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Volumn 8, Issue 4, 1997, Pages 451-462

Inhibition of junction assembly in cultured epithelial cells by hepatocyte growth factor/scatter factor is concomitant with increased stability and altered phosphorylation of the soluble junctional molecules

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; COLONY STIMULATING FACTOR 1; PLAKOGLOBIN; PROTEIN TYROSINE KINASE; RECEPTOR PROTEIN; SCATTER FACTOR; TRITON X 100; UVOMORULIN;

EID: 0030991289     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (32)

References (78)
  • 1
    • 0024784640 scopus 로고
    • Protein factors which regulate cell motility
    • Rosen, E. M., and Goldberg, I. D. Protein factors which regulate cell motility. In Vitro Cell Dev. Biol., 25: 1079-1087, 1989.
    • (1989) In Vitro Cell Dev. Biol. , vol.25 , pp. 1079-1087
    • Rosen, E.M.1    Goldberg, I.D.2
  • 2
    • 0028999868 scopus 로고
    • The many faces of hepatocyte growth factor: From hepatopoiesis to hematopoiesis
    • Zarnegar, R., and Michalopoulos, G. K. The many faces of hepatocyte growth factor: from hepatopoiesis to hematopoiesis. J. Cell Biol., 129: 1177-1180, 1995.
    • (1995) J. Cell Biol. , vol.129 , pp. 1177-1180
    • Zarnegar, R.1    Michalopoulos, G.K.2
  • 3
    • 0028564863 scopus 로고
    • Scatter factor and the c-Met receptor: A paradigm for mesenchymal/epithelial interaction
    • Rosen, E. M., Nigam, S. K., and Goldberg, I. D. Scatter factor and the c-Met receptor: a paradigm for mesenchymal/epithelial interaction. J. Cell Biol., 127: 1783-1787, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1783-1787
    • Rosen, E.M.1    Nigam, S.K.2    Goldberg, I.D.3
  • 4
    • 0000975548 scopus 로고
    • Purification and characterization of a growth factor from rat platelets for mature parenchymal hepatocytes in primary culture
    • Nakamura, T., Teramoto, H., and Ichihara, A. Purification and characterization of a growth factor from rat platelets for mature parenchymal hepatocytes in primary culture. Proc. Natl. Acad. Sci. USA, 83: 6489-6494, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6489-6494
    • Nakamura, T.1    Teramoto, H.2    Ichihara, A.3
  • 5
    • 0025805633 scopus 로고
    • Identification of the hepatocyte growth factor receptor as the c-met-proto-oncogene product
    • Washington DC
    • Bottaro, D. P., Rubin, J. S., Faletto, D. L., Chan, A. M. L., Kmiecik, T. E., Vande Woude, G. F., and Aaronson, S. A. Identification of the hepatocyte growth factor receptor as the c-met-proto-oncogene product. Science (Washington DC), 251: 802-804, 1991.
    • (1991) Science , vol.251 , pp. 802-804
    • Bottaro, D.P.1    Rubin, J.S.2    Faletto, D.L.3    Chan, A.M.L.4    Kmiecik, T.E.5    Vande Woude, G.F.6    Aaronson, S.A.7
  • 6
    • 0025119463 scopus 로고
    • Scatter factor: Molecular characteristics and effect on the invasiveness of epithelial cells
    • Weidner, K. M., Behrens, J., Vandekerckhove, J., and Birchmeier, W. Scatter factor: molecular characteristics and effect on the invasiveness of epithelial cells. J. Cell Biol., 111: 2097-2108, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 2097-2108
    • Weidner, K.M.1    Behrens, J.2    Vandekerckhove, J.3    Birchmeier, W.4
  • 7
    • 0026696638 scopus 로고
    • Hepatocyte growth factor and transforming growth factor-β stimulate both cell growth and migration of human gastric adenocarcinoma cells
    • Shibamoto, S. Hepatocyte growth factor and transforming growth factor-β stimulate both cell growth and migration of human gastric adenocarcinoma cells. Cell Struct. Funct., 17: 185-190, 1992.
    • (1992) Cell Struct. Funct. , vol.17 , pp. 185-190
    • Shibamoto, S.1
  • 9
    • 0025734655 scopus 로고
    • Hepatocyte growth factor (HGF) stimulates the tyrosine kinase activity of the receptor encoded by the protooncogene c-MET
    • Naldini, L., Vigna, E., Narsimhan, R. P., Gaudino, G., Zarnegar, R., Michalopoulos, G. K., and Comoglio, P. M. Hepatocyte growth factor (HGF) stimulates the tyrosine kinase activity of the receptor encoded by the protooncogene c-MET. Oncogene, 6: 501-504, 1991.
    • (1991) Oncogene , vol.6 , pp. 501-504
    • Naldini, L.1    Vigna, E.2    Narsimhan, R.P.3    Gaudino, G.4    Zarnegar, R.5    Michalopoulos, G.K.6    Comoglio, P.M.7
  • 10
    • 1242348060 scopus 로고
    • Sequence of met-proto-oncogene cDNA has features characteristic of tyrosine kinase family of growth factor receptors
    • Park, M., Dean, M., Kaul, K., Braun, M. J., Gond, M. A., and Vande Woude, G. Sequence of met-proto-oncogene cDNA has features characteristic of tyrosine kinase family of growth factor receptors. Proc. Natl. Acad. Sci. USA, 84: 6379-6383, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6379-6383
    • Park, M.1    Dean, M.2    Kaul, K.3    Braun, M.J.4    Gond, M.A.5    Vande Woude, G.6
  • 11
    • 0026489665 scopus 로고
    • The presence of hepatocyte growth factor in the developing rat
    • Camb.
    • Defrances, M. C., Wolf, H. K., Michalopoulos, G. K., and Zarnegar, R. The presence of hepatocyte growth factor in the developing rat. Development (Camb.), 116: 387-395, 1992.
    • (1992) Development , vol.116 , pp. 387-395
    • Defrances, M.C.1    Wolf, H.K.2    Michalopoulos, G.K.3    Zarnegar, R.4
  • 13
    • 0027348751 scopus 로고
    • Expression of the met-receptor and its ligand, HGF-SF during mouse embryogenesis
    • Sonnenberg, E., Weidner, K. M., and Birchmeier, C. Expression of the met-receptor and its ligand, HGF-SF during mouse embryogenesis. EXS., 65: 381-394, 1993.
    • (1993) EXS , vol.65 , pp. 381-394
    • Sonnenberg, E.1    Weidner, K.M.2    Birchmeier, C.3
  • 14
    • 0027208193 scopus 로고
    • Expression of the met/hepatocyte growth factor/scatter factor receptor and its ligand during differentiation of murine p19 embryonal carcinoma cells
    • Yang, X. M., and Park, M. Expression of the met/hepatocyte growth factor/scatter factor receptor and its ligand during differentiation of murine p19 embryonal carcinoma cells. Dev. Biol., 157: 308-320, 1993.
    • (1993) Dev. Biol. , vol.157 , pp. 308-320
    • Yang, X.M.1    Park, M.2
  • 15
    • 0027437547 scopus 로고
    • Scatter factor/hepatocyte growth factor and its receptor, the c-met tyrosine kinase, can mediate a signal exchange between mesenchyme and epithelia during mouse development
    • Sonnenberg, E., Meyer, D., Weidner, K. M., and Birchmeier, C. Scatter factor/hepatocyte growth factor and its receptor, the c-met tyrosine kinase, can mediate a signal exchange between mesenchyme and epithelia during mouse development. J. Cell Biol., 123: 223-235, 1993.
    • (1993) J. Cell Biol. , vol.123 , pp. 223-235
    • Sonnenberg, E.1    Meyer, D.2    Weidner, K.M.3    Birchmeier, C.4
  • 16
    • 0027830892 scopus 로고
    • Hepatocyte growth factor/scatter factor (HGF/SF), the c-Met receptor and the behaviour of epithelial cells
    • Gherardi, E., Sharp, M., Lane, K., Sirulnik, A., and Stoker, M. Hepatocyte growth factor/scatter factor (HGF/SF), the c-Met receptor and the behaviour of epithelial cells. Symp. Soc. Exp. Biol., 47: 163-181, 1993.
    • (1993) Symp. Soc. Exp. Biol. , vol.47 , pp. 163-181
    • Gherardi, E.1    Sharp, M.2    Lane, K.3    Sirulnik, A.4    Stoker, M.5
  • 17
    • 0027759435 scopus 로고
    • Molecular mechanisms leading to loss of differentiation and gain of invasiveness in epithelial cells
    • Birchmeier, W., Weidner, K. M., and Behrens, J. Molecular mechanisms leading to loss of differentiation and gain of invasiveness in epithelial cells. J. Cell Sci. Suppl., 17: 159-164, 1993.
    • (1993) J. Cell Sci. Suppl. , vol.17 , pp. 159-164
    • Birchmeier, W.1    Weidner, K.M.2    Behrens, J.3
  • 18
    • 0028349254 scopus 로고
    • Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and non-transformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in transformed model epithelium
    • Nusrat, A., Parkos, C. A., Bacarra, A. E., Godowski, P. J., Delp-Archer, C., Rosen, E. M., and Madara, J. L. Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and non-transformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in transformed model epithelium. J. Clin. Invest., 93: 2056-2065, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2056-2065
    • Nusrat, A.1    Parkos, C.A.2    Bacarra, A.E.3    Godowski, P.J.4    Delp-Archer, C.5    Rosen, E.M.6    Madara, J.L.7
  • 19
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as morphogenetic regulator
    • Washington DC
    • Takeichi, M. Cadherin cell adhesion receptors as morphogenetic regulator. Science (Washington DC), 252: 1451-1455, 1991.
    • (1991) Science , vol.252 , pp. 1451-1455
    • Takeichi, M.1
  • 21
    • 0027548587 scopus 로고
    • Desmosomes and hemidesmosomes
    • Garrod, D. R. Desmosomes and hemidesmosomes. Curr. Opin. Cell Biol., 5: 30-40, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 30-40
    • Garrod, D.R.1
  • 22
    • 0026687386 scopus 로고
    • Plakoglobin, or an 83 kD homologue distinct from β-catenin, interacts with E-cadherin and N-cadherin
    • Knudsen, K. A., and Wheelock, M. J. Plakoglobin, or an 83 kD homologue distinct from β-catenin, interacts with E-cadherin and N-cadherin. J. Cell Biol., 118: 671-679, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 671-679
    • Knudsen, K.A.1    Wheelock, M.J.2
  • 23
    • 0026661360 scopus 로고
    • The vertebrate adhesive junction proteins β-catenin, and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties
    • Peifer, M., McCrea, P. D., Green, K. J., Wieschaus, E., and Gumbiner, B. M. The vertebrate adhesive junction proteins β-catenin, and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties. J. Cell Biol., 118: 681-691, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 681-691
    • Peifer, M.1    McCrea, P.D.2    Green, K.J.3    Wieschaus, E.4    Gumbiner, B.M.5
  • 24
    • 0027273236 scopus 로고
    • Defining E-cadherin associated protein complexes in epithelial cells: Plakoglobin, β-catenin and γ-catenin are distinct components
    • Piepenhagen, P. A., and Nelson, W. J. Defining E-cadherin associated protein complexes in epithelial cells: plakoglobin, β-catenin and γ-catenin are distinct components. J. Cell Sci., 104: 751-762, 1993.
    • (1993) J. Cell Sci. , vol.104 , pp. 751-762
    • Piepenhagen, P.A.1    Nelson, W.J.2
  • 27
    • 0023643123 scopus 로고
    • Biochemical characterization of the soluble form of the junctional protein, plakoglobin, from different cell types
    • Kapprell, H-P., Cowin, P., and Franke, W. W. Biochemical characterization of the soluble form of the junctional protein, plakoglobin, from different cell types. Eur. J. Biochem., 166: 505-517, 1987.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 505-517
    • Kapprell, H.-P.1    Cowin, P.2    Franke, W.W.3
  • 28
    • 0028035292 scopus 로고
    • Unraveling the cytoplasmic interactions of the cadherin superfamily
    • Cowin, P. Unraveling the cytoplasmic interactions of the cadherin superfamily. Proc. Natl. Acad. Sci. USA, 91: 10759-10761, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10759-10761
    • Cowin, P.1
  • 29
    • 0020695954 scopus 로고
    • Calcium regulation of cell-cell contact and differentiation of epidermal cells in culture: An ultrastructural study
    • Henning, H., and Holbrook, K. A. Calcium regulation of cell-cell contact and differentiation of epidermal cells in culture: an ultrastructural study. Exp. Cell Res., 143: 127-142, 1983.
    • (1983) Exp. Cell Res. , vol.143 , pp. 127-142
    • Henning, H.1    Holbrook, K.A.2
  • 30
    • 0026505270 scopus 로고
    • Protein kinase inhibitors prevent junctional dissociation induced by low extracellular calcium in MDCK epithelial cells
    • Citi, S. Protein kinase inhibitors prevent junctional dissociation induced by low extracellular calcium in MDCK epithelial cells. J. Cell Biol., 117: 169-178, 1994.
    • (1994) J. Cell Biol. , vol.117 , pp. 169-178
    • Citi, S.1
  • 31
    • 0028936246 scopus 로고
    • Desmosome assembly and disassembly are regulated by reversible protein phosphorylation in cultured epithelial cells
    • Pasdar, M., Li, Z., and Chan, H. Desmosome assembly and disassembly are regulated by reversible protein phosphorylation in cultured epithelial cells. Cell Motil. Cytoskeleton, 30: 108-122, 1995.
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 108-122
    • Pasdar, M.1    Li, Z.2    Chan, H.3
  • 33
    • 0023864445 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis
    • Pasdar, M., and Nelson, W. J. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis. J. Cell Biol., 106: 677-685, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 677-685
    • Pasdar, M.1    Nelson, W.J.2
  • 34
    • 0024076701 scopus 로고
    • Organization of desmosomal plaque proteins in cells growing at low calcium concentrations
    • Duden, R., and Franke, W. W. Organization of desmosomal plaque proteins in cells growing at low calcium concentrations. J. Cell Biol., 107: 1049-1064, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 1049-1064
    • Duden, R.1    Franke, W.W.2
  • 35
    • 0022787708 scopus 로고
    • Splitting and internalization of the desmosomes of cultured kidney epithelial cells by reduction in calcium concentration
    • Mattey, D. L., and Garrod, D. R. Splitting and internalization of the desmosomes of cultured kidney epithelial cells by reduction in calcium concentration. J. Cell Sci., 85: 95-111, 1986.
    • (1986) J. Cell Sci. , vol.85 , pp. 95-111
    • Mattey, D.L.1    Garrod, D.R.2
  • 36
    • 0025937744 scopus 로고
    • The role of E-cadherin and scatter factor in tumor invasion and cell motility
    • I. D. Goldberg (ed.), Basel, Switzerland: Birkhauser Verlag
    • Behrens, J., Weidner, K. M., Frixen, U. H., Schipper, J. H., Sachs, M., Arakaki, N., Daikuhara, Y., and Birchmeier, W. The role of E-cadherin and scatter factor in tumor invasion and cell motility. In: I. D. Goldberg (ed.), Cell Motility Factors, pp. 109-126. Basel, Switzerland: Birkhauser Verlag, 1991.
    • (1991) Cell Motility Factors , pp. 109-126
    • Behrens, J.1    Weidner, K.M.2    Frixen, U.H.3    Schipper, J.H.4    Sachs, M.5    Arakaki, N.6    Daikuhara, Y.7    Birchmeier, W.8
  • 37
    • 0028043577 scopus 로고
    • Effect of hepatocyte growth factor on the expression of E- and P-cadherin in gastric carcinoma cell lines
    • Tannapfel, A., Yasui, W., Yokozaki, H., Wittekind, C., and Tahara, E. Effect of hepatocyte growth factor on the expression of E-and P-cadherin in gastric carcinoma cell lines. Virchows Arch. A Pathol. Anat. Hist., 425: 139-144, 1994.
    • (1994) Virchows Arch. A Pathol. Anat. Hist. , vol.425 , pp. 139-144
    • Tannapfel, A.1    Yasui, W.2    Yokozaki, H.3    Wittekind, C.4    Tahara, E.5
  • 38
    • 0027219750 scopus 로고
    • Effect of hepatocyte growth factor on cadherin-mediated cell-cell adhesion
    • Watabe, M., Matsumoto, K., Nakamura, T., Takeichi, M. Effect of hepatocyte growth factor on cadherin-mediated cell-cell adhesion. Cell Struct. Funct., 18: 117-124, 1993.
    • (1993) Cell Struct. Funct. , vol.18 , pp. 117-124
    • Watabe, M.1    Matsumoto, K.2    Nakamura, T.3    Takeichi, M.4
  • 39
    • 0028026665 scopus 로고
    • Receptor chimeras indicate that the Met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor
    • Zhu, H., Naujokas, M. A., and Park, M. Receptor chimeras indicate that the Met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor. Cell Growth & Differ., 5: 1-8, 1994.
    • (1994) Cell Growth & Differ. , vol.5 , pp. 1-8
    • Zhu, H.1    Naujokas, M.A.2    Park, M.3
  • 40
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily: Domains for cell surface recognition
    • Williams, A, F., and Barclay, A. N. The immunoglobulin superfamily: domains for cell surface recognition. Annu. Rev. Immunol., 6: 381-405, 1988.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 41
    • 0028028202 scopus 로고
    • Tyrosine 1356 in the carboxyl-terminal tail of the HGF/SF receptor is essential for the transduction of signals for cell motility and morphogenesis
    • Zhu, H., Najokas, M. A., Fixman, E. D., Torossian, K., and Park, M. Tyrosine 1356 in the carboxyl-terminal tail of the HGF/SF receptor is essential for the transduction of signals for cell motility and morphogenesis. J. Biol. Chem., 269: 29943-29948, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29943-29948
    • Zhu, H.1    Najokas, M.A.2    Fixman, E.D.3    Torossian, K.4    Park, M.5
  • 42
    • 0028351702 scopus 로고
    • A multifunctional docking site mediates signaling and transformation by hepatocyte growth factor/scatter factor receptor family
    • Ponzetto, C., Bardelli, A., Zhen, Z., Maina, F., Dallazonca, P., Giordano, S., Graziani, A., Panayotou, G., and Comoglio, P. M. A multifunctional docking site mediates signaling and transformation by hepatocyte growth factor/scatter factor receptor family. Cell, 77: 261-271, 1994.
    • (1994) Cell , vol.77 , pp. 261-271
    • Ponzetto, C.1    Bardelli, A.2    Zhen, Z.3    Maina, F.4    Dallazonca, P.5    Giordano, S.6    Graziani, A.7    Panayotou, G.8    Comoglio, P.M.9
  • 43
    • 0028847161 scopus 로고
    • Plakoglobin: Kinetics of synthesis, phosphorylation, stability, and interactions with desmoglein and E-cadherin
    • Pasdar, M., Li, Z., and Chlumecky, V. Plakoglobin: kinetics of synthesis, phosphorylation, stability, and interactions with desmoglein and E-cadherin. Cell Motil. Cytoskeleton, 32: 258-272, 1995.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 258-272
    • Pasdar, M.1    Li, Z.2    Chlumecky, V.3
  • 44
    • 0026723902 scopus 로고
    • Epithelial morphogenesis
    • Gumbiner, B. M. Epithelial morphogenesis. Cell, 69: 385-387, 1992.
    • (1992) Cell , vol.69 , pp. 385-387
    • Gumbiner, B.M.1
  • 45
    • 0026742310 scopus 로고
    • Cadherin mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi, N., Hamaguchi, M., Taniguchi, S., Nagafuchi, A., Tsukita, S., and Takeichi, M. Cadherin mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol., 118: 703-714, 1991.
    • (1991) J. Cell Biol. , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 46
    • 0027459346 scopus 로고
    • p60vsrc causes tyrosine phosphorylation and inactivation of the N-cadherin cell adhesion system
    • Hamaguchi, M., Matsuyoshi, N., Ohnishi, Y., Gotoh, B., Takeichi, M., and Nagai, Y. p60vsrc causes tyrosine phosphorylation and inactivation of the N-cadherin cell adhesion system. EMBO J., 12: 307-314, 1993.
    • (1993) EMBO J. , vol.12 , pp. 307-314
    • Hamaguchi, M.1    Matsuyoshi, N.2    Ohnishi, Y.3    Gotoh, B.4    Takeichi, M.5    Nagai, Y.6
  • 47
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature sensitive v-SRC gene
    • Behrens, J., Vakaet, L., Fritis, R., Winterberger, E., Van Roy, F., Mareel, M. M., and Birchmeier, W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature sensitive v-SRC gene. J. Cell Biol., 120: 757-766, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Fritis, R.3    Winterberger, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 48
    • 0026338562 scopus 로고
    • The role of phosphorylation in development of tight junctions in cultured renal epithelial (MDCK) cells
    • Nigam, S. K., Denisenko, N., Rodriguez-Boulan, E., and Citi, S. The role of phosphorylation in development of tight junctions in cultured renal epithelial (MDCK) cells. Biochem. Biophys. Res. Commun., 181: 548-553, 1991.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 548-553
    • Nigam, S.K.1    Denisenko, N.2    Rodriguez-Boulan, E.3    Citi, S.4
  • 49
    • 0022993985 scopus 로고
    • Plakoglobin: A protein common to different kinds of intercellular adhering junctions
    • Cowin, P., Kapprell, H. P., Franke, W. W., Tamkun, J., and Hynes, R. O. Plakoglobin: a protein common to different kinds of intercellular adhering junctions. Cell, 46: 1063-1073, 1986.
    • (1986) Cell , vol.46 , pp. 1063-1073
    • Cowin, P.1    Kapprell, H.P.2    Franke, W.W.3    Tamkun, J.4    Hynes, R.O.5
  • 51
    • 0029076819 scopus 로고
    • Anterior axis duplication in Xenopus induced by the over-expression of the cadherin-binding protein plakoglobin
    • Karnovsky, A., and Klymkowsky, M. W. Anterior axis duplication in Xenopus induced by the over-expression of the cadherin-binding protein plakoglobin. Proc. Natl. Acad. Sci. USA, 92: 4522-4526, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4522-4526
    • Karnovsky, A.1    Klymkowsky, M.W.2
  • 52
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol., 7: 619-627, 1995.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 53
    • 0003126743 scopus 로고
    • The cell adhesion molecule uvomorulin
    • G. M. Edelman, B. A. Cunningham, and J. P. Theiry (eds.), New York: John Wiley & Sons
    • Kemler, R., Gossler, A., Mansouri, A., and Vestweber, D. The cell adhesion molecule uvomorulin. In: G. M. Edelman, B. A. Cunningham, and J. P. Theiry (eds.), Morphoregulatory Molecules, pp. 41-56. New York: John Wiley & Sons, 1990.
    • (1990) Morphoregulatory Molecules , pp. 41-56
    • Kemler, R.1    Gossler, A.2    Mansouri, A.3    Vestweber, D.4
  • 54
    • 0023577552 scopus 로고
    • Calcium-dependent cell-cell adhesion molecules (cadherins): Subclass specificities and possible involvement of actin bundles
    • Hirano, S., Nose, A., Hatta, K., Kawakami, A., and Takeichi, M. Calcium-dependent cell-cell adhesion molecules (cadherins): subclass specificities and possible involvement of actin bundles. J. Cell Biol., 105: 2501-2510, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2501-2510
    • Hirano, S.1    Nose, A.2    Hatta, K.3    Kawakami, A.4    Takeichi, M.5
  • 55
    • 0025933683 scopus 로고
    • Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells
    • Shore, E. M., and Nelson, W. J. Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells. J. Biol. Chem., 266: 19672-19680, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19672-19680
    • Shore, E.M.1    Nelson, W.J.2
  • 56
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • McNeill, H., Ryan, T. A., Smith, S. J., and Nelson, W. J. Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J. Cell Biol., 120: 1217-1226, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 57
    • 1842368519 scopus 로고
    • Tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature sensitive vSRC gene
    • Shibamoto, S. M., Hayakawa, K., Takeuchi, T., Hori, T., Oku, N., Miyazawa, K., Kitamura, N., Takeichi, M., and Ito, F. Tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature sensitive vSRC gene. J. Cell Biol., 120: 757-766, 1994.
    • (1994) J. Cell Biol. , vol.120 , pp. 757-766
    • Shibamoto, S.M.1    Hayakawa, K.2    Takeuchi, T.3    Hori, T.4    Oku, N.5    Miyazawa, K.6    Kitamura, N.7    Takeichi, M.8    Ito, F.9
  • 58
    • 0029125390 scopus 로고
    • HGF/SF inhibits junctional communication
    • Moorby, C. D., Stoker, M., and Gherardi, E. HGF/SF inhibits junctional communication. Exp. Cell Res., 219: 657-663, 1995.
    • (1995) Exp. Cell Res. , vol.219 , pp. 657-663
    • Moorby, C.D.1    Stoker, M.2    Gherardi, E.3
  • 59
  • 60
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin 43 in junctional communication-competent and deficient cell lines
    • Musil, L. S., Cunningham, B. A., Edelman, G. M., and Goodenough, D. A. Differential phosphorylation of the gap junction protein connexin 43 in junctional communication-competent and deficient cell lines. J. Cell Biol., 111: 2077-2088, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 61
    • 0028176375 scopus 로고
    • Alterations in β-catenin phosphorylation and plakoglobin expression in breast cancer cells
    • Sommers, C. L., Gelmann, E. P., Kemler, R., Cowin, P., and Byers, S. W. Alterations in β-catenin phosphorylation and plakoglobin expression in breast cancer cells. Cancer Res., 54: 3544-3552, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 3544-3552
    • Sommers, C.L.1    Gelmann, E.P.2    Kemler, R.3    Cowin, P.4    Byers, S.W.5
  • 62
    • 0026114963 scopus 로고
    • Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells
    • Volberg, T., Gieger, B., Dror, R., and Zick, Y. Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells. Cell Regul., 2: 105-120, 1991.
    • (1991) Cell Regul. , vol.2 , pp. 105-120
    • Volberg, T.1    Gieger, B.2    Dror, R.3    Zick, Y.4
  • 63
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions
    • Volberg, T., Zick, Y., Dror, R., Sabanay, I., Gilon, C., Levitzki, A., and Geiger, B. The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions. EMBO J., 11: 1733-1742, 1992.
    • (1992) EMBO J. , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3    Sabanay, I.4    Gilon, C.5    Levitzki, A.6    Geiger, B.7
  • 64
    • 0028982101 scopus 로고
    • Signal transduction by β-catenin
    • Gumbiner, B. Signal transduction by β-catenin. Curr. Opin. Cell Biol., 7: 634-640, 1995.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 634-640
    • Gumbiner, B.1
  • 65
    • 0028047389 scopus 로고
    • Wingless Signal and Zeste-white 3 kinase trigger opposing changes in the intracellular distribution of Armadillo
    • Camb.
    • Peifer, M., Sweeton, D., Casey, M., and Weischaus, E. Wingless Signal and Zeste-white 3 kinase trigger opposing changes in the intracellular distribution of Armadillo. Development (Camb.), 120: 369-380, 1994.
    • (1994) Development , vol.120 , pp. 369-380
    • Peifer, M.1    Sweeton, D.2    Casey, M.3    Weischaus, E.4
  • 66
    • 0029762881 scopus 로고    scopus 로고
    • Regulating cell proliferation: As easy as APC
    • Washington DC
    • Peifer, M. Regulating cell proliferation: as easy as APC. Science (Washington DC), 272: 974-975, 1996.
    • (1996) Science , vol.272 , pp. 974-975
    • Peifer, M.1
  • 67
    • 0026772731 scopus 로고
    • Wnt genes
    • Nusse, R., and Varmus, H. E. Wnt genes. Cell, 69: 1073-1087, 1992.
    • (1992) Cell , vol.69 , pp. 1073-1087
    • Nusse, R.1    Varmus, H.E.2
  • 68
    • 0029019497 scopus 로고
    • Regulation of Wnt5a mRNA expression in human mammary epithelial cells by cell shape, confluence, and hepatocyte growth factor
    • Huguet, E. L., Smith, K., Bicknell, R., and Harris, A. L. Regulation of Wnt5a mRNA expression in human mammary epithelial cells by cell shape, confluence, and hepatocyte growth factor. J. Biol. Chem., 270: 12851-12856, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12851-12856
    • Huguet, E.L.1    Smith, K.2    Bicknell, R.3    Harris, A.L.4
  • 69
    • 0028258532 scopus 로고
    • Targeting of the SF/HGF receptor to the basolateral domain of polarized epithelial cells
    • Crepaldi, T., Pollack, A. L., Prat, M., Zborek, A., Mostov, K., and Comoglio, P. M. Targeting of the SF/HGF receptor to the basolateral domain of polarized epithelial cells. J. Cell Biol., 125: 313-320, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 313-320
    • Crepaldi, T.1    Pollack, A.L.2    Prat, M.3    Zborek, A.4    Mostov, K.5    Comoglio, P.M.6
  • 70
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa, M., Baribault, H., and Kemler, R. The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J., 8: 1711-1717, 1989.
    • (1989) EMBO J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 71
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi, A., and Takeichi, M. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO J., 7: 3679-3684, 1988.
    • (1988) EMBO J. , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 72
    • 0024095524 scopus 로고
    • Role of cell adhesion molecule uvomorulin in formation and maintenance of the epithelial junctional complex
    • Gumbiner, B. M., Stevenson, B. R., and Grimaldi, A. Role of cell adhesion molecule uvomorulin in formation and maintenance of the epithelial junctional complex. J. Cell Biol., 107: 1575-1587, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 1575-1587
    • Gumbiner, B.M.1    Stevenson, B.R.2    Grimaldi, A.3
  • 73
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex assembly
    • Hinck, L., Nathke, I. S., Papkoff, J., and Nelson, W. J. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol., 125: 1327-1340, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Nathke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 74
    • 0028289669 scopus 로고
    • Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells
    • Nathke, I. S., Hinck, L., Swedlow, J. R., Papkoff, J., and Nelson, W. J. Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells. J. Cell Biol., 125: 1341-1352, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 1341-1352
    • Nathke, I.S.1    Hinck, L.2    Swedlow, J.R.3    Papkoff, J.4    Nelson, W.J.5
  • 75
    • 0024383949 scopus 로고
    • Regulation of desmosome assembly in epithelial cells: Kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain
    • Pasdar, M., and Nelson, W. J. Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain. J. Cell Biol., 109: 163-177, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 163-177
    • Pasdar, M.1    Nelson, W.J.2
  • 76
    • 1842288006 scopus 로고
    • Biochemical approaches for analyzing de novo assembly of epithelial junctional components
    • B. R. Stevenson, W. J. Gallin, and D. L. Paul (eds.), Oxford: IRL Press
    • Pasdar, M. Biochemical approaches for analyzing de novo assembly of epithelial junctional components. In: B. R. Stevenson, W. J. Gallin, and D. L. Paul (eds.), Cell-Cell Interactions, A Practical Approach, pp. 203-226. Oxford: IRL Press, 1992.
    • (1992) Cell-Cell Interactions, a Practical Approach , pp. 203-226
    • Pasdar, M.1
  • 77
  • 78
    • 0023838729 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. II. Morphological analysis
    • Pasdar, M., and Nelson, W. J. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. II. Morphological analysis. J. Cell Biol., 106: 687-695, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 687-695
    • Pasdar, M.1    Nelson, W.J.2


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