메뉴 건너뛰기




Volumn 34, Issue 6, 2014, Pages 1127-1145

Desmosomes and Extradesmosomal Adhesive Signaling Contacts in Pemphigus

Author keywords

Autoantibodies; Cell adhesion; Desmogleins; Desmosomes; Pemphigus; Steric hindrance

Indexed keywords

ARMADILLO DOMAIN PROTEIN; AUTOANTIBODY; DESMOGLEIN 3; DESMOSOMAL CADHERIN; EPIDERMAL GROWTH FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE P38; PLAKIN; PROTEIN KINASE C; CADHERIN;

EID: 84907971653     PISSN: 01986325     EISSN: 10981128     Source Type: Journal    
DOI: 10.1002/med.21310     Document Type: Article
Times cited : (63)

References (138)
  • 1
    • 77955073513 scopus 로고    scopus 로고
    • Desmosomes: Adhesive strength and signalling in health and disease
    • Thomason HA, Scothern A, McHarg S, Garrod DR. Desmosomes: Adhesive strength and signalling in health and disease. Biochem J 2010;429(3):419-433.
    • (2010) Biochem J , vol.429 , Issue.3 , pp. 419-433
    • Thomason, H.A.1    Scothern, A.2    McHarg, S.3    Garrod, D.R.4
  • 2
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar MG, Palade GE. Junctional complexes in various epithelia. J Cell Biol 1963;17(2):375-412.
    • (1963) J Cell Biol , vol.17 , Issue.2 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 5
    • 79960709751 scopus 로고    scopus 로고
    • Desmosomes
    • Dubash AD, Green KJ. Desmosomes. Curr Biol 2011;21(14):R529-R531.
    • (2011) Curr Biol , vol.21 , Issue.14 , pp. R529-R531
    • Dubash, A.D.1    Green, K.J.2
  • 6
    • 82755194912 scopus 로고    scopus 로고
    • Cell-cell connectivity: Desmosomes and disease
    • Brooke MA, Nitoiu D, Kelsell DP. Cell-cell connectivity: Desmosomes and disease. J Pathol 2012;226(2):158-171.
    • (2012) J Pathol , vol.226 , Issue.2 , pp. 158-171
    • Brooke, M.A.1    Nitoiu, D.2    Kelsell, D.P.3
  • 8
    • 84879710397 scopus 로고    scopus 로고
    • Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells
    • Franke W, Heid H, Zimbelmann R, Kuhn C, Winter-Simanowski S, Dörflinger Y, Grund C, Rickelt S. Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells. Cell Tissue Res 2013;353(1):99-115.
    • (2013) Cell Tissue Res , vol.353 , Issue.1 , pp. 99-115
    • Franke, W.1    Heid, H.2    Zimbelmann, R.3    Kuhn, C.4    Winter-Simanowski, S.5    Dörflinger, Y.6    Grund, C.7    Rickelt, S.8
  • 9
    • 84862804462 scopus 로고    scopus 로고
    • Non-junctional human desmoglein 3 acts as an upstream regulator of Src in E-cadherin adhesion, a pathway possibly involved in the pathogenesis of pemphigus vulgaris
    • Tsang SM, Brown L, Lin K, Liu L, Piper K, O'Toole EA, Grose R, Hart IR, Garrod DR, Fortune F, Wan H. Non-junctional human desmoglein 3 acts as an upstream regulator of Src in E-cadherin adhesion, a pathway possibly involved in the pathogenesis of pemphigus vulgaris. J Pathol 2012;227(1):81-93.
    • (2012) J Pathol , vol.227 , Issue.1 , pp. 81-93
    • Tsang, S.M.1    Brown, L.2    Lin, K.3    Liu, L.4    Piper, K.5    O'Toole, E.A.6    Grose, R.7    Hart, I.R.8    Garrod, D.R.9    Fortune, F.10    Wan, H.11
  • 10
    • 39149091017 scopus 로고    scopus 로고
    • Outside-in signaling through integrins and cadherins: A central mechanism to control epidermal growth and differentiation
    • Müller EJ, Williamson L, Kolly C, Suter MM. Outside-in signaling through integrins and cadherins: A central mechanism to control epidermal growth and differentiation? J Invest Dermatol 2008;128(3):501-516.
    • (2008) J Invest Dermatol , vol.128 , Issue.3 , pp. 501-516
    • Müller, E.J.1    Williamson, L.2    Kolly, C.3    Suter, M.M.4
  • 11
    • 84856909766 scopus 로고    scopus 로고
    • Desmoglein as a target in skin disease and beyond
    • Amagai M, Stanley JR. Desmoglein as a target in skin disease and beyond. J Invest Dermatol 2012;132(3):776-784.
    • (2012) J Invest Dermatol , vol.132 , Issue.3 , pp. 776-784
    • Amagai, M.1    Stanley, J.R.2
  • 13
    • 77957267604 scopus 로고    scopus 로고
    • The cardiac desmosome and arrhythmogenic cardiomyopathies: From gene to disease
    • Delmar M, McKenna WJ. The cardiac desmosome and arrhythmogenic cardiomyopathies: From gene to disease. Circ Res 2010;107(6):700-714.
    • (2010) Circ Res , vol.107 , Issue.6 , pp. 700-714
    • Delmar, M.1    McKenna, W.J.2
  • 14
    • 84859111164 scopus 로고    scopus 로고
    • Pathophysiology of arrhythmogenic cardiomyopathy
    • Basso C, Bauce B, Corrado D, Thiene G. Pathophysiology of arrhythmogenic cardiomyopathy. Nat Rev Cardiol 2012;9(4):223-233.
    • (2012) Nat Rev Cardiol , vol.9 , Issue.4 , pp. 223-233
    • Basso, C.1    Bauce, B.2    Corrado, D.3    Thiene, G.4
  • 15
    • 84862764554 scopus 로고    scopus 로고
    • Mutations with pathogenic potential in proteins located in or at the composite junctions of the intercalated disk connecting mammalian cardiomyocytes: A reference thesaurus for arrhythmogenic cardiomyopathies and for Naxos and Carvajal diseases
    • Rickelt S, Pieperhoff S. Mutations with pathogenic potential in proteins located in or at the composite junctions of the intercalated disk connecting mammalian cardiomyocytes: A reference thesaurus for arrhythmogenic cardiomyopathies and for Naxos and Carvajal diseases. Cell Tissue Res 2012;348(2):325-333.
    • (2012) Cell Tissue Res , vol.348 , Issue.2 , pp. 325-333
    • Rickelt, S.1    Pieperhoff, S.2
  • 16
    • 34250365241 scopus 로고    scopus 로고
    • Desmosomes: A role in cancer
    • Chidgey M, Dawson C. Desmosomes: A role in cancer? Br J Cancer 2007;96(12):1783-1787.
    • (2007) Br J Cancer , vol.96 , Issue.12 , pp. 1783-1787
    • Chidgey, M.1    Dawson, C.2
  • 18
    • 41949131198 scopus 로고    scopus 로고
    • Sequence and structural determinants of strand swapping in cadherin domains: Do all cadherins bind through the same adhesive interface
    • Posy S, Shapiro L, Honig B. Sequence and structural determinants of strand swapping in cadherin domains: Do all cadherins bind through the same adhesive interface? J Mol Biol 2008;378(4):954-968.
    • (2008) J Mol Biol , vol.378 , Issue.4 , pp. 954-968
    • Posy, S.1    Shapiro, L.2    Honig, B.3
  • 19
    • 78751494023 scopus 로고    scopus 로고
    • Membrane-impermeable cross-linking provides evidence for homophilic, isoform-specific binding of desmosomal cadherins in epithelial cells
    • Nie Z, Merritt A, Rouhi-Parkouhi M, Tabernero L, Garrod D. Membrane-impermeable cross-linking provides evidence for homophilic, isoform-specific binding of desmosomal cadherins in epithelial cells. J Biol Chem 2011;286(3):2143-2154.
    • (2011) J Biol Chem , vol.286 , Issue.3 , pp. 2143-2154
    • Nie, Z.1    Merritt, A.2    Rouhi-Parkouhi, M.3    Tabernero, L.4    Garrod, D.5
  • 20
    • 36849060240 scopus 로고    scopus 로고
    • The molecular architecture of cadherins in native epidermal desmosomes
    • Al-Amoudi A, Diez DC, Betts MJ, Frangakis AS. The molecular architecture of cadherins in native epidermal desmosomes. Nature 2007;450(7171):832-837.
    • (2007) Nature , vol.450 , Issue.7171 , pp. 832-837
    • Al-Amoudi, A.1    Diez, D.C.2    Betts, M.J.3    Frangakis, A.S.4
  • 21
    • 0141865704 scopus 로고    scopus 로고
    • Untangling desmosomal knots with electron tomography
    • He W, Cowin P, Stokes DL. Untangling desmosomal knots with electron tomography. Science 2003;302(5642):109-113.
    • (2003) Science , vol.302 , Issue.5642 , pp. 109-113
    • He, W.1    Cowin, P.2    Stokes, D.L.3
  • 22
    • 27644507915 scopus 로고    scopus 로고
    • Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction
    • Waschke J, Bruggeman P, Baumgartner W, Zillikens D, Drenckhahn D. Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction. J Clin Invest 2005;115(11):3157-3165.
    • (2005) J Clin Invest , vol.115 , Issue.11 , pp. 3157-3165
    • Waschke, J.1    Bruggeman, P.2    Baumgartner, W.3    Zillikens, D.4    Drenckhahn, D.5
  • 24
    • 49649084477 scopus 로고    scopus 로고
    • Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction
    • Heupel WM, Zillikens D, Drenckhahn D, Waschke J. Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction. J Immunol 2008;181(3):1825-1834.
    • (2008) J Immunol , vol.181 , Issue.3 , pp. 1825-1834
    • Heupel, W.M.1    Zillikens, D.2    Drenckhahn, D.3    Waschke, J.4
  • 26
    • 33645114837 scopus 로고    scopus 로고
    • Delineation of diversified desmoglein distribution in stratified squamous epithelia: Implications in diseases
    • Mahoney MG, Hu Y, Brennan D, Bazzi H, Christiano AM, Wahl JK, 3rd. Delineation of diversified desmoglein distribution in stratified squamous epithelia: Implications in diseases. Exp Dermatol 2006;15(2):101-109.
    • (2006) Exp Dermatol , vol.15 , Issue.2 , pp. 101-109
    • Mahoney, M.G.1    Hu, Y.2    Brennan, D.3    Bazzi, H.4    Christiano, A.M.5    Wahl III, J.K.6
  • 27
    • 84872224315 scopus 로고    scopus 로고
    • Desmoglein 2 is less important than desmoglein 3 for keratinocyte cohesion
    • Hartlieb E, Kempf B, Partilla M, Vigh B, Spindler V, Waschke J. Desmoglein 2 is less important than desmoglein 3 for keratinocyte cohesion. PLoS One 2013;8(1):e53739.
    • (2013) PLoS One , vol.8 , Issue.1 , pp. e53739
    • Hartlieb, E.1    Kempf, B.2    Partilla, M.3    Vigh, B.4    Spindler, V.5    Waschke, J.6
  • 28
    • 1842857530 scopus 로고    scopus 로고
    • Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells
    • Eshkind L, Tian Q, Schmidt A, Franke WW, Windoffer R, Leube RE. Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells. Eur J Cell Biol 2002;81(11):592-598.
    • (2002) Eur J Cell Biol , vol.81 , Issue.11 , pp. 592-598
    • Eshkind, L.1    Tian, Q.2    Schmidt, A.3    Franke, W.W.4    Windoffer, R.5    Leube, R.E.6
  • 29
    • 0030902370 scopus 로고    scopus 로고
    • Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris
    • Koch PJ, Mahoney MG, Ishikawa H, Pulkkinen L, Uitto J, Shultz L, Murphy GF, Whitaker-Menezes D, Stanley JR. Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris. J Cell Biol 1997;137(5):1091-1102.
    • (1997) J Cell Biol , vol.137 , Issue.5 , pp. 1091-1102
    • Koch, P.J.1    Mahoney, M.G.2    Ishikawa, H.3    Pulkkinen, L.4    Uitto, J.5    Shultz, L.6    Murphy, G.F.7    Whitaker-Menezes, D.8    Stanley, J.R.9
  • 30
    • 53349175477 scopus 로고    scopus 로고
    • Loss of desmocollin 3 in mice leads to epidermal blistering
    • Chen J, Den Z, Koch PJ. Loss of desmocollin 3 in mice leads to epidermal blistering. J Cell Sci 2008;121(17):2844-2849.
    • (2008) J Cell Sci , vol.121 , Issue.17 , pp. 2844-2849
    • Chen, J.1    Den, Z.2    Koch, P.J.3
  • 31
    • 0033557198 scopus 로고    scopus 로고
    • Explanations for the clinical and microscopic localization of lesions in pemphigus foliaceus and vulgaris
    • Mahoney MG, Wang Z, Rothenberger K, Koch PJ, Amagai M, Stanley JR. Explanations for the clinical and microscopic localization of lesions in pemphigus foliaceus and vulgaris. J Clin Invest 1999;103(4):461-468.
    • (1999) J Clin Invest , vol.103 , Issue.4 , pp. 461-468
    • Mahoney, M.G.1    Wang, Z.2    Rothenberger, K.3    Koch, P.J.4    Amagai, M.5    Stanley, J.R.6
  • 33
    • 34047099312 scopus 로고    scopus 로고
    • Suprabasal Dsg2 expression in transgenic mouse skin confers a hyperproliferative and apoptosis-resistant phenotype to keratinocytes
    • Brennan D, Hu Y, Joubeh S, Choi YW, Whitaker-Menezes D, O'Brien T, Uitto J, Rodeck U, Mahoney MG. Suprabasal Dsg2 expression in transgenic mouse skin confers a hyperproliferative and apoptosis-resistant phenotype to keratinocytes. J Cell Sci 2007;120(5):758-771.
    • (2007) J Cell Sci , vol.120 , Issue.5 , pp. 758-771
    • Brennan, D.1    Hu, Y.2    Joubeh, S.3    Choi, Y.W.4    Whitaker-Menezes, D.5    O'Brien, T.6    Uitto, J.7    Rodeck, U.8    Mahoney, M.G.9
  • 34
    • 34748902244 scopus 로고    scopus 로고
    • Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca(2+)-dependent, low-affinity trans-interaction
    • Waschke J, Menendez-Castro C, Bruggeman P, Koob R, Amagai M, Gruber HJ, Drenckhahn D, Baumgartner W. Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca(2+)-dependent, low-affinity trans-interaction. J Membr Biol 2007;216(2-3):83-92.
    • (2007) J Membr Biol , vol.216 , Issue.2-3 , pp. 83-92
    • Waschke, J.1    Menendez-Castro, C.2    Bruggeman, P.3    Koob, R.4    Amagai, M.5    Gruber, H.J.6    Drenckhahn, D.7    Baumgartner, W.8
  • 35
    • 77749315803 scopus 로고    scopus 로고
    • The epidermal Ca(2+) gradient: Measurement using the phasor representation of fluorescent lifetime imaging
    • Celli A, Sanchez S, Behne M, Hazlett T, Gratton E, Mauro T. The epidermal Ca(2+) gradient: Measurement using the phasor representation of fluorescent lifetime imaging. Biophys J 2010;98(5):911-921.
    • (2010) Biophys J , vol.98 , Issue.5 , pp. 911-921
    • Celli, A.1    Sanchez, S.2    Behne, M.3    Hazlett, T.4    Gratton, E.5    Mauro, T.6
  • 40
    • 78649515383 scopus 로고    scopus 로고
    • Plakoglobin rescues adhesive defects induced by ectodomain truncation of the desmosomal cadherin desmoglein 1: Implications for exfoliative toxin-mediated skin blistering
    • Simpson CL, Kojima S-i, Cooper-Whitehair V, Getsios S, Green KJ. Plakoglobin rescues adhesive defects induced by ectodomain truncation of the desmosomal cadherin desmoglein 1: Implications for exfoliative toxin-mediated skin blistering. Am J Pathol 2010;177(6):2921-2937.
    • (2010) Am J Pathol , vol.177 , Issue.6 , pp. 2921-2937
    • Simpson, C.L.1    Kojima, S.-i.2    Cooper-Whitehair, V.3    Getsios, S.4    Green, K.J.5
  • 41
    • 84866087012 scopus 로고    scopus 로고
    • Plakoglobin-dependent regulation of keratinocyte apoptosis by Rnd3
    • Ryan KR, Lock FE, Heath JK, Hotchin NA. Plakoglobin-dependent regulation of keratinocyte apoptosis by Rnd3. J Cell Sci 2012;125(13):3202-3209.
    • (2012) J Cell Sci , vol.125 , Issue.13 , pp. 3202-3209
    • Ryan, K.R.1    Lock, F.E.2    Heath, J.K.3    Hotchin, N.A.4
  • 42
    • 79959685575 scopus 로고    scopus 로고
    • The role of Wnt in cell signaling and cell adhesion during early vertebrate development
    • Sylvie J, Ellen C, Kris V. The role of Wnt in cell signaling and cell adhesion during early vertebrate development. Front Biosci 2011;16:2352-2366.
    • (2011) Front Biosci , vol.16 , pp. 2352-2366
    • Sylvie, J.1    Ellen, C.2    Kris, V.3
  • 44
    • 84859739090 scopus 로고    scopus 로고
    • Plakoglobin: Role in tumorigenesis and metastasis
    • Aktary Z, Pasdar M. Plakoglobin: Role in tumorigenesis and metastasis. Int J Cell Biol 2012;2012:189521.
    • (2012) Int J Cell Biol , vol.2012 , pp. 189521
    • Aktary, Z.1    Pasdar, M.2
  • 45
    • 84856102438 scopus 로고    scopus 로고
    • Nuclear plakoglobin is essential for differentiation of cardiac progenitor cells to adipocytes in arrhythmogenic right ventricular cardiomyopathy
    • Lombardi R, da Graca Cabreira-Hansen M, Bell A, Fromm RR, Willerson JT, Marian AJ. Nuclear plakoglobin is essential for differentiation of cardiac progenitor cells to adipocytes in arrhythmogenic right ventricular cardiomyopathy. Circ Res 2011;109(12):1342-1353.
    • (2011) Circ Res , vol.109 , Issue.12 , pp. 1342-1353
    • Lombardi, R.1    da Graca Cabreira-Hansen, M.2    Bell, A.3    Fromm, R.R.4    Willerson, J.T.5    Marian, A.J.6
  • 46
    • 70349333829 scopus 로고    scopus 로고
    • Plakophilins: Multifunctional scaffolds for adhesion and signaling
    • Bass-Zubek AE, Godsel LM, Delmar M, Green KJ. Plakophilins: Multifunctional scaffolds for adhesion and signaling. Curr Opin Cell Biol 2009;21(5):708-716.
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.5 , pp. 708-716
    • Bass-Zubek, A.E.1    Godsel, L.M.2    Delmar, M.3    Green, K.J.4
  • 47
    • 77957931099 scopus 로고    scopus 로고
    • Plakophilin-1 localizes to the nucleus and interacts with single-stranded DNA
    • Sobolik-Delmaire T, Reddy R, Pashaj A, Roberts BJ, Wahl JK. Plakophilin-1 localizes to the nucleus and interacts with single-stranded DNA. J Invest Dermatol 2010;130(11):2638-2646.
    • (2010) J Invest Dermatol , vol.130 , Issue.11 , pp. 2638-2646
    • Sobolik-Delmaire, T.1    Reddy, R.2    Pashaj, A.3    Roberts, B.J.4    Wahl, J.K.5
  • 49
    • 84855945224 scopus 로고    scopus 로고
    • Desmoplakin regulates desmosome hyperadhesion
    • Hobbs RP, Green KJ. Desmoplakin regulates desmosome hyperadhesion. J Invest Dermatol 2012;132(2):482-485.
    • (2012) J Invest Dermatol , vol.132 , Issue.2 , pp. 482-485
    • Hobbs, R.P.1    Green, K.J.2
  • 50
    • 79958027310 scopus 로고    scopus 로고
    • Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain
    • Choi H-J, Weis WI. Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain. J Mol Biol 2011;409(5):800-812.
    • (2011) J Mol Biol , vol.409 , Issue.5 , pp. 800-812
    • Choi, H.-J.1    Weis, W.I.2
  • 52
    • 84871789319 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome system in the stabilization of cell-cell contacts in human keratinocytes
    • Löffek S, Bruckner-Tuderman L, Magin TM. Involvement of the ubiquitin-proteasome system in the stabilization of cell-cell contacts in human keratinocytes. Exp Dermatol 2012;21(10):791-793.
    • (2012) Exp Dermatol , vol.21 , Issue.10 , pp. 791-793
    • Löffek, S.1    Bruckner-Tuderman, L.2    Magin, T.M.3
  • 53
    • 84896910767 scopus 로고    scopus 로고
    • Desmosomes and desmosomal cadherin function in skin and heart diseases-Advancements in basic and clinical research
    • Mahoney MG, Muller EJ, Koch PJ. Desmosomes and desmosomal cadherin function in skin and heart diseases-Advancements in basic and clinical research. Dermatol Res Pract 2010; vol. 2010, Article ID 725647.
    • (2010) Dermatol Res Pract , vol.2010
    • Mahoney, M.G.1    Muller, E.J.2    Koch, P.J.3
  • 54
    • 84857871591 scopus 로고    scopus 로고
    • Desmoplakin controls microvilli length but not cell adhesion or keratin organization in the intestinal epithelium
    • Sumigray KD, Lechler T. Desmoplakin controls microvilli length but not cell adhesion or keratin organization in the intestinal epithelium. Mol Biol Cell 2012;23(5):792-799.
    • (2012) Mol Biol Cell , vol.23 , Issue.5 , pp. 792-799
    • Sumigray, K.D.1    Lechler, T.2
  • 55
    • 70849105396 scopus 로고    scopus 로고
    • KazrinE is a desmosome-associated liprin that colocalises with acetylated microtubules
    • Nachat R, Cipolat S, Sevilla LM, Chhatriwala M, Groot KR, Watt FM. KazrinE is a desmosome-associated liprin that colocalises with acetylated microtubules. J Cell Sci 2009;122(22):4035-4041.
    • (2009) J Cell Sci , vol.122 , Issue.22 , pp. 4035-4041
    • Nachat, R.1    Cipolat, S.2    Sevilla, L.M.3    Chhatriwala, M.4    Groot, K.R.5    Watt, F.M.6
  • 56
    • 84878537119 scopus 로고    scopus 로고
    • Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation
    • Kröger C, Loschke F, Schwarz N, Windoffer R, Leube RE, Magin TM. Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation. J Cell Biol 2013;201(5):681-692.
    • (2013) J Cell Biol , vol.201 , Issue.5 , pp. 681-692
    • Kröger, C.1    Loschke, F.2    Schwarz, N.3    Windoffer, R.4    Leube, R.E.5    Magin, T.M.6
  • 57
    • 84873731727 scopus 로고    scopus 로고
    • The expanding significance of keratin intermediate filaments in normal and diseased epithelia
    • Pan X, Hobbs RP, Coulombe PA. The expanding significance of keratin intermediate filaments in normal and diseased epithelia. Curr Opin Cell Biol 2013;25(1):47-56.
    • (2013) Curr Opin Cell Biol , vol.25 , Issue.1 , pp. 47-56
    • Pan, X.1    Hobbs, R.P.2    Coulombe, P.A.3
  • 60
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner B, Stevenson B, Grimaldi A. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J Cell Biol 1988;107(4):1575-1587.
    • (1988) J Cell Biol , vol.107 , Issue.4 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 61
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin V, Bauer C, Yin M, Fuchs E. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 2000;100(2):209-219.
    • (2000) Cell , vol.100 , Issue.2 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 62
    • 26444498679 scopus 로고    scopus 로고
    • A role for plakophilin-1 in the initiation of desmosome assembly
    • Wahl JK. A role for plakophilin-1 in the initiation of desmosome assembly. J Cell Biochem 2005;96(2):390-403.
    • (2005) J Cell Biochem , vol.96 , Issue.2 , pp. 390-403
    • Wahl, J.K.1
  • 63
    • 0028842803 scopus 로고
    • Continual assembly of half-desmosomal structures in the absence of cell contacts and their frustrated endocytosis: A coordinated Sisyphus cycle
    • Demlehner MP, Schäfer S, Grund C, Franke WW. Continual assembly of half-desmosomal structures in the absence of cell contacts and their frustrated endocytosis: A coordinated Sisyphus cycle. J Cell Biol 1995;131(3):745-760.
    • (1995) J Cell Biol , vol.131 , Issue.3 , pp. 745-760
    • Demlehner, M.P.1    Schäfer, S.2    Grund, C.3    Franke, W.W.4
  • 64
    • 79953717096 scopus 로고    scopus 로고
    • E-cadherin and plakoglobin recruit plakophilin3 to the cell border to initiate desmosome assembly
    • Gosavi P, Kundu S, Khapare N, Sehgal L, Karkhanis M, Dalal S. E-cadherin and plakoglobin recruit plakophilin3 to the cell border to initiate desmosome assembly. Cell Mol Life Sci 2011;68(8):1439-1454.
    • (2011) Cell Mol Life Sci , vol.68 , Issue.8 , pp. 1439-1454
    • Gosavi, P.1    Kundu, S.2    Khapare, N.3    Sehgal, L.4    Karkhanis, M.5    Dalal, S.6
  • 68
  • 69
    • 0033792693 scopus 로고    scopus 로고
    • Assembly pathway of desmoglein 3 to desmosomes and its perturbation by pemphigus vulgaris-IgG in cultured keratinocytes, as revealed by time-lapsed labeling immunoelectron microscopy
    • Sato M, Aoyama Y, Kitajima Y. Assembly pathway of desmoglein 3 to desmosomes and its perturbation by pemphigus vulgaris-IgG in cultured keratinocytes, as revealed by time-lapsed labeling immunoelectron microscopy. Lab Invest 2000;80(10):1583-1592.
    • (2000) Lab Invest , vol.80 , Issue.10 , pp. 1583-1592
    • Sato, M.1    Aoyama, Y.2    Kitajima, Y.3
  • 70
    • 84865293046 scopus 로고    scopus 로고
    • Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics
    • Tsang SM, Brown L, Gadmor H, Gammon L, Fortune F, Wheeler A, Wan H. Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics. Exp Cell Res 2012;318(18):2269-2283.
    • (2012) Exp Cell Res , vol.318 , Issue.18 , pp. 2269-2283
    • Tsang, S.M.1    Brown, L.2    Gadmor, H.3    Gammon, L.4    Fortune, F.5    Wheeler, A.6    Wan, H.7
  • 71
    • 0037089075 scopus 로고    scopus 로고
    • Desmosomes: interconnected calcium-dependent structures of remarkable stability with significant integral membrane protein turnover
    • Windoffer R, Borchert-Stuhltrager M, Leube RE. Desmosomes: interconnected calcium-dependent structures of remarkable stability with significant integral membrane protein turnover. J Cell Sci 2002;115(8):1717-1732.
    • (2002) J Cell Sci , vol.115 , Issue.8 , pp. 1717-1732
    • Windoffer, R.1    Borchert-Stuhltrager, M.2    Leube, R.E.3
  • 72
    • 42449098549 scopus 로고    scopus 로고
    • Hyper-adhesion: A new concept in cell-cell adhesion
    • Garrod D, Kimura TE. Hyper-adhesion: A new concept in cell-cell adhesion. Biochem Soc Trans 2008;36(Pt 2):195-201.
    • (2008) Biochem Soc Trans , vol.36 , pp. 195-201
    • Garrod, D.1    Kimura, T.E.2
  • 73
    • 33947191090 scopus 로고    scopus 로고
    • Calcium-independent desmosomes of keratinocytes are hyper-adhesive
    • Kimura TE, Merritt AJ, Garrod DR. Calcium-independent desmosomes of keratinocytes are hyper-adhesive. J Invest Dermatol 2007;127(4):775-781.
    • (2007) J Invest Dermatol , vol.127 , Issue.4 , pp. 775-781
    • Kimura, T.E.1    Merritt, A.J.2    Garrod, D.R.3
  • 74
    • 0034020357 scopus 로고    scopus 로고
    • The alpha isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells
    • Wallis S, Lloyd S, Wise I, Ireland G, Fleming TP, Garrod D. The alpha isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells. Mol Biol Cell 2000;11(3):1077-1092.
    • (2000) Mol Biol Cell , vol.11 , Issue.3 , pp. 1077-1092
    • Wallis, S.1    Lloyd, S.2    Wise, I.3    Ireland, G.4    Fleming, T.P.5    Garrod, D.6
  • 75
    • 30544454786 scopus 로고    scopus 로고
    • Hyper-adhesion in desmosomes: Its regulation in wound healing and possible relationship to cadherin crystal structure
    • Garrod DR, Berika MY, Bardsley WF, Holmes D, Tabernero L. Hyper-adhesion in desmosomes: Its regulation in wound healing and possible relationship to cadherin crystal structure. J Cell Sci 2005;118(Pt 24):5743-5754.
    • (2005) J Cell Sci , vol.118 , pp. 5743-5754
    • Garrod, D.R.1    Berika, M.Y.2    Bardsley, W.F.3    Holmes, D.4    Tabernero, L.5
  • 76
    • 84907980342 scopus 로고    scopus 로고
    • Regulation and impairments of dynamic desmosome and corneodesmosome remodeling
    • Apr 30 [Epub ahead of print] in PubMED.
    • Kitajima Y. Regulation and impairments of dynamic desmosome and corneodesmosome remodeling. Eur J Dermatol 2013 Apr 30 [Epub ahead of print] in PubMED.
    • (2013) Eur J Dermatol
    • Kitajima, Y.1
  • 77
    • 0032900965 scopus 로고    scopus 로고
    • Pemphigus vulgaris-IgG causes a rapid depletion of desmoglein 3 (Dsg3) from the Triton X-100 soluble pools, leading to the formation of Dsg3-depleted desmosomes in a human squamous carcinoma cell line, DJM-1 cells
    • Aoyama Y, Kitajima Y. Pemphigus vulgaris-IgG causes a rapid depletion of desmoglein 3 (Dsg3) from the Triton X-100 soluble pools, leading to the formation of Dsg3-depleted desmosomes in a human squamous carcinoma cell line, DJM-1 cells. J Invest Dermatol 1999;112(1):67-71.
    • (1999) J Invest Dermatol , vol.112 , Issue.1 , pp. 67-71
    • Aoyama, Y.1    Kitajima, Y.2
  • 80
    • 44449118711 scopus 로고    scopus 로고
    • E-cadherin is an additional immunological target for pemphigus autoantibodies
    • Evangelista F, Dasher DA, Diaz LA, Prisayanh PS, Li N. E-cadherin is an additional immunological target for pemphigus autoantibodies. J Invest Dermatol 2008;128(7):1710-1718.
    • (2008) J Invest Dermatol , vol.128 , Issue.7 , pp. 1710-1718
    • Evangelista, F.1    Dasher, D.A.2    Diaz, L.A.3    Prisayanh, P.S.4    Li, N.5
  • 81
    • 0028948197 scopus 로고
    • Intracellular domain of desmoglein 3 (pemphigus vulgaris antigen) confers adhesive function on the extracellular domain of E-cadherin without binding catenins
    • Roh JY, Stanley JR. Intracellular domain of desmoglein 3 (pemphigus vulgaris antigen) confers adhesive function on the extracellular domain of E-cadherin without binding catenins. J Cell Biol 1995;128(5):939-947.
    • (1995) J Cell Biol , vol.128 , Issue.5 , pp. 939-947
    • Roh, J.Y.1    Stanley, J.R.2
  • 83
  • 87
    • 79959703249 scopus 로고    scopus 로고
    • RNAi-mediated inhibition of the desmosomal cadherin (desmoglein 3) impairs epithelial cell proliferation
    • Mannan T, Jing S, Foroushania SH, Fortune F, Wan H. RNAi-mediated inhibition of the desmosomal cadherin (desmoglein 3) impairs epithelial cell proliferation. Cell Prolif 2011;44(4):301-310.
    • (2011) Cell Prolif , vol.44 , Issue.4 , pp. 301-310
    • Mannan, T.1    Jing, S.2    Foroushania, S.H.3    Fortune, F.4    Wan, H.5
  • 88
    • 79954610504 scopus 로고    scopus 로고
    • Loss of desmocollin-2 confers a tumorigenic phenotype to colonic epithelial cells through activation of Akt/{beta}-catenin signaling
    • Kolegraff K, Nava P, Helms MN, Parkos CA, Nusrat A. Loss of desmocollin-2 confers a tumorigenic phenotype to colonic epithelial cells through activation of Akt/{beta}-catenin signaling. Mol Biol Cell 2011;22(8):1121-1134.
    • (2011) Mol Biol Cell , vol.22 , Issue.8 , pp. 1121-1134
    • Kolegraff, K.1    Nava, P.2    Helms, M.N.3    Parkos, C.A.4    Nusrat, A.5
  • 90
    • 79951840005 scopus 로고    scopus 로고
    • IgG autoantibodies against desmocollin 3 in pemphigus sera induce loss of keratinocyte adhesion
    • Rafei D, Müller R, Ishii N, Llamazares M, Hashimoto T, Hertl M, Eming R. IgG autoantibodies against desmocollin 3 in pemphigus sera induce loss of keratinocyte adhesion. Am J Pathol 2011;178(2):718-723.
    • (2011) Am J Pathol , vol.178 , Issue.2 , pp. 718-723
    • Rafei, D.1    Müller, R.2    Ishii, N.3    Llamazares, M.4    Hashimoto, T.5    Hertl, M.6    Eming, R.7
  • 92
    • 84856457013 scopus 로고    scopus 로고
    • Pemphigus autoimmunity: Hypotheses and realities
    • Grando S. Pemphigus autoimmunity: Hypotheses and realities. Autoimmunity 2012;45(1):7-35.
    • (2012) Autoimmunity , vol.45 , Issue.1 , pp. 7-35
    • Grando, S.1
  • 94
    • 78651396165 scopus 로고    scopus 로고
    • p38 MAPK activation is downstream of the loss of intercellular adhesion in pemphigus vulgaris
    • Mao X, Sano Y, Park JM, Payne AS. p38 MAPK activation is downstream of the loss of intercellular adhesion in pemphigus vulgaris. J Biol Chem 2011;286(2):1283-1291.
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1283-1291
    • Mao, X.1    Sano, Y.2    Park, J.M.3    Payne, A.S.4
  • 95
    • 84890970477 scopus 로고    scopus 로고
    • MAPKAP kinase 2 (MK2)-dependent and -independent models of blister formation in pemphigus vulgaris
    • Mao X, Li H, Sano Y, Gaestel M, Mo Park J, Payne AS. MAPKAP kinase 2 (MK2)-dependent and -independent models of blister formation in pemphigus vulgaris. J Invest Dermatol 2013;134:68-76.
    • (2013) J Invest Dermatol , vol.134 , pp. 68-76
    • Mao, X.1    Li, H.2    Sano, Y.3    Gaestel, M.4    Mo Park, J.5    Payne, A.S.6
  • 97
    • 60749113371 scopus 로고    scopus 로고
    • Desmosome splitting is a primary ultrastructural change in the acantholysis of pemphigus
    • Wang W, Amagai M, Ishiko A. Desmosome splitting is a primary ultrastructural change in the acantholysis of pemphigus. J Dermatol Sci 2008;54:59-61.
    • (2008) J Dermatol Sci , vol.54 , pp. 59-61
    • Wang, W.1    Amagai, M.2    Ishiko, A.3
  • 98
    • 78049440518 scopus 로고    scopus 로고
    • Homologous regions of autoantibody heavy chain complementarity-determining region 3 (H-CDR3) in patients with pemphigus cause pathogenicity
    • Yamagami J, Payne AS, Kacir S, Ishii K, Siegel DL, Stanley JR. Homologous regions of autoantibody heavy chain complementarity-determining region 3 (H-CDR3) in patients with pemphigus cause pathogenicity. J Clin Invest 2010;120(11):4111-4117.
    • (2010) J Clin Invest , vol.120 , Issue.11 , pp. 4111-4117
    • Yamagami, J.1    Payne, A.S.2    Kacir, S.3    Ishii, K.4    Siegel, D.L.5    Stanley, J.R.6
  • 99
    • 70349744007 scopus 로고    scopus 로고
    • Pathogenic epitopes of autoantibodies in pemphigus reside in the amino-terminal adhesive region of desmogleins which are unmasked by proteolytic processing of prosequence
    • Yokouchi M, Saleh MA, Kuroda K, Hachiya T, Stanley JR, Amagai M, Ishii K. Pathogenic epitopes of autoantibodies in pemphigus reside in the amino-terminal adhesive region of desmogleins which are unmasked by proteolytic processing of prosequence. J Invest Dermatol 2009;129:2156-2166.
    • (2009) J Invest Dermatol , vol.129 , pp. 2156-2166
    • Yokouchi, M.1    Saleh, M.A.2    Kuroda, K.3    Hachiya, T.4    Stanley, J.R.5    Amagai, M.6    Ishii, K.7
  • 100
    • 0037442123 scopus 로고    scopus 로고
    • Induction of pemphigus phenotype by a mouse monoclonal antibody against the amino-terminal adhesive interface of desmoglein 3
    • Tsunoda K, Ota T, Aoki M, Yamada T, Nagai T, Nakagawa T, Koyasu S, Nishikawa T, Amagai M. Induction of pemphigus phenotype by a mouse monoclonal antibody against the amino-terminal adhesive interface of desmoglein 3. J Immunol 2003;170(4):2170-2178.
    • (2003) J Immunol , vol.170 , Issue.4 , pp. 2170-2178
    • Tsunoda, K.1    Ota, T.2    Aoki, M.3    Yamada, T.4    Nagai, T.5    Nakagawa, T.6    Koyasu, S.7    Nishikawa, T.8    Amagai, M.9
  • 101
    • 67649846396 scopus 로고    scopus 로고
    • Peptides targeting the desmoglein 3 adhesive interface prevent autoantibody-induced acantholysis in pemphigus
    • Heupel W-M, Müller T, Efthymiadis A, Schmidt E, Drenckhahn D, Waschke J. Peptides targeting the desmoglein 3 adhesive interface prevent autoantibody-induced acantholysis in pemphigus. J Biol Chem 2009;284(13):8589-8595.
    • (2009) J Biol Chem , vol.284 , Issue.13 , pp. 8589-8595
    • Heupel, W.-M.1    Müller, T.2    Efthymiadis, A.3    Schmidt, E.4    Drenckhahn, D.5    Waschke, J.6
  • 103
    • 77953585901 scopus 로고    scopus 로고
    • From cell signaling to novel therapeutic concepts: International pemphigus meeting on advances in pemphigus research and therapy
    • Getsios S, Waschke J, Borradori L, Hertl M, Muller EJ. From cell signaling to novel therapeutic concepts: International pemphigus meeting on advances in pemphigus research and therapy. J Invest Dermatol 2010;130(7):1764-1768.
    • (2010) J Invest Dermatol , vol.130 , Issue.7 , pp. 1764-1768
    • Getsios, S.1    Waschke, J.2    Borradori, L.3    Hertl, M.4    Muller, E.J.5
  • 104
    • 21244476854 scopus 로고    scopus 로고
    • Desmosome signaling. Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization
    • Berkowitz P, Hu P, Liu Z, Diaz LA, Enghild JJ, Chua MP, Rubenstein DS. Desmosome signaling. Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization. J Biol Chem 2005;280(25):23778-23784.
    • (2005) J Biol Chem , vol.280 , Issue.25 , pp. 23778-23784
    • Berkowitz, P.1    Hu, P.2    Liu, Z.3    Diaz, L.A.4    Enghild, J.J.5    Chua, M.P.6    Rubenstein, D.S.7
  • 105
    • 33751098790 scopus 로고    scopus 로고
    • Pathogenic monoclonal antibody against desmoglein 3 augments desmoglein 3 and p38 MAPK phosphorylation in human squamous carcinoma cell line
    • Kawasaki Y, Aoyama Y, Tsunoda K, Amagai M, Kitajima Y. Pathogenic monoclonal antibody against desmoglein 3 augments desmoglein 3 and p38 MAPK phosphorylation in human squamous carcinoma cell line. Autoimmunity 2006;39(7):587-590.
    • (2006) Autoimmunity , vol.39 , Issue.7 , pp. 587-590
    • Kawasaki, Y.1    Aoyama, Y.2    Tsunoda, K.3    Amagai, M.4    Kitajima, Y.5
  • 106
    • 66449087840 scopus 로고    scopus 로고
    • Biphasic activation of p38MAPK suggests that apoptosis is a downstream event in pemphigus acantholysis
    • Lee HE, Berkowitz P, Jolly PS, Diaz LA, Chua MP, Rubenstein DS. Biphasic activation of p38MAPK suggests that apoptosis is a downstream event in pemphigus acantholysis. J Biol Chem 2009;284(18):12524-12532.
    • (2009) J Biol Chem , vol.284 , Issue.18 , pp. 12524-12532
    • Lee, H.E.1    Berkowitz, P.2    Jolly, P.S.3    Diaz, L.A.4    Chua, M.P.5    Rubenstein, D.S.6
  • 108
    • 57149087666 scopus 로고    scopus 로고
    • Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin
    • Berkowitz P, Chua M, Liu Z, Diaz LA, Rubenstein DS. Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin. Am J Pathol 2008;173(6):1628-1636.
    • (2008) Am J Pathol , vol.173 , Issue.6 , pp. 1628-1636
    • Berkowitz, P.1    Chua, M.2    Liu, Z.3    Diaz, L.A.4    Rubenstein, D.S.5
  • 109
    • 39149110925 scopus 로고    scopus 로고
    • Induction of p38MAPK and HSP27 phosphorylation in pemphigus patient skin
    • Berkowitz P, Diaz LA, Hall RP, Rubenstein DS. Induction of p38MAPK and HSP27 phosphorylation in pemphigus patient skin. J Invest Dermatol 2007;128(3):738-740.
    • (2007) J Invest Dermatol , vol.128 , Issue.3 , pp. 738-740
    • Berkowitz, P.1    Diaz, L.A.2    Hall, R.P.3    Rubenstein, D.S.4
  • 110
    • 63149188134 scopus 로고    scopus 로고
    • Disruption of desmosome assembly by monovalent human pemphigus vulgaris monoclonal antibodies
    • Mao X, Choi EJ, Payne AS. Disruption of desmosome assembly by monovalent human pemphigus vulgaris monoclonal antibodies. J Invest Dermatol 2009;129(4):908-918.
    • (2009) J Invest Dermatol , vol.129 , Issue.4 , pp. 908-918
    • Mao, X.1    Choi, E.J.2    Payne, A.S.3
  • 111
    • 84875969766 scopus 로고    scopus 로고
    • A pathophysiologic role for epidermal growth factor receptor in pemphigus acantholysis
    • Bektas M, Jolly PS, Berkowitz P, Amagai M, Rubenstein DS. A pathophysiologic role for epidermal growth factor receptor in pemphigus acantholysis. J Biol Chem 2013;288(13):9447-9456.
    • (2013) J Biol Chem , vol.288 , Issue.13 , pp. 9447-9456
    • Bektas, M.1    Jolly, P.S.2    Berkowitz, P.3    Amagai, M.4    Rubenstein, D.S.5
  • 112
    • 78650630568 scopus 로고    scopus 로고
    • Protective endogenous cyclic adenosine 5'-monophosphate signaling triggered by pemphigus autoantibodies
    • Spindler V, Vielmuth F, Schmidt E, Rubenstein DS, Waschke J. Protective endogenous cyclic adenosine 5'-monophosphate signaling triggered by pemphigus autoantibodies. J Immunol 2010;185(11):6831-6838.
    • (2010) J Immunol , vol.185 , Issue.11 , pp. 6831-6838
    • Spindler, V.1    Vielmuth, F.2    Schmidt, E.3    Rubenstein, D.S.4    Waschke, J.5
  • 114
    • 84865293046 scopus 로고    scopus 로고
    • Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics
    • Man
    • Man Tsang S, Brown L, Gadmor H, Gammon L, Fortune F, Wheeler A, Wan H. Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics. Exp Cell Res 2012;318(18):2269-2283.
    • (2012) Exp Cell Res , vol.318 , Issue.18 , pp. 2269-2283
    • Tsang, S.1    Brown, L.2    Gadmor, H.3    Gammon, L.4    Fortune, F.5    Wheeler, A.6    Wan, H.7
  • 115
    • 49649095012 scopus 로고    scopus 로고
    • Pemphigus vulgaris IgG-induced desmoglein-3 endocytosis and desmosomal disassembly are mediated by a clathrin- and dynamin-independent mechanism
    • Delva E, Jennings JM, Calkins CC, Kottke MD, Faundez V, Kowalczyk AP. Pemphigus vulgaris IgG-induced desmoglein-3 endocytosis and desmosomal disassembly are mediated by a clathrin- and dynamin-independent mechanism. J Biol Chem 2008;283(26):18303-18313.
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 18303-18313
    • Delva, E.1    Jennings, J.M.2    Calkins, C.C.3    Kottke, M.D.4    Faundez, V.5    Kowalczyk, A.P.6
  • 116
    • 79951518111 scopus 로고    scopus 로고
    • Desmosome disassembly in response to pemphigus vulgaris IgG occurs in distinct phases and can be reversed by expression of exogenous Dsg3
    • Jennings JM, Tucker DK, Kottke MD, Saito M, Delva E, Hanakawa Y, Amagai M, Kowalczyk AP. Desmosome disassembly in response to pemphigus vulgaris IgG occurs in distinct phases and can be reversed by expression of exogenous Dsg3. J Invest Dermatol 2011;131(3):706-718.
    • (2011) J Invest Dermatol , vol.131 , Issue.3 , pp. 706-718
    • Jennings, J.M.1    Tucker, D.K.2    Kottke, M.D.3    Saito, M.4    Delva, E.5    Hanakawa, Y.6    Amagai, M.7    Kowalczyk, A.P.8
  • 117
    • 67449150190 scopus 로고    scopus 로고
    • Loss of the desmosomal protein perp enhances the phenotypic effects of pemphigus vulgaris autoantibodies
    • Nguyen B, Dusek RL, Beaudry VG, Marinkovich MP, Attardi LD. Loss of the desmosomal protein perp enhances the phenotypic effects of pemphigus vulgaris autoantibodies. J Invest Dermatol 2009;129(7):1710-1718.
    • (2009) J Invest Dermatol , vol.129 , Issue.7 , pp. 1710-1718
    • Nguyen, B.1    Dusek, R.L.2    Beaudry, V.G.3    Marinkovich, M.P.4    Attardi, L.D.5
  • 118
    • 80052249651 scopus 로고    scopus 로고
    • IgG-induced clustering of desmogleins 1 and 3 in skin of patients with pemphigus fits with the desmoglein nonassembly depletion hypothesis
    • Oktarina DAM, van der Wier G, Diercks GFH, Jonkman MF, Pas HH. IgG-induced clustering of desmogleins 1 and 3 in skin of patients with pemphigus fits with the desmoglein nonassembly depletion hypothesis. Br J Dermatol 2011;165(3):552-562.
    • (2011) Br J Dermatol , vol.165 , Issue.3 , pp. 552-562
    • Oktarina, D.A.M.1    van der Wier, G.2    Diercks, G.F.H.3    Jonkman, M.F.4    Pas, H.H.5
  • 119
    • 77951243214 scopus 로고    scopus 로고
    • Binding of pemphigus vulgaris IgG to antigens in desmosome core domains excludes immune complexes rather than directly splitting desmosomes
    • Aoyama Y, Nagai M, Kitajima Y. Binding of pemphigus vulgaris IgG to antigens in desmosome core domains excludes immune complexes rather than directly splitting desmosomes. Br J Dermatol 2010;162(5):1049-1055.
    • (2010) Br J Dermatol , vol.162 , Issue.5 , pp. 1049-1055
    • Aoyama, Y.1    Nagai, M.2    Kitajima, Y.3
  • 120
    • 84871280700 scopus 로고    scopus 로고
    • New insights into desmosome regulation and pemphigus blistering as a desmosome-remodeling disease
    • Kitajima Y. New insights into desmosome regulation and pemphigus blistering as a desmosome-remodeling disease. Kaohsiung J Med Sci 2013;29(1):1-13.
    • (2013) Kaohsiung J Med Sci , vol.29 , Issue.1 , pp. 1-13
    • Kitajima, Y.1
  • 121
    • 77449142413 scopus 로고    scopus 로고
    • Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC
    • Cirillo N, Lanza A, Prime SS. Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC. Exp Cell Res 2010;316(4):580-592.
    • (2010) Exp Cell Res , vol.316 , Issue.4 , pp. 580-592
    • Cirillo, N.1    Lanza, A.2    Prime, S.S.3
  • 122
    • 80053332932 scopus 로고    scopus 로고
    • The extent of desmoglein 3 depletion in pemphigus vulgaris is dependent on Ca(2+)-induced differentiation: A role in suprabasal epidermal skin splitting
    • Spindler V, Endlich A, Hartlieb E, Vielmuth F, Schmidt E, Waschke J. The extent of desmoglein 3 depletion in pemphigus vulgaris is dependent on Ca(2+)-induced differentiation: A role in suprabasal epidermal skin splitting? Am J Pathol 2011;179(4):1905-1916.
    • (2011) Am J Pathol , vol.179 , Issue.4 , pp. 1905-1916
    • Spindler, V.1    Endlich, A.2    Hartlieb, E.3    Vielmuth, F.4    Schmidt, E.5    Waschke, J.6
  • 123
    • 44449092953 scopus 로고    scopus 로고
    • The desmosome and pemphigus
    • Waschke J. The desmosome and pemphigus. Histochem Cell Biol 2008;130(1):21-54.
    • (2008) Histochem Cell Biol , vol.130 , Issue.1 , pp. 21-54
    • Waschke, J.1
  • 125
    • 33751085125 scopus 로고    scopus 로고
    • Apoptotic mechanism in pemphigus autoimmunoglobulins-induced acantholysis-Possible involvement of the EGF receptor
    • Frusic-Zlotkin M, Raichenberg D, Wang X, David M, Michel B, Milner Y. Apoptotic mechanism in pemphigus autoimmunoglobulins-induced acantholysis-Possible involvement of the EGF receptor. Autoimmunity 2006;39(7):563-575.
    • (2006) Autoimmunity , vol.39 , Issue.7 , pp. 563-575
    • Frusic-Zlotkin, M.1    Raichenberg, D.2    Wang, X.3    David, M.4    Michel, B.5    Milner, Y.6
  • 126
    • 34250354415 scopus 로고    scopus 로고
    • Desmoglein versus non-desmoglein signaling in pemphigus acantholysis: Characterization of novel signaling pathways downstream of pemphigus vulgaris antigens
    • Chernyavsky AI, Arredondo J, Kitajima Y, Sato-Nagai M, Grando SA. Desmoglein versus non-desmoglein signaling in pemphigus acantholysis: Characterization of novel signaling pathways downstream of pemphigus vulgaris antigens. J Biol Chem 2007;282(18):13804-13812.
    • (2007) J Biol Chem , vol.282 , Issue.18 , pp. 13804-13812
    • Chernyavsky, A.I.1    Arredondo, J.2    Kitajima, Y.3    Sato-Nagai, M.4    Grando, S.A.5
  • 127
    • 79957538229 scopus 로고    scopus 로고
    • Transgenic rescue of desmoglein 3 null mice with desmoglein 1 to develop a syngeneic mouse model for pemphigus vulgaris
    • Hata T, Nishifuji K, Shimoda K, Sasaki T, Yamada T, Nishikawa T, Koyasu S, Amagai M. Transgenic rescue of desmoglein 3 null mice with desmoglein 1 to develop a syngeneic mouse model for pemphigus vulgaris. J Dermatol Sci 2011;63(1):33-39.
    • (2011) J Dermatol Sci , vol.63 , Issue.1 , pp. 33-39
    • Hata, T.1    Nishifuji, K.2    Shimoda, K.3    Sasaki, T.4    Yamada, T.5    Nishikawa, T.6    Koyasu, S.7    Amagai, M.8
  • 128
    • 69149097139 scopus 로고    scopus 로고
    • An imbalance in Akt/mTOR is involved in the apoptotic and acantholytic processes in a mouse model of pemphigus vulgaris
    • Pretel M, España A, Marquina M, Beatriz Pelacho, López-Picazo J, López-Zabalza J. An imbalance in Akt/mTOR is involved in the apoptotic and acantholytic processes in a mouse model of pemphigus vulgaris. Exp Dermatol 2009;18(9):771-780.
    • (2009) Exp Dermatol , vol.18 , Issue.9 , pp. 771-780
    • Pretel, M.1    España, A.2    Marquina, M.3    Beatriz, P.4    López-Picazo, J.5    López-Zabalza, J.6
  • 129
    • 84858451814 scopus 로고    scopus 로고
    • Inhibition of FAK prevents blister formation in the neonatal mouse model of pemphigus vulgaris
    • Gil MP, Modol T, España A, López-Zabalza MJ. Inhibition of FAK prevents blister formation in the neonatal mouse model of pemphigus vulgaris. Exp Dermatol 2012;21(4):254-259.
    • (2012) Exp Dermatol , vol.21 , Issue.4 , pp. 254-259
    • Gil, M.P.1    Modol, T.2    España, A.3    López-Zabalza, M.J.4
  • 130
    • 84873183133 scopus 로고    scopus 로고
    • Neural nitric oxide synthase participates in pemphigus vulgaris acantholysis through upregulation of Rous sarcoma, mammalian target of rapamycin and focal adhesion kinase
    • España A, Mòdol T, Gil MP, López-Zabalza MJ. Neural nitric oxide synthase participates in pemphigus vulgaris acantholysis through upregulation of Rous sarcoma, mammalian target of rapamycin and focal adhesion kinase. Exp Dermatol 2013;22(2):125-130.
    • (2013) Exp Dermatol , vol.22 , Issue.2 , pp. 125-130
    • España, A.1    Mòdol, T.2    Gil, M.P.3    López-Zabalza, M.J.4
  • 132
    • 67349196440 scopus 로고    scopus 로고
    • Apoptosis in pemphigus
    • Schmidt E, Waschke J. Apoptosis in pemphigus. Autoimmun Rev 2009;8(7):533-537.
    • (2009) Autoimmun Rev , vol.8 , Issue.7 , pp. 533-537
    • Schmidt, E.1    Waschke, J.2
  • 134
    • 51949092571 scopus 로고    scopus 로고
    • Cleavage of desmoglein 3 can explain its depletion from keratinocytes in pemphigus vulgaris
    • Cirillo N, Campisi G, Gombos F, Perillo L, Femiano F, Lanza A. Cleavage of desmoglein 3 can explain its depletion from keratinocytes in pemphigus vulgaris. Exp Dermatol 2008;17(10):858-863.
    • (2008) Exp Dermatol , vol.17 , Issue.10 , pp. 858-863
    • Cirillo, N.1    Campisi, G.2    Gombos, F.3    Perillo, L.4    Femiano, F.5    Lanza, A.6
  • 135
    • 59849099433 scopus 로고    scopus 로고
    • Involvement of the apoptotic mechanism in pemphigus foliaceus autoimmune injury of the skin
    • Li N, Zhao M, Wang J, Liu Z, Diaz LA. Involvement of the apoptotic mechanism in pemphigus foliaceus autoimmune injury of the skin. J Immunol 2009;182(1):711-717.
    • (2009) J Immunol , vol.182 , Issue.1 , pp. 711-717
    • Li, N.1    Zhao, M.2    Wang, J.3    Liu, Z.4    Diaz, L.A.5
  • 136
    • 59649096544 scopus 로고    scopus 로고
    • Pemphigus vulgaris IgG cause loss of desmoglein-mediated adhesion and keratinocyte dissociation independent of epidermal growth factor receptor
    • Heupel W-M, Engerer P, Schmidt E, Waschke J. Pemphigus vulgaris IgG cause loss of desmoglein-mediated adhesion and keratinocyte dissociation independent of epidermal growth factor receptor. Am J Pathol 2009;174(2):475-485.
    • (2009) Am J Pathol , vol.174 , Issue.2 , pp. 475-485
    • Heupel, W.-M.1    Engerer, P.2    Schmidt, E.3    Waschke, J.4
  • 137
    • 78651396165 scopus 로고    scopus 로고
    • p38 MAPK activation is downstream of the loss of intercellular adhesion in pemphigus vulgaris
    • Mao X, Sano Y, Park JM, Payne AS. p38 MAPK activation is downstream of the loss of intercellular adhesion in pemphigus vulgaris. J Biol Chem 2011;286(2):1283-1291.
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1283-1291
    • Mao, X.1    Sano, Y.2    Park, J.M.3    Payne, A.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.