121-142

Molecular architecture of tight junctions

Author keywords

Actin; Adherens junction; Occludin; ZO 1; ZO 2

Indexed keywords

ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANYLATE KINASE; MEMBRANE PROTEIN; OCCLUDIN; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; TRANSDUCIN;

EID: 0031944250     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.60.1.121     Document Type: Review
Times cited : (640)

References (19)
  • 1
    • 0001901261 scopus 로고
    • Tight junction permeability to ions and water
    • ed. M Cereijido, Boca Raton: CRC Press
    • Reuss L. 1991. Tight junction permeability to ions and water. In Tight Junctions. ed. M Cereijido, pp. 49-06. Boca Raton: CRC Press
    • (1991) Tight Junctions , pp. 49-106
    • Reuss, L.1
  • 2
    • 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
  • 3
    • 0001964701 scopus 로고
    • Evolution of ideas on the tight junction
    • Boca Raton: CRC Press
    • Cereijido M, ed. 1992. Evolution of ideas on the tight junction. In Tight Junctions, pp. 1-13. Boca Raton: CRC Press
    • (1992) Tight Junctions , pp. 1-13
    • Cereijido, M.1
  • 4
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells
    • van Meer G, Simons K. 1986. The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J. 5:1455-64
    • (1986) EMBO J. , vol.5 , pp. 1455-1464
    • Van Meer, G.1    Simons, K.2
  • 5
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson JM, Van Itallie CM. 1995. Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269:G467-75
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 7
    • 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. 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    Silicano, J.D.2    Mooseker, M.3    Goodenough, D.A.4
  • 8
    • 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. 1993. The tight junction protein ZO-1 is homologous to the Drosophila Discs-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA 90:7834-38
    • (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
  • 9
    • 0000757510 scopus 로고    scopus 로고
    • Protein interactions in the tight junction: The role of MAGUK proteins in regulating tight junction organization and function
    • Fanning AS, Lapierre LA, Brecher AR, Van Itallie CM, Anderson JM. 1996. Protein interactions in the tight junction: the role of MAGUK proteins in regulating tight junction organization and function. Curr. Topics Membr. 43:211-35
    • (1996) Curr. Topics Membr. , vol.43 , pp. 211-235
    • Fanning, A.S.1    Lapierre, L.A.2    Brecher, A.R.3    Van Itallie, C.M.4    Anderson, J.M.5
  • 10
    • 0026345292 scopus 로고
    • Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D. 1991. Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA 88:3460-64
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 11
    • 0029908483 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced region
    • Beatch M, Jesaitis LA, Gallin WJ, Goodenough DA, Stevenson BR. 1996. The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced region. J. Biol. Chem. 271:25723-26
    • (1996) J. Biol. Chem. , vol.271 , pp. 25723-25726
    • Beatch, M.1    Jesaitis, L.A.2    Gallin, W.J.3    Goodenough, D.A.4    Stevenson, B.R.5
  • 12
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M, Palade GE. 1963. Junctional complexes in various epithelia. J. Cell Biol. 17:375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.1    Palade, G.E.2
  • 13
    • 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. 1995. 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. 108:3443-49
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 14
    • 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. 39:219-32
    • (1978) J. Membr. Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 15
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi M. 1990. Cadherins: a molecular family important in selective cell-cell adhesion. Annu. Rev. Biochem. 59:237-52
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 16
    • 0029143488 scopus 로고
    • Epithelial differentiation in the mouse preimplantation embryo: Making adhesive contacts for the first time
    • Collins JE, Fleming TP. 1995. Epithelial differentiation in the mouse preimplantation embryo: making adhesive contacts for the first time. Trends Biochem. Sci. 20:307-12
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 307-312
    • Collins, J.E.1    Fleming, T.P.2
  • 17
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of epithelial junctional complex
    • Gumbiner B, Stevenson BR, Grimaldi A. 1988. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of epithelial junctional complex. J. Cell Biol. 107:1575-87
    • (1988) J. Cell Biol. , vol.107 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.R.2    Grimaldi, A.3
  • 19
    • 0025261141 scopus 로고
    • Activation of protein kinase C triggers premature compaction in the four-cell stage mouse embryo
    • Winkel GK, Ferguson JE, Takeichi M, Nuccitelli R. 1990. Activation of protein kinase C triggers premature compaction in the four-cell stage mouse embryo. Dev. Biol. 138:1-15
    • (1990) Dev. Biol. , vol.138 , pp. 1-15
    • Winkel, G.K.1    Ferguson, J.E.2    Takeichi, M.3    Nuccitelli, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.