메뉴 건너뛰기




Volumn 9, Issue 5, 1997, Pages 674-682

Interendothelial junctions: Structure, signalling and functional roles

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; MEMBRANE PROTEIN;

EID: 0000593022     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80121-4     Document Type: Article
Times cited : (199)

References (93)
  • 2
    • 0027283806 scopus 로고
    • Update on the cellular and molecular basis of capillary permeability
    • Schnitzer JE: Update on the cellular and molecular basis of capillary permeability. Cardiovasc Med 1993, 3:124-130.
    • (1993) Cardiovasc Med , vol.3 , pp. 124-130
    • Schnitzer, J.E.1
  • 3
    • 0030273255 scopus 로고    scopus 로고
    • Cell adhesion, cell junctions and the blood brain barrier
    • Staddon JM, Rubin LL: Cell adhesion, cell junctions and the blood brain barrier. Curr Opin Neurobiol 1996, 6:622-627. Describes endothelial cell junction organization in the blood brain barrier.
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 622-627
    • Staddon, J.M.1    Rubin, L.L.2
  • 4
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi M: Cadherins in cancer: implications for invasion and metastasis. Curr Opin Cell Biol 1993, 5:806-811.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 5
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin functions
    • Aberle H, Schwartz H, Kemler R: Cadherin-catenin complex: protein interactions and their implications for cadherin functions. J Cell Biochem 1996, 61:514-523. A review on the structural biology of cadherins and catenins. The authors discuss the role of cadherin-catenin complexes in promoting cell adhesion and tissue morphogenesis during embryonic development.
    • (1996) J Cell Biochem , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 6
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM: Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 1996, 84:345-357. An extensive review on cell adhesion mechanisms and their role in signal transduction, cell growth and differentiation.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 7
    • 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 1995, 269:G467-G475.
    • (1995) Am J Physiol , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 8
    • 0031025201 scopus 로고    scopus 로고
    • The biology of PECAM-1
    • Newman PJ: The biology of PECAM-1. J Clin Invest 1997, 99:3-8.
    • (1997) J Clin Invest , vol.99 , pp. 3-8
    • Newman, P.J.1
  • 9
    • 0026301518 scopus 로고
    • Endothelial transport macromolecules: Transcytosis and endocytosis
    • Simionescu N, Simionescu M: Endothelial transport macromolecules: transcytosis and endocytosis. Cell Biol Rev 1991, 25:5-80.
    • (1991) Cell Biol Rev , vol.25 , pp. 5-80
    • Simionescu, N.1    Simionescu, M.2
  • 10
    • 0029858026 scopus 로고    scopus 로고
    • Endothelial cell-cell adherens junctions: Implications in the control of vascular permeability and angiogenesis
    • Dejana E: Endothelial cell-cell adherens junctions: implications in the control of vascular permeability and angiogenesis. J Clin Invest 1996, 98:1949-1953. A review which makes an attempt to discuss the specific role of adherens junctions in the endothelium.
    • (1996) J Clin Invest , vol.98 , pp. 1949-1953
    • Dejana, E.1
  • 12
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through β-catenin and specification of cell fate during embryogenesis
    • Miller JR, Moon RT: Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev 1996, 10:2527-2539. An update on recent progress in the study of the role of Armadillo proteins in signal transduction and embryonic development.
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 13
    • 0028069007 scopus 로고
    • Tumor-suppressor gene products in cell contacts: The cadherin-APC-armadillo connection
    • Hulsken J, Behrens J, Birchmeier W: Tumor-suppressor gene products in cell contacts: the cadherin-APC-armadillo connection. Curr Opin Cell Biol 1994, 6:711-716.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 711-716
    • Hulsken, J.1    Behrens, J.2    Birchmeier, W.3
  • 14
    • 0029003699 scopus 로고
    • Cell adhesion and signal transduction: The Armadillo connection
    • Peifer M: Cell adhesion and signal transduction: the Armadillo connection. Trends Cell Biol 1995, 5:224-229.
    • (1995) Trends Cell Biol , vol.5 , pp. 224-229
    • Peifer, M.1
  • 15
    • 0030760544 scopus 로고    scopus 로고
    • Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells
    • in press
    • Lampugnani MG, Corada M, Andriopoulou P, Esser S, Risau W, Dejana E: Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells. J Cell Sci 1997, in press.
    • (1997) J Cell Sci
    • Lampugnani, M.G.1    Corada, M.2    Andriopoulou, P.3    Esser, S.4    Risau, W.5    Dejana, E.6
  • 16
    • 0029102071 scopus 로고
    • The tyrosine kinase substrate p120 cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or α-catenin
    • Daniel JM, Reynolds AB: The tyrosine kinase substrate p120 cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or α-catenin. Mol Cell Biol 1995, 15:4819-4824.
    • (1995) Mol Cell Biol , vol.15 , pp. 4819-4824
    • Daniel, J.M.1    Reynolds, A.B.2
  • 17
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesion of ras-transformed breast epithelia
    • Kinch MS, Clark GJ, Der CJ, Burridge K: Tyrosine phosphorylation regulates the adhesion of ras-transformed breast epithelia. J Cell Biol 1995, 130:461-471.
    • (1995) J Cell Biol , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 18
    • 0029797378 scopus 로고    scopus 로고
    • Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex
    • Kypta RM, Su H, Reichardt LF: Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex J Cell Biol 1996, 134:1519-1529.
    • (1996) J Cell Biol , vol.134 , pp. 1519-1529
    • Kypta, R.M.1    Su, H.2    Reichardt, L.F.3
  • 19
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of a PTP 1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • Balsamo J, Leung TC, Ernst H, Zanin MKB, Hoffman S, Lilien J: Regulated binding of a PTP 1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of β-catenin. J Cell Biol 1996, 134:801-813.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.C.2    Ernst, H.3    Zanin, M.K.B.4    Hoffman, S.5    Lilien, J.6
  • 20
    • 0030012613 scopus 로고    scopus 로고
    • Association of human protein-tyrosine phosphatase K with members of the Armadillo family
    • Fuchs M, Muller T, Lerch MM, Ullrich A: Association of human protein-tyrosine phosphatase K with members of the Armadillo family. J Biol Chem 1996, 271:16712-16719.
    • (1996) J Biol Chem , vol.271 , pp. 16712-16719
    • Fuchs, M.1    Muller, T.2    Lerch, M.M.3    Ullrich, A.4
  • 21
    • 0028170977 scopus 로고
    • Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky H, Aberle H, Kemler R: Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J Cell Biol 1994, 127:1375-1380.
    • (1994) J Cell Biol , vol.127 , pp. 1375-1380
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 23
    • 0030917251 scopus 로고    scopus 로고
    • A versatile transcriptional effector of wingless signalling
    • Nusse R: A versatile transcriptional effector of wingless signalling. Cell 1997, 89:321-323. A short, excellent review summarizing the latest progress in the study of signal transduction via wingless/Wnt and the role of catenin/Armadillo proteins.
    • (1997) Cell , vol.89 , pp. 321-323
    • Nusse, R.1
  • 27
    • 0029776445 scopus 로고    scopus 로고
    • β-catenin associates with the actin-bundling protein fascin in a noncadherin complex
    • Tao YS, Edwards RA, Tubb B, Wang S, Bryan J, Mc Crea PD: β-catenin associates with the actin-bundling protein fascin in a noncadherin complex. J Cell Biol 1996, 134:1271-1281.
    • (1996) J Cell Biol , vol.134 , pp. 1271-1281
    • Tao, Y.S.1    Edwards, R.A.2    Tubb, B.3    Wang, S.4    Bryan, J.5    Mc Crea, P.D.6
  • 28
    • 0030614352 scopus 로고    scopus 로고
    • NH2-terminal deletion of β-catenin results in stable colocalization of mutant β-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion
    • Barth AIM, Pollack AL, Altschuler Y, Mostov KE, Nelson WJ: NH2-terminal deletion of β-catenin results in stable colocalization of mutant β-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion. J Cell Biol 1997, 136:693-706.
    • (1997) J Cell Biol , vol.136 , pp. 693-706
    • Barth, A.I.M.1    Pollack, A.L.2    Altschuler, Y.3    Mostov, K.E.4    Nelson, W.J.5
  • 29
    • 0029768676 scopus 로고    scopus 로고
    • An in vivo structure-function study of Armadillo, the β-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for Wingless signaling
    • Orsulic S, Peifer M: An in vivo structure-function study of Armadillo, the β-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for Wingless signaling. J Cell Biol 1996, 134:1283-1300. This paper reports direct evidence for different roles of Armadillo in the wingless signalling pathway and in cell-cell adhesion.
    • (1996) J Cell Biol , vol.134 , pp. 1283-1300
    • Orsulic, S.1    Peifer, M.2
  • 31
    • 0031000282 scopus 로고    scopus 로고
    • Targeted null-mutation in the VE-cadherin gene impairs the organization of vascular-like structures in embryoid bodies
    • Vittet D, Buchou T, Schweitzer A, Dejana E, Huber P: Targeted null-mutation in the VE-cadherin gene impairs the organization of vascular-like structures in embryoid bodies. Proc Natl Acad Sci USA 1997, 94:6273-6278.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6273-6278
    • Vittet, D.1    Buchou, T.2    Schweitzer, A.3    Dejana, E.4    Huber, P.5
  • 32
    • 0028129695 scopus 로고
    • Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line
    • Watabe M, Nagafuchi A, Tsukita S, Takeichi M: Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line. J Cell Biol 1994, 127:247-256.
    • (1994) J Cell Biol , vol.127 , pp. 247-256
    • Watabe, M.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4
  • 34
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Balda MS, Anderson JM: Two classes of tight junctions are revealed by ZO-1 isoforms. Am J Phys 1993, 264:C918-C924.
    • (1993) Am J Phys , vol.264
    • Balda, M.S.1    Anderson, J.M.2
  • 35
    • 0030454252 scopus 로고    scopus 로고
    • Angiogenesis in the developing brain and in brain tumours
    • Breier G, Risau W: Angiogenesis in the developing brain and in brain tumours. Trends Exp Med 1996, 6:362-376.
    • (1996) Trends Exp Med , vol.6 , pp. 362-376
    • Breier, G.1    Risau, W.2
  • 37
    • 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: A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J Cell Biol 1997, 136:399-409. The functional activity of occludin in terms of control of junctional permeability is demonstrated and mapped to specific regions of the molecule.
    • (1997) J Cell Biol , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 38
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M, Itoh M; Hirase T, Nagafuchi A, Yonemura S, Tsukita Sa, Tsukita Sh: Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol 1994, 127:1617-1626.
    • (1994) J Cell Biol , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, Sa.6    Tsukita, Sh.7
  • 39
    • 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, Siciliano JD, Mooseker MS, 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 1986, 103:755-766.
    • (1986) J Cell Biol , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siciliano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 40
    • 0023918616 scopus 로고
    • Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells
    • Anderson JM, Stevenson BR, Jesaitis LA, Goodenough DA, Mooseker MS: Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. J Cell Biol 1988, 106:1141-1149.
    • (1988) J Cell Biol , vol.106 , pp. 1141-1149
    • Anderson, J.M.1    Stevenson, B.R.2    Jesaitis, L.A.3    Goodenough, D.A.4    Mooseker, M.S.5
  • 41
    • 0025888954 scopus 로고
    • A 220-KD undercoat-constitutive protein: Its specific localization at cadherin-based cell-cell adhesion sites
    • Itoh M, Yonemura S, Nagafuchi A, Tsukita Sa, Tsukita Sh: A 220-KD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites. J Cell Biol 1991, 115:1449-1462.
    • (1991) J Cell Biol , vol.115 , pp. 1449-1462
    • Itoh, M.1    Yonemura, S.2    Nagafuchi, A.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 42
    • 0009529569 scopus 로고    scopus 로고
    • Molecular interactions among the tight junction proteins ZO-1, ZO-2 and occludin
    • Fanning A, Jameson BT, Anderson JM: Molecular interactions among the tight junction proteins ZO-1, ZO-2 and occludin [abstract]. Mol Biol Cell 1996, 7:3530.
    • (1996) Mol Biol Cell , vol.7 , pp. 3530
    • Fanning, A.1    Jameson, B.T.2    Anderson, J.M.3
  • 43
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D: Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc Natl Acad Sci USA 1991, 88:3460-3464.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 44
    • 0029143156 scopus 로고
    • Tight junctions, membrane-associated guanylate kinases and cell signalling
    • Kim SK: Tight junctions, membrane-associated guanylate kinases and cell signalling. Curr Opin Cell Biol 1995, 7:641-649.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 641-649
    • Kim, S.K.1
  • 45
    • 0026603087 scopus 로고
    • Detection of the tight junction-associated protein ZO-1 in astrocytes and other nonepithelial cell types
    • Howarth AG, Hughes MR, Stevenson BR: Detection of the tight junction-associated protein ZO-1 in astrocytes and other nonepithelial cell types. Am J Physiol 1992, 262:C461-C469.
    • (1992) Am J Physiol , vol.262
    • Howarth, A.G.1    Hughes, M.R.2    Stevenson, B.R.3
  • 46
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran AK, Hojo M, Huima T, Rodriguez-Boulan E: Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J Cell Biol 1996, 132:451-463.
    • (1996) J Cell Biol , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 48
    • 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 1993, 120:477-483.
    • (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
  • 52
    • 0025094190 scopus 로고
    • Characterization of the ZO-1 protein in endothelial and other cell lines
    • Li C, Poznansky MJ: Characterization of the ZO-1 protein in endothelial and other cell lines. J Cell Sci 1990, 97:231-237.
    • (1990) J Cell Sci , vol.97 , pp. 231-237
    • Li, C.1    Poznansky, M.J.2
  • 53
    • 0030457242 scopus 로고    scopus 로고
    • Histamine reduces ZO-1 tight-junction protein expresssion in cultured retinal microvascular endothelial cells
    • Gardner TW, Lesher T, Khin S, Vu C, Barber AJ, Brennan WA: Histamine reduces ZO-1 tight-junction protein expresssion in cultured retinal microvascular endothelial cells. Biochem J 1996, 320:717-721.
    • (1996) Biochem J , vol.320 , pp. 717-721
    • Gardner, T.W.1    Lesher, T.2    Khin, S.3    Vu, C.4    Barber, A.J.5    Brennan, W.A.6
  • 54
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon JM, Herrenknecht K, Smales C, Rubin LL: Evidence that tyrosine phosphorylation may increase tight junction permeability. J Cell Sci 1995, 108:609-619.
    • (1995) J Cell Sci , vol.108 , pp. 609-619
    • Staddon, J.M.1    Herrenknecht, K.2    Smales, C.3    Rubin, L.L.4
  • 55
    • 0030027609 scopus 로고    scopus 로고
    • Localization of 7H6 tight junction-associated antigen along the cell border of vascular endothelial cells correlates with paracellular barrier function against ions, large molecules and cancer cells
    • Satoh H, Zhoug Y, Isomura H, Saitoh M, Enomoto K, Sawada M, Mori M: Localization of 7H6 tight junction-associated antigen along the cell border of vascular endothelial cells correlates with paracellular barrier function against ions, large molecules and cancer cells. Exp Cell Res 1996, 222:269-274.
    • (1996) Exp Cell Res , vol.222 , pp. 269-274
    • Satoh, H.1    Zhoug, Y.2    Isomura, H.3    Saitoh, M.4    Enomoto, K.5    Sawada, M.6    Mori, M.7
  • 57
    • 9344271549 scopus 로고    scopus 로고
    • Binding of APC to the human homolog of the drosophila discs large tumor suppressor protein
    • Matsumine A, Ogai A, Senda T, Okumura N, Satoh K, Baeg G-H, Kawahara T, Kobayashi S, Okada M, Tohyoshima K, Akiyama T: Binding of APC to the human homolog of the drosophila discs large tumor suppressor protein. Science 1996, 272:1020-1023. Hdlg, which belongs to the membrane-associated guanylate kinase (MAGUK) family, is reported to be a novel partner for adenomatous polyposis coli (APC) protein. The paper also envisages a potential association of both zonula occludens-1 and zonula occludens-2, members of the MAGUK family and components of tight junctions, with the APC protein through their conserved PDZ/DHR repeats.
    • (1996) Science , vol.272 , pp. 1020-1023
    • Matsumine, A.1    Ogai, A.2    Senda, T.3    Okumura, N.4    Satoh, K.5    Baeg, G.-H.6    Kawahara, T.7    Kobayashi, S.8    Okada, M.9    Tohyoshima, K.10    Akiyama, T.11
  • 58
    • 0029846832 scopus 로고    scopus 로고
    • Two independent domains of hDlg are sufficient for subcellular targeting: The PDZ1-2 conformational unit and an alternatively spliced domain
    • ••], offers a molecular basis to the regulation of cell-cell junctions by the cytoskeletal/cytoplasmic undercoat of the plasma membrane.
    • (1996) J Cell Biol , vol.135 , pp. 1125-1137
    • Lue, R.A.1    Brandin, E.2    Chan, E.P.3    Branton, D.4
  • 59
    • 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 1996, 399:326-332.
    • (1996) FEBS Lett , vol.399 , pp. 326-332
    • Balda, M.S.1    Anderson, J.M.2    Matter, K.3
  • 60
    • 0029819449 scopus 로고    scopus 로고
    • Dig protein is required for junction structure, cell polarity and proliferation control in Drosophila epithelia
    • Woods DF, Hough C, Peel D, Callain G, Bryant PJ: Dig protein is required for junction structure, cell polarity and proliferation control in Drosophila epithelia. J Cell Biol 1996, 134:1469-1482. This paper demonstrates the effect of a junctional molecule on very important cell functions such as cell proliferation and polarity.
    • (1996) J Cell Biol , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callain, G.4    Bryant, P.J.5
  • 61
    • 0028922237 scopus 로고
    • Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells
    • Van Itallie CM, Balda MS, Anderson JM: Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells. J Cell Sci 1995, 108:1735-1742.
    • (1995) J Cell Sci , vol.108 , pp. 1735-1742
    • Van Itallie, C.M.1    Balda, M.S.2    Anderson, J.M.3
  • 62
    • 0029837674 scopus 로고    scopus 로고
    • Desmoplakin expression and organization at human umbilical vein endothelial cell-to-cell junctions
    • Valiron O, Chevrier V, Usson Y, Breviario F, Job D, Dejana E: Desmoplakin expression and organization at human umbilical vein endothelial cell-to-cell junctions. J Cell Sci 1996, 109:2141-2149.
    • (1996) J Cell Sci , vol.109 , pp. 2141-2149
    • Valiron, O.1    Chevrier, V.2    Usson, Y.3    Breviario, F.4    Job, D.5    Dejana, E.6
  • 63
    • 0027491462 scopus 로고
    • Complexus adhaerens, a new group of desmoplakin-containing junctions in endothelial cells: The syndesmos connecting retothelial cells in lymph nodes
    • Schmelz M, Franke WW: Complexus adhaerens, a new group of desmoplakin-containing junctions in endothelial cells: the syndesmos connecting retothelial cells in lymph nodes. Eur J Cell Biol 1993, 61:274-289.
    • (1993) Eur J Cell Biol , vol.61 , pp. 274-289
    • Schmelz, M.1    Franke, W.W.2
  • 64
    • 0026740788 scopus 로고
    • Extrajunctional distribution of N-cadherin in cultured human endothelial cells
    • Salomon D, Ayalon O, Patel-King L, Hynes RO, Geiger B: Extrajunctional distribution of N-cadherin in cultured human endothelial cells. J Cell Sci 1992, 102:1-11.
    • (1992) J Cell Sci , vol.102 , pp. 1-11
    • Salomon, D.1    Ayalon, O.2    Patel-King, L.3    Hynes, R.O.4    Geiger, B.5
  • 66
    • 0029858914 scopus 로고    scopus 로고
    • Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1
    • Lu TY, Van LG, Madri JA: Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1. Proc Natl Acad Sci USA 1996, 93:11808-11813.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11808-11813
    • Lu, T.Y.1    Van, L.G.2    Madri, J.A.3
  • 67
    • 0030910268 scopus 로고    scopus 로고
    • Interaction of the adaptor protein She and the adhesive molecule cadherin
    • Xu Y, Guo D, Davidson M, Inagami T, Carpenter G: Interaction of the adaptor protein She and the adhesive molecule cadherin. J Biol Chem 1997, 272:13463-13466.
    • (1997) J Biol Chem , vol.272 , pp. 13463-13466
    • Xu, Y.1    Guo, D.2    Davidson, M.3    Inagami, T.4    Carpenter, G.5
  • 68
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A, Furuse M, Ando-Akatsuka Y, Tsukita S: Possible involvement of phosphorylation of occludin in tight junction formation. J Cell Biol 1997, 137:1393-1401.
    • (1997) J Cell Biol , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Ando-Akatsuka, Y.3    Tsukita, S.4
  • 69
    • 0030585353 scopus 로고    scopus 로고
    • Insulin-like growth factor 1 binding protein 3 synthesis by aortic endothelial cells is a function of cell density
    • Delafontaine P, Ku L, Anwar A, Hayzer D: Insulin-like growth factor 1 binding protein 3 synthesis by aortic endothelial cells is a function of cell density. Biochem Biophys Res Commun 1996, 222:478-482.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 478-482
    • Delafontaine, P.1    Ku, L.2    Anwar, A.3    Hayzer, D.4
  • 70
    • 0021145287 scopus 로고
    • Release of endothelial cell-derived growth factor (ECDGF) by heparin
    • Gajdusek CM: Release of endothelial cell-derived growth factor (ECDGF) by heparin. J Cell Physiol 1984, 121:12-21.
    • (1984) J Cell Physiol , vol.121 , pp. 12-21
    • Gajdusek, C.M.1
  • 71
    • 0029851233 scopus 로고    scopus 로고
    • Cell density-dependent regulation of basic fibroblast growth factor expression in human renal cell carcinoma cell
    • Singh RK, Llansa N, Bucana CD, Sanchez R, Koura A, Fidler IJ: Cell density-dependent regulation of basic fibroblast growth factor expression in human renal cell carcinoma cell. Cell Growth Diff 1996, 7:397-404.
    • (1996) Cell Growth Diff , vol.7 , pp. 397-404
    • Singh, R.K.1    Llansa, N.2    Bucana, C.D.3    Sanchez, R.4    Koura, A.5    Fidler, I.J.6
  • 72
    • 0026437599 scopus 로고
    • Synthesis of TGF-beta 1 by vascular endothelial cells is correlated with cell spreading
    • Merrilees MJ, Sodek J: Synthesis of TGF-beta 1 by vascular endothelial cells is correlated with cell spreading. J Vasc Res 1992, 29:376-384.
    • (1992) J Vasc Res , vol.29 , pp. 376-384
    • Merrilees, M.J.1    Sodek, J.2
  • 73
    • 0027221555 scopus 로고
    • Transforming growth factor-beta inhibits E-selectin expression on human endothelial cells
    • Gamble JR, Khew-Goodall Y, Vadas MA: Transforming growth factor-beta inhibits E-selectin expression on human endothelial cells. J Immunol 1993, 150:4494-4503.
    • (1993) J Immunol , vol.150 , pp. 4494-4503
    • Gamble, J.R.1    Khew-Goodall, Y.2    Vadas, M.A.3
  • 74
    • 0026636896 scopus 로고
    • Cell density dependent effects of TGF-β demonstrated by a plasminogen activator-based assay for TGF-β
    • Flaumenhaft R, Rifkin DB: Cell density dependent effects of TGF-β demonstrated by a plasminogen activator-based assay for TGF-β. J Cell Physiol 1992, 152:48-55.
    • (1992) J Cell Physiol , vol.152 , pp. 48-55
    • Flaumenhaft, R.1    Rifkin, D.B.2
  • 75
    • 0029033041 scopus 로고
    • Rapid identification of differentially expressed endothelial cell genes by RNA display
    • Kozian DH, Augustin HG: Rapid identification of differentially expressed endothelial cell genes by RNA display. Biochem Biophys Res Commun 1995, 209:1068-1075.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 1068-1075
    • Kozian, D.H.1    Augustin, H.G.2
  • 76
    • 0025811546 scopus 로고
    • Differential expression of extracellular proteins is correlated with angiogenesis in vitro
    • Iruela-Arispe ML, Hasselaar P, Sage H: Differential expression of extracellular proteins is correlated with angiogenesis in vitro. Lab Invest 1991, 64:174-186.
    • (1991) Lab Invest , vol.64 , pp. 174-186
    • Iruela-Arispe, M.L.1    Hasselaar, P.2    Sage, H.3
  • 77
    • 0029053599 scopus 로고
    • The ATF site mediates downregulation of the cyclin a gene during contact inhibition in vascular endothelial cells
    • Yoshizumi M, Hsieh C-M, Zhou F, Tsai J-C, Patterson C, Perrella MA, Lee M-E: The ATF site mediates downregulation of the cyclin A gene during contact inhibition in vascular endothelial cells. Mol Cell Biol 1995, 15:3266-3272.
    • (1995) Mol Cell Biol , vol.15 , pp. 3266-3272
    • Yoshizumi, M.1    Hsieh, C.-M.2    Zhou, F.3    Tsai, J.-C.4    Patterson, C.5    Perrella, M.A.6    Lee, M.-E.7
  • 78
    • 0029964391 scopus 로고    scopus 로고
    • A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells
    • Alliegro MC, Alligro MA: A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells. Dev Biol 1996, 174:288-297.
    • (1996) Dev Biol , vol.174 , pp. 288-297
    • Alliegro, M.C.1    Alligro, M.A.2
  • 79
    • 0029095913 scopus 로고
    • Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells
    • Gaits F, LI RY, Ragab A, Ragab-Thomas JMF, Chap H: Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells. Biochem J 1995, 311:97-103.
    • (1995) Biochem J , vol.311 , pp. 97-103
    • Gaits, F.1    Li, R.Y.2    Ragab, A.3    Ragab-Thomas, J.M.F.4    Chap, H.5
  • 80
    • 0029968728 scopus 로고    scopus 로고
    • Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: The role of PC5, a member of the subtilisin family
    • Campan M, Yoshizumi M, Seidah NG, Lee ME, Bianchi C, Haber E: Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family. Biochemistry 1996, 35:3797-3802.
    • (1996) Biochemistry , vol.35 , pp. 3797-3802
    • Campan, M.1    Yoshizumi, M.2    Seidah, N.G.3    Lee, M.E.4    Bianchi, C.5    Haber, E.6
  • 81
    • 0028063419 scopus 로고
    • Proliferation-dependent changes in release of arachidonic acid from endothelial cells
    • Whatley RE, Satoh K, Zimmerman GA, McIntyre TM, Prescott SM: Proliferation-dependent changes in release of arachidonic acid from endothelial cells. J Clin Invest 1994, 94:1889-1900.
    • (1994) J Clin Invest , vol.94 , pp. 1889-1900
    • Whatley, R.E.1    Satoh, K.2    Zimmerman, G.A.3    McIntyre, T.M.4    Prescott, S.M.5
  • 82
    • 0029928234 scopus 로고    scopus 로고
    • 'Cytosolic' phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation
    • Sierra-Honigmann MR, Bradley JR, Pober JS: 'Cytosolic' phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation. Lab Invest 1996, 74:684-695.
    • (1996) Lab Invest , vol.74 , pp. 684-695
    • Sierra-Honigmann, M.R.1    Bradley, J.R.2    Pober, J.S.3
  • 84
    • 0026754460 scopus 로고
    • Plasminogen activator inhibitor-1 is induced in migrating endothelial cells
    • Pepper MS, Sappino AP, Montesano R, Orci L, Vassalli JD: Plasminogen activator inhibitor-1 is induced in migrating endothelial cells. J Cell Phys 1992, 153:129-139.
    • (1992) J Cell Phys , vol.153 , pp. 129-139
    • Pepper, M.S.1    Sappino, A.P.2    Montesano, R.3    Orci, L.4    Vassalli, J.D.5
  • 86
    • 0031459886 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (bFGF) regulates the expression of the CC chemokine monocyte chemoattractant protein-1 (MCP-1) in autocrine activated endothelial cells
    • in press
    • Wempe F, Lindner V, Augustin HG: Basic fibroblast growth factor (bFGF) regulates the expression of the CC chemokine monocyte chemoattractant protein-1 (MCP-1) in autocrine activated endothelial cells. Arther Throm Vasc Biol 1997, in press.
    • (1997) Arther Throm Vasc Biol
    • Wempe, F.1    Lindner, V.2    Augustin, H.G.3
  • 87
    • 0026746163 scopus 로고
    • Effect of cell density on endothelin release from endothelial cells and phosphoramidon dependent inhibition
    • Zaragoza R, Budzik GP, Dillon TP, Opgenorth TJ: Effect of cell density on endothelin release from endothelial cells and phosphoramidon dependent inhibition. Biochem Pharmacol 1992, 44:851-856.
    • (1992) Biochem Pharmacol , vol.44 , pp. 851-856
    • Zaragoza, R.1    Budzik, G.P.2    Dillon, T.P.3    Opgenorth, T.J.4
  • 88
    • 0024439169 scopus 로고
    • Enhanced responsiveness of endothelium in the growing/motile state to tumor necrosis factor/cachectin
    • Gerlach H, Lieberman H, Bach R, Godman G, Brett J, Stern D: Enhanced responsiveness of endothelium in the growing/motile state to tumor necrosis factor/cachectin. J Exp Med 1989, 170:913-931.
    • (1989) J Exp Med , vol.170 , pp. 913-931
    • Gerlach, H.1    Lieberman, H.2    Bach, R.3    Godman, G.4    Brett, J.5    Stern, D.6
  • 89
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, β-catenin and α-catenin with vascular endothelial (VE)-cadherin
    • Lampugnani MG, Corada M, Caveda L, Breviario F, Ayalon O, Geiger B, Dejana E: The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, β-catenin and α-catenin with vascular endothelial (VE)-cadherin. J Cell Biol 1995, 129:203-217.
    • (1995) J Cell Biol , vol.129 , pp. 203-217
    • Lampugnani, M.G.1    Corada, M.2    Caveda, L.3    Breviario, F.4    Ayalon, O.5    Geiger, B.6    Dejana, E.7
  • 90
    • 0020041794 scopus 로고
    • Synthesis and distribution of cytoskeletal elements in endothelial cells as a function of cell growth and organization
    • Savion N, Vlodavsky I, Greenburg G, Gospodarowicz D: Synthesis and distribution of cytoskeletal elements in endothelial cells as a function of cell growth and organization. J Cell Physiol 1982, 110:129-141.
    • (1982) J Cell Physiol , vol.110 , pp. 129-141
    • Savion, N.1    Vlodavsky, I.2    Greenburg, G.3    Gospodarowicz, D.4
  • 91
    • 0029782951 scopus 로고    scopus 로고
    • Filamin translocation is an early endothelial cell inflammatory response to bradykinin: Regulation by calcium, protein kinases, and protein phosphatases
    • Wang Q, Patton WF, Chiang ET, Hechtman HB, Shepro D: Filamin translocation is an early endothelial cell inflammatory response to bradykinin: regulation by calcium, protein kinases, and protein phosphatases. J Cell Biochem 1996, 62:383-396.
    • (1996) J Cell Biochem , vol.62 , pp. 383-396
    • Wang, Q.1    Patton, W.F.2    Chiang, E.T.3    Hechtman, H.B.4    Shepro, D.5
  • 92
    • 0025818549 scopus 로고
    • Density-dependent expression of hyaluronic acid binding to vascular cells in vitro
    • Antonelli A, D'Amore PA: Density-dependent expression of hyaluronic acid binding to vascular cells in vitro. Microvasc Res 1991, 41:239-251.
    • (1991) Microvasc Res , vol.41 , pp. 239-251
    • Antonelli, A.1    D'Amore, P.A.2
  • 93
    • 0026739264 scopus 로고
    • Migrating endothelial cells are distinctly hyperglycosylated and express specific migration-asssociated cell surface glycoproteins
    • Augustin-Voss HG, Pauli BU: Migrating endothelial cells are distinctly hyperglycosylated and express specific migration-asssociated cell surface glycoproteins. J Cell Biol 1992, 119:483-491.
    • (1992) J Cell Biol , vol.119 , pp. 483-491
    • Augustin-Voss, H.G.1    Pauli, B.U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.