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Volumn 250, Issue 2, 1999, Pages 298-312

Regulation of the type II hemidesmosomal plaque assembly in intestinal epithelial cells

Author keywords

Actin; HD1; Hemidesmosomes; 6 4 integrin

Indexed keywords

ACTIN; INTEGRIN; LAMININ RECEPTOR; MEMBRANE PROTEIN; PLECTIN;

EID: 0033179106     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4549     Document Type: Article
Times cited : (23)

References (62)
  • 1
    • 0030006606 scopus 로고    scopus 로고
    • Desmosomes and hemidesmosomes: Structure and function of molecular components
    • Green K. J., Jones J. C. Desmosomes and hemidesmosomes: Structure and function of molecular components. FASEB J. 10:1996;871-881.
    • (1996) FASEB J. , vol.10 , pp. 871-881
    • Green, K.J.1    Jones, J.C.2
  • 2
    • 0030272476 scopus 로고    scopus 로고
    • Hemidesmosomes: Roles in adhesion, signaling and human diseases
    • Borradori L., Sonnenberg A. Hemidesmosomes: Roles in adhesion, signaling and human diseases. Curr. Opin. Cell. Biol. 8:1996;647-656.
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 647-656
    • Borradori, L.1    Sonnenberg, A.2
  • 4
    • 0025615956 scopus 로고
    • The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia
    • Owaribe K., Kartenbeck J., Stumpp S., Magin T. M., Krieg T., Diaz L. A., Franke W. W. The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia. Differentiation. 45:1990;207-220.
    • (1990) Differentiation , vol.45 , pp. 207-220
    • Owaribe, K.1    Kartenbeck, J.2    Stumpp, S.3    Magin, T.M.4    Krieg, T.5    Diaz, L.A.6    Franke, W.W.7
  • 9
    • 0026726355 scopus 로고
    • Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180
    • Giudice G. J., Emery D. J., Diaz L. A. Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180. J. Invest. Dermatol. 99:1992;243-250.
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 243-250
    • Giudice, G.J.1    Emery, D.J.2    Diaz, L.A.3
  • 10
    • 0026667871 scopus 로고
    • Cloning of partial cDNA for mouse 180-kDa bullous pemphigoid antigen (BPAG2), a highly conserved collagenous protein of the cutaneous basement membrane zone
    • Li K., Guidice G. J., Tamai K., Do H. C., Sawamura D., Diaz L. A., Uitto J. Cloning of partial cDNA for mouse 180-kDa bullous pemphigoid antigen (BPAG2), a highly conserved collagenous protein of the cutaneous basement membrane zone. J. Invest. Dermatol. 99:1992;258-263.
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 258-263
    • Li, K.1    Guidice, G.J.2    Tamai, K.3    Do, H.C.4    Sawamura, D.5    Diaz, L.A.6    Uitto, J.7
  • 11
    • 0027194934 scopus 로고
    • HD4, a 180 kDa bullous pemphigoid antigen, is a major transmembrane glycoprotein of the hemidesmosome
    • Nishizawa Y., Uematsu J., Owaribe K. HD4, a 180 kDa bullous pemphigoid antigen, is a major transmembrane glycoprotein of the hemidesmosome. J. Biochem. 113:1993;493-501.
    • (1993) J. Biochem. , vol.113 , pp. 493-501
    • Nishizawa, Y.1    Uematsu, J.2    Owaribe, K.3
  • 12
    • 0019417455 scopus 로고
    • Characterization of bullous pemphigoid antigen: A unique basement membrane protein of stratified squamous epithelia
    • Stanley J. R., Hawley-Nelson P., Yuspa S. H., Shevach E. M., Katz S. I. Characterization of bullous pemphigoid antigen: A unique basement membrane protein of stratified squamous epithelia. Cell. 24:1981;897-903.
    • (1981) Cell , vol.24 , pp. 897-903
    • Stanley, J.R.1    Hawley-Nelson, P.2    Yuspa, S.H.3    Shevach, E.M.4    Katz, S.I.5
  • 13
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda Y., Nishizawa Y., Uematsu J., Owaribe K. Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116:1992;1497-1506.
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 14
    • 0026755162 scopus 로고
    • Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments
    • Green K. J., Virata M. L., Elgart G. W., Stanley J. R., Parry D. A. Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments. Int. J. Biol. Macromol. 14:1992;145-153.
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.5
  • 15
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: Versatile organizers of cytoskeletal architecture
    • Ruhrberg C., Watt F. M. The plakin family: Versatile organizers of cytoskeletal architecture. Curr. Opin. Genet. Dev. 7:1997;392-397.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, F.M.2
  • 20
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes
    • Carter W. G., Ryan M. C., Gahr P. J. Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell. 65:1991;599-610.
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 21
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle P., Lunstrum G. P., Keene D. R., Burgeson R. E. Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114:1991;567-576.
    • (1991) J. Cell Biol. , vol.114 , pp. 567-576
    • Rousselle, P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 22
    • 0024651413 scopus 로고
    • Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton
    • Burridge K., Fath K. Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton. BioEssays. 10:1989;104-108.
    • (1989) BioEssays , vol.10 , pp. 104-108
    • Burridge, K.1    Fath, K.2
  • 23
    • 0025728669 scopus 로고
    • Intermediate filament-plasma membrane interactions
    • Jones J. C., Green K. J. Intermediate filament-plasma membrane interactions. Curr. Opin. Cell Biol. 3:1991;127-132.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 127-132
    • Jones, J.C.1    Green, K.J.2
  • 24
    • 0028197645 scopus 로고
    • Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H
    • Uematsu J., Nishizawa Y., Sonnenberg A., Owaribe K. Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H. J. Biochem. 115:1994;469-476.
    • (1994) J. Biochem. , vol.115 , pp. 469-476
    • Uematsu, J.1    Nishizawa, Y.2    Sonnenberg, A.3    Owaribe, K.4
  • 25
    • 0029916097 scopus 로고    scopus 로고
    • Developmental expression of laminin-5 and HD1 in the intestine: Epithelial to mesenchymal shift for the laminin gamma 2 chain subunit deposition
    • Orian-Rousseau V., Aberdam D., Fontao L., Chevalier L., Meneguzzi G., Kedinger M., Simon-Assmann P. Developmental expression of laminin-5 and HD1 in the intestine: Epithelial to mesenchymal shift for the laminin gamma 2 chain subunit deposition. Dev. Dyn. 206:1996;12-23.
    • (1996) Dev. Dyn. , vol.206 , pp. 12-23
    • Orian-Rousseau, V.1    Aberdam, D.2    Fontao, L.3    Chevalier, L.4    Meneguzzi, G.5    Kedinger, M.6    Simon-Assmann, P.7
  • 26
    • 0031568977 scopus 로고    scopus 로고
    • Polarized expression of HD1: Relationship with the cytoskeleton in cultured human colonic carcinoma cells
    • Fontao L., Dirrig S., Owaribe K., Kedinger M., Launay J. F. Polarized expression of HD1: Relationship with the cytoskeleton in cultured human colonic carcinoma cells. Exp. Cell Res. 231:1997;319-327.
    • (1997) Exp. Cell Res. , vol.231 , pp. 319-327
    • Fontao, L.1    Dirrig, S.2    Owaribe, K.3    Kedinger, M.4    Launay, J.F.5
  • 27
    • 0028129795 scopus 로고
    • Differential expression of laminin isoforms and α6β4 integrin subunits in the developing human and mouse intestine
    • Simon-Assmann P., Duclos B., Orian-Rousseau V., Arnold C., Mathelin C., Engvall E., Kedinger M. Differential expression of laminin isoforms and α6β4 integrin subunits in the developing human and mouse intestine. Dev. Dyn. 201:1994;71-85.
    • (1994) Dev. Dyn. , vol.201 , pp. 71-85
    • Simon-Assmann, P.1    Duclos, B.2    Orian-Rousseau, V.3    Arnold, C.4    Mathelin, C.5    Engvall, E.6    Kedinger, M.7
  • 28
    • 0026245786 scopus 로고
    • Transmembrane molecular assemblies in cell-extracellular matrix interactions
    • Turner C. E., Burridge K. Transmembrane molecular assemblies in cell-extracellular matrix interactions. Curr. Opin. Cell Biol. 3:1991;849-853.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 849-853
    • Turner, C.E.1    Burridge, K.2
  • 29
    • 0030820604 scopus 로고    scopus 로고
    • A minimal region on the integrin β4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells
    • Niessen C. M., Hulsman E. H. M., Oomen L. C. J. M., Kuikman I., Sonnenberg A. A minimal region on the integrin β4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells. J. Cell Sci. 110:1997;1705-1716.
    • (1997) J. Cell Sci. , vol.110 , pp. 1705-1716
    • Niessen, C.M.1    Hulsman, E.H.M.2    Oomen, L.C.J.M.3    Kuikman, I.4    Sonnenberg, A.5
  • 31
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R. O. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 32
    • 0026061088 scopus 로고
    • Polarized expression of integrin receptors (α6β4, α2β1, α3β1, and αvβ5) and their relationship with the cytoskeleton and basement membrane matrix in cultured human keratinocytes
    • Marchisio P. C., Bondanza S., Cremona O., Cancedda R., De Luca M. Polarized expression of integrin receptors (α6β4, α2β1, α3β1, and αvβ5) and their relationship with the cytoskeleton and basement membrane matrix in cultured human keratinocytes. J. Cell Biol. 112:1991;761-773.
    • (1991) J. Cell Biol. , vol.112 , pp. 761-773
    • Marchisio, P.C.1    Bondanza, S.2    Cremona, O.3    Cancedda, R.4    De Luca, M.5
  • 33
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson K., Sheets E. D., Simson R. Revisiting the fluid mosaic model of membranes. Science. 268:1995;1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 34
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E. A., Brugge J. S. Integrins and signal transduction pathways: The road taken. Science. 268:1995;233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 35
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada K. M., Miyamoto S. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:1995;681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 37
    • 0028169729 scopus 로고
    • The α6 and β4 integrin subunits are expressed by smooth muscle cells of human small vessels: A new localization in mesenchymal cells
    • Cremona O., Savoia P., Marchisio P. C., Gabbiani G., Chaponnier C. The α6 and β4 integrin subunits are expressed by smooth muscle cells of human small vessels: A new localization in mesenchymal cells. J. Histochem. Cytochem. 42:1994;1221-1228.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 1221-1228
    • Cremona, O.1    Savoia, P.2    Marchisio, P.C.3    Gabbiani, G.4    Chaponnier, C.5
  • 38
  • 39
    • 0027242415 scopus 로고
    • The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro
    • Langhofer M., Hopkinson S. B., Jones J. C. The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro. J. Cell Sci. 105:1993;753-764.
    • (1993) J. Cell Sci. , vol.105 , pp. 753-764
    • Langhofer, M.1    Hopkinson, S.B.2    Jones, J.C.3
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0026566812 scopus 로고
    • Differential expression of laminin isoforms and β4 integrin epitopes in the basement membrane zone of normal human skin and basal cell carcinomas
    • Sollberg S., Peltonen J., Uitto J. Differential expression of laminin isoforms and β4 integrin epitopes in the basement membrane zone of normal human skin and basal cell carcinomas. J. Invest. Dermatol. 98:1992;864-870.
    • (1992) J. Invest. Dermatol. , vol.98 , pp. 864-870
    • Sollberg, S.1    Peltonen, J.2    Uitto, J.3
  • 44
    • 0028307978 scopus 로고
    • Developmental expression of nicein adhesion protein (laminin-5) subunits suggests multiple morphogenic roles
    • Aberdam D., Aguzzi A., Baudoin C., Galliano M. F., Ortonne J. P., Meneguzzi G. Developmental expression of nicein adhesion protein (laminin-5) subunits suggests multiple morphogenic roles. Cell Adhes. Commun. 2:1994;115-129.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 115-129
    • Aberdam, D.1    Aguzzi, A.2    Baudoin, C.3    Galliano, M.F.4    Ortonne, J.P.5    Meneguzzi, G.6
  • 45
    • 0027746104 scopus 로고
    • Formation of hemidesmosomes in cells of a transformed murine mammary tumor cell line and mechanisms involved in adherence of these cells to laminin and kalinin
    • Sonnenberg A., de Melker A. A., Martinez d. V., Janssen H., Calafat J., Niessen C. M. Formation of hemidesmosomes in cells of a transformed murine mammary tumor cell line and mechanisms involved in adherence of these cells to laminin and kalinin. J. Cell Sci. 106:1993;1083-1102.
    • (1993) J. Cell Sci. , vol.106 , pp. 1083-1102
    • Sonnenberg, A.1    De Melker, A.A.2    Martinez, D.V.3    Janssen, H.4    Calafat, J.5    Niessen, C.M.6
  • 46
    • 0031868639 scopus 로고    scopus 로고
    • Human colonic cancer cells synthesize and adhere to laminin-5. Their adhesion to laminin-5 involves multiple receptors among which is integrin α2β1
    • Orian-Rousseau V., Aberdam D., Rousselle P., Messent A., Gavrilovic J., Meneguzzi G., Kedinger M., Simon-Assmann P. Human colonic cancer cells synthesize and adhere to laminin-5. Their adhesion to laminin-5 involves multiple receptors among which is integrin α2β1. J. Cell Sci. 111:1998;1993-2004.
    • (1998) J. Cell Sci. , vol.111 , pp. 1993-2004
    • Orian-Rousseau, V.1    Aberdam, D.2    Rousselle, P.3    Messent, A.4    Gavrilovic, J.5    Meneguzzi, G.6    Kedinger, M.7    Simon-Assmann, P.8
  • 48
    • 0020162216 scopus 로고
    • The nuclear matrix: Three-dimensional architecture and protein composition
    • Capco D. G., Wan K. M., Penman S. The nuclear matrix: Three-dimensional architecture and protein composition. Cell. 29:1982;847-858.
    • (1982) Cell , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 49
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • Fey E. G., Wan K. M., Penman S. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition. J. Cell Biol. 98:1984;1973-1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 50
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo L., Degenstein L., Dowling J., Yu Q. C., Wollmann R., Perman B., Fuchs E. Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:1995;233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 51
    • 0029990621 scopus 로고    scopus 로고
    • Deficiency of the integrin beta 4 subunit in junctional epidermolysis bullosa with pyloric atresia: Consequences for hemidesmosome formation and adhesion properties
    • Niessen C. M., van der Raaij-Helmer M. H., Hulsman E. H., van der Neut R., Jonkman M. F., Sonnenberg A. Deficiency of the integrin beta 4 subunit in junctional epidermolysis bullosa with pyloric atresia: Consequences for hemidesmosome formation and adhesion properties. J. Cell Sci. 109:1996;1695-1706.
    • (1996) J. Cell Sci. , vol.109 , pp. 1695-1706
    • Niessen, C.M.1    Van Der Raaij-Helmer, M.H.2    Hulsman, E.H.3    Van Der Neut, R.4    Jonkman, M.F.5    Sonnenberg, A.6
  • 52
    • 0030462929 scopus 로고    scopus 로고
    • Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: Possible involvement of the rho signal cascade
    • Enomoto T. Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: Possible involvement of the rho signal cascade. Cell Struct. Funct. 21:1996;317-326.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 317-326
    • Enomoto, T.1
  • 53
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • ChrzanowskaWodnicka M., Burridge K. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1996;1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowskawodnicka, M.1    Burridge, K.2
  • 54
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science. 279:1998;509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 56
    • 0031971198 scopus 로고    scopus 로고
    • Modulation of hepatocyte growth factor-induced scattering of HT29 colon carcinoma cells - Involvement of the MAPK pathway
    • Herrera R. Modulation of hepatocyte growth factor-induced scattering of HT29 colon carcinoma cells - Involvement of the MAPK pathway. J. Cell Sci. 111:1998;1039-1049.
    • (1998) J. Cell Sci. , vol.111 , pp. 1039-1049
    • Herrera, R.1
  • 58
    • 0031980707 scopus 로고    scopus 로고
    • Cell adhesion to laminin 1 or 5 induces isoform-specific clustering of integrins and other focal adhesion components
    • Dogic D., Rousselle P., Aumailley M. Cell adhesion to laminin 1 or 5 induces isoform-specific clustering of integrins and other focal adhesion components. J. Cell Sci. 111:1998;793-802.
    • (1998) J. Cell Sci. , vol.111 , pp. 793-802
    • Dogic, D.1    Rousselle, P.2    Aumailley, M.3
  • 59
    • 0031283128 scopus 로고    scopus 로고
    • The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • Rabinovitz I., Mercurio A. M. The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J. Cell Biol. 139:1997;1873-1884.
    • (1997) J. Cell Biol. , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2


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