메뉴 건너뛰기




Volumn 20, Issue 2, 1999, Pages 85-91

Hereditary diseases of desmosomes

Author keywords

Ectodermal dysplasia; Keratinocyte; Skin blistering

Indexed keywords

CADHERIN; DESMOCOLLIN; DESMOGLEIN;

EID: 0033049427     PISSN: 09231811     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-1811(99)00015-8     Document Type: Conference Paper
Times cited : (26)

References (37)
  • 1
    • 0027548587 scopus 로고
    • Desmosomes and hemidesmosomes
    • Garrod D.R. Desmosomes and hemidesmosomes. Curr Opin Cell Biol. 5:1993;30-40.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 30-40
    • Garrod, D.R.1
  • 2
    • 0030178994 scopus 로고    scopus 로고
    • Epithelial development and differentiation: The role of desmosomes
    • Garrod D.R. Epithelial development and differentiation: the role of desmosomes. J R Coll Phys Lond. 30:1996;366-373.
    • (1996) J R Coll Phys Lond , vol.30 , pp. 366-373
    • Garrod, D.R.1
  • 3
    • 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
  • 4
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filament and desmosomal proteins
    • Kouklis P.D., Hutton E., Fuchs E. Making a connection: direct binding between keratin intermediate filament and desmosomal proteins. J Cell Biol. 127:1995;1049-1060.
    • (1995) J Cell Biol , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 5
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interactions
    • Cowin P., Burke B. Cytoskeleton-membrane interactions. Curr Opin Cell Biol. 8:1996;56-65.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 56-65
    • Cowin, P.1    Burke, B.2
  • 6
    • 0027264134 scopus 로고
    • Nomenclature of the desmosomal cadherins
    • Buxton R.S., Cowin P., Franke W.W. et al. Nomenclature of the desmosomal cadherins. J Cell Biol. 121:1993;481-483.
    • (1993) J Cell Biol , vol.121 , pp. 481-483
    • Buxton, R.S.1    Cowin, P.2    Franke, W.W.3
  • 7
    • 0029095515 scopus 로고
    • Hailey-Hailey disease maps to a 5cM interval on chromosome 3q21-p24
    • Richard G., Korge B.E., Wright A.R. et al. Hailey-Hailey disease maps to a 5cM interval on chromosome 3q21-p24. J Invest Dermatol. 105:1995;257-260.
    • (1995) J Invest Dermatol , vol.105 , pp. 257-260
    • Richard, G.1    Korge, B.E.2    Wright, A.R.3
  • 8
    • 9044240868 scopus 로고    scopus 로고
    • Localization of the Darier disease gene to a 2-cM portion of 12q23-24.1
    • Wakem P., Ikeda S., Haake A. et al. Localization of the Darier disease gene to a 2-cM portion of 12q23-24.1. J Invest Dermatol. 106:1996;365-367.
    • (1996) J Invest Dermatol , vol.106 , pp. 365-367
    • Wakem, P.1    Ikeda, S.2    Haake, A.3
  • 9
    • 0025719081 scopus 로고
    • Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP) and plakoglobin DPIII (JUP)
    • Arnemann J., Spurr N.K., Wheeler G.N. et al. Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP) and plakoglobin DPIII (JUP). Genomics. 10:1991;640-645.
    • (1991) Genomics , vol.10 , pp. 640-645
    • Arnemann, J.1    Spurr, N.K.2    Wheeler, G.N.3
  • 10
    • 0029041276 scopus 로고
    • Localization of a locus for the striated form of palmoplantar keratoderma to chromosome 18q near the desmosomal cadherin gene cluster
    • Hennies H.C., Kuster W., Mischke D., Reis A. Localization of a locus for the striated form of palmoplantar keratoderma to chromosome 18q near the desmosomal cadherin gene cluster. Hum Mol Genet. 4:1995;1015-1020.
    • (1995) Hum Mol Genet , vol.4 , pp. 1015-1020
    • Hennies, H.C.1    Kuster, W.2    Mischke, D.3    Reis, A.4
  • 11
    • 0030931871 scopus 로고    scopus 로고
    • The plakophilin 1 (PKP1) and plakoglobin (JUP) genes map to human chromosomes 1q and 17, respectively
    • Cowley C.M., Simrak D., Spurr N.K. et al. The plakophilin 1 (PKP1) and plakoglobin (JUP) genes map to human chromosomes 1q and 17, respectively. Hum Genet. 100:1997;486-488.
    • (1997) Hum Genet , vol.100 , pp. 486-488
    • Cowley, C.M.1    Simrak, D.2    Spurr, N.K.3
  • 12
    • 0028144738 scopus 로고
    • Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family
    • Hatzfeld M., Kristjansson G.I., Plessmann U., Weber W. Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family. J Cell Sci. 107:1994;2259-2270.
    • (1994) J Cell Sci , vol.107 , pp. 2259-2270
    • Hatzfeld, M.1    Kristjansson, G.I.2    Plessmann, U.3    Weber, W.4
  • 13
    • 0028609366 scopus 로고
    • Cell type-specific desmosomal plaque proteins of the plakoglobin family: Plakophilin 1 (band 6 protein)
    • Heid H.W., Schmidt A., Zimbelmann R. et al. Cell type-specific desmosomal plaque proteins of the plakoglobin family: plakophilin 1 (band 6 protein). Differentiation. 58:1994;113-131.
    • (1994) Differentiation , vol.58 , pp. 113-131
    • Heid, H.W.1    Schmidt, A.2    Zimbelmann, R.3
  • 14
    • 0030856140 scopus 로고    scopus 로고
    • Plakophilins 1a and 1b: Widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components
    • Schmidt A., Langbein L., Rode M. et al. Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components. Cell Tissue Res. 290:1997;481-499.
    • (1997) Cell Tissue Res , vol.290 , pp. 481-499
    • Schmidt, A.1    Langbein, L.2    Rode, M.3
  • 15
    • 84984774604 scopus 로고    scopus 로고
    • Mutations in the plakophilin 1 gene result in ectodermal dysplasia/skin fragility syndrome
    • McGrath J.A., McMillan J.R., Shemanko C.S. et al. Mutations in the plakophilin 1 gene result in ectodermal dysplasia/skin fragility syndrome. Nat Genet. 17:1997;240-244.
    • (1997) Nat Genet , vol.17 , pp. 240-244
    • McGrath, J.A.1    McMillan, J.R.2    Shemanko, C.S.3
  • 16
    • 0032988426 scopus 로고    scopus 로고
    • Skin fragility and hypohidrotic ectodermal dysplasia resulting from ablation of plakophilin 1
    • McGrath J.A., Hoeger P.H., Christiano A.M. et al. Skin fragility and hypohidrotic ectodermal dysplasia resulting from ablation of plakophilin 1. Br J Dermatol. 140:1999;297-307.
    • (1999) Br J Dermatol , vol.140 , pp. 297-307
    • McGrath, J.A.1    Hoeger, P.H.2    Christiano, A.M.3
  • 17
    • 0031019355 scopus 로고    scopus 로고
    • The distribution of the desmosomal protein, plakophilin 1, in human skin and skin tumors
    • Moll I., Kurzen H., Langbein L., Franke W.W. The distribution of the desmosomal protein, plakophilin 1, in human skin and skin tumors. J Invest Dermatol. 108:1997;139-146.
    • (1997) J Invest Dermatol , vol.108 , pp. 139-146
    • Moll, I.1    Kurzen, H.2    Langbein, L.3    Franke, W.W.4
  • 18
    • 0027985785 scopus 로고
    • Tylosis oesophageal cancer mapped
    • Risk J.M., Field E.A., Field J.K. et al. Tylosis oesophageal cancer mapped. Nat Genet. 8:1994;219-221.
    • (1994) Nat Genet , vol.8 , pp. 219-221
    • Risk, J.M.1    Field, E.A.2    Field, J.K.3
  • 19
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer M., Berg S., Reynolds A.B. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell. 76:1994;789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 20
    • 0001920132 scopus 로고    scopus 로고
    • Band 6 protein and cytoskeletal organization
    • P. Cowin, & M.W. Klymkowsky. Heidelberg: Springer
    • Hatzfeld M. Band 6 protein and cytoskeletal organization. Cowin P., Klymkowsky M.W. Cytoskeletal-Membrane Interactions and Signal Transduction. 1997;49-60 Springer, Heidelberg.
    • (1997) Cytoskeletal-Membrane Interactions and Signal Transduction , pp. 49-60
    • Hatzfeld, M.1
  • 21
    • 0027937655 scopus 로고
    • Overexpression of cadherins and underexpression of β-catenin inhibit dorsal mesoderm induction in early Xenopus embryos
    • Heasman J., Crawford A., Goldstone K. et al. Overexpression of cadherins and underexpression of β-catenin inhibit dorsal mesoderm induction in early Xenopus embryos. Cell. 79:1994;791-803.
    • (1994) Cell , vol.79 , pp. 791-803
    • Heasman, J.1    Crawford, A.2    Goldstone, K.3
  • 22
    • 0028982101 scopus 로고
    • Signal transduction by β-catenin
    • Gumbiner B.M. Signal transduction by β-catenin. Curr Opin Cell Biol. 7:1995;634-640.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 634-640
    • Gumbiner, B.M.1
  • 23
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF-1
    • Behrens J., von Kries J.P., Kuhl M. et al. Functional interaction of β-catenin with the transcription factor LEF-1. Nature. 382:1996;638-642.
    • (1996) Nature , vol.382 , pp. 638-642
    • Behrens, J.1    Von Kries, J.P.2    Kuhl, M.3
  • 24
    • 0029915306 scopus 로고    scopus 로고
    • Binding to cadherins antagonizes the signaling capacity of β-catenin during axis formation in xenopus
    • Fagotto F., Funayama N., Gluck U., Gumbiner B.M. Binding to cadherins antagonizes the signaling capacity of β-catenin during axis formation in xenopus. J Cell Biol. 132:1996;1105-1114.
    • (1996) J Cell Biol , vol.132 , pp. 1105-1114
    • Fagotto, F.1    Funayama, N.2    Gluck, U.3    Gumbiner, B.M.4
  • 25
    • 0028839834 scopus 로고
    • The body language of cells: The intimate connection between cell adhesion and behavior
    • Klymkowsky M.W., Parr B. The body language of cells: the intimate connection between cell adhesion and behavior. Cell. 83:1995;5-8.
    • (1995) Cell , vol.83 , pp. 5-8
    • Klymkowsky, M.W.1    Parr, B.2
  • 26
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through β-catenin and specification of cell fate during embryogenesis
    • Miller J.R., Moon R.T. Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev. 10:1996;2527-2539.
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 27
    • 0026511055 scopus 로고
    • The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells
    • Stappenbeck T.S., Green K.J. The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells. J Cell Biol. 116:1992;1197-1209.
    • (1992) J Cell Biol , vol.116 , pp. 1197-1209
    • Stappenbeck, T.S.1    Green, K.J.2
  • 28
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • Stappenbeck T.S., Bornslaeger E.A., Corcoran C.M. et al. Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks. J Cell Biol. 123:1993;691-705.
    • (1993) J Cell Biol , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3
  • 29
    • 0030856050 scopus 로고    scopus 로고
    • Two-hybrid analysis reveals fundamental differences in direct interations between desmoplakin and cell type-specific intermediate filaments
    • Meng J.J., Bornslaeger E.A., Green K.J., Steinert P.M., Ip W. Two-hybrid analysis reveals fundamental differences in direct interations between desmoplakin and cell type-specific intermediate filaments. J Biol Chem. 272:1997;21495-21503.
    • (1997) J Biol Chem , vol.272 , pp. 21495-21503
    • Meng, J.J.1    Bornslaeger, E.A.2    Green, K.J.3    Steinert, P.M.4    Ip, W.5
  • 30
    • 0013610245 scopus 로고    scopus 로고
    • Desmoplakin interacts with armadillo proteins in both classic and desmosomal cadherin complexes
    • (Abstract)
    • Green K.J., Kowalczyk A.P., Hatzfeld M., Bornslaeger E.A. Desmoplakin interacts with armadillo proteins in both classic and desmosomal cadherin complexes. J Invest Dermatol. 110:1998;498. (Abstract).
    • (1998) J Invest Dermatol , vol.110 , pp. 498
    • Green, K.J.1    Kowalczyk, A.P.2    Hatzfeld, M.3    Bornslaeger, E.A.4
  • 31
    • 0030699073 scopus 로고    scopus 로고
    • The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes
    • Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E. et al. The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes. J Cell Biol. 139:1997;773-784.
    • (1997) J Cell Biol , vol.139 , pp. 773-784
    • Kowalczyk, A.P.1    Bornslaeger, E.A.2    Borgwardt, J.E.3
  • 32
    • 0032100705 scopus 로고    scopus 로고
    • Defining the interactions between intermediate filaments and desmosomes
    • Smith E.A., Fuchs E. Defining the interactions between intermediate filaments and desmosomes. J Cell Biol. 141:1998;1229-1241.
    • (1998) J Cell Biol , vol.141 , pp. 1229-1241
    • Smith, E.A.1    Fuchs, E.2
  • 33
    • 21544441484 scopus 로고    scopus 로고
    • Roles of plakoglobin end domains in desmosome assembly
    • Palka H.L., Green K.J. Roles of plakoglobin end domains in desmosome assembly. J Cell Sci. 110:1997;2359-2371.
    • (1997) J Cell Sci , vol.110 , pp. 2359-2371
    • Palka, H.L.1    Green, K.J.2
  • 34
    • 0030589631 scopus 로고    scopus 로고
    • Embryonic heart and skin defects in mice lacking plakoglobin
    • Bierkamp C., Mclaughlin K.J., Schwarz H. et al. Embryonic heart and skin defects in mice lacking plakoglobin. Dev Biol. 180:1996;780-785.
    • (1996) Dev Biol , vol.180 , pp. 780-785
    • Bierkamp, C.1    McLaughlin, K.J.2    Schwarz, H.3
  • 35
    • 0029895526 scopus 로고    scopus 로고
    • Mice expressing a mutant desmosomal cadherin exhibit abnormalities in desmosomes, proliferation and epidermal differentiation
    • Allen E., Yu Q.C., Fuchs E. Mice expressing a mutant desmosomal cadherin exhibit abnormalities in desmosomes, proliferation and epidermal differentiation. J Cell Biol. 133:1996;1367-1382.
    • (1996) J Cell Biol , vol.133 , pp. 1367-1382
    • Allen, E.1    Yu, Q.C.2    Fuchs, E.3
  • 36
    • 0030902370 scopus 로고    scopus 로고
    • Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris
    • Koch P.J., Mahoney M.G., Ishikawa H. et al. Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris. J Cell Biol. 137:1997;1091-1102.
    • (1997) J Cell Biol , vol.137 , pp. 1091-1102
    • Koch, P.J.1    Mahoney, M.G.2    Ishikawa, H.3
  • 37
    • 0013602405 scopus 로고    scopus 로고
    • Pemphigus vulgaris (PV) antigen (desmoglein 3) anchors telogen hair in the follicle
    • (Abstract)
    • Koch P.J., Mahoney M.G., Rothenberger K. et al. Pemphigus vulgaris (PV) antigen (desmoglein 3) anchors telogen hair in the follicle. J Invest Dermatol. 110:1998;493. (Abstract).
    • (1998) J Invest Dermatol , vol.110 , pp. 493
    • Koch, P.J.1    Mahoney, M.G.2    Rothenberger, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.