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Volumn 128, Issue 6, 2011, Pages

Polyinosinic:polycytidylic acid induces protein kinase D-dependent disassembly of apical junctions and barrier dysfunction in airway epithelial cells

Author keywords

adherens junctions; Asthma; epithelial permeability; polyI:C; protein kinase C; tight junctions; Toll like receptor 3

Indexed keywords

1 (5 IODO 1 NAPHTHALENESULFONYL)HEXAHYDRO 1H 1,4 DIAZEPINE; 4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; BETA CATENIN; BLEBBISTATIN; DOUBLE STRANDED RNA; OCCLUDIN; POLYINOSINIC POLYCYTIDYLIC ACID; PROTEIN KINASE D; PROTEIN ZO1; UVOMORULIN;

EID: 82555205301     PISSN: 00916749     EISSN: 10976825     Source Type: Journal    
DOI: 10.1016/j.jaci.2011.08.035     Document Type: Article
Times cited : (79)

References (63)
  • 2
    • 39849088124 scopus 로고    scopus 로고
    • Molecular components of the adherens junction
    • C.M. Niessen, and C.J. Gottardi Molecular components of the adherens junction Biochim Biophys Acta 1778 2008 562 571
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 562-571
    • Niessen, C.M.1    Gottardi, C.J.2
  • 5
    • 35348841509 scopus 로고    scopus 로고
    • Tight junctions/adherens junctions: Basic structure and function
    • DOI 10.1038/sj.jid.5700865, PII 5700865
    • C.M. Niessen Tight junctions/adherens junctions: basic structure and function J Invest Dermatol 127 2007 2525 2532 (Pubitemid 47585053)
    • (2007) Journal of Investigative Dermatology , vol.127 , Issue.11 , pp. 2525-2532
    • Niessen, C.M.1
  • 6
    • 67249085206 scopus 로고    scopus 로고
    • Tight junctions: Molecular structure meets function
    • J.D. Schulzke, and M. Fromm Tight junctions: molecular structure meets function Ann N Y Acad Sci 1165 2009 1 6
    • (2009) Ann N y Acad Sci , vol.1165 , pp. 1-6
    • Schulzke, J.D.1    Fromm, M.2
  • 7
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • C.M. Van Itallie, A.S. Fanning, A. Bridges, and J.M. Anderson ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton Mol Biol Cell 20 2009 3930 3940
    • (2009) Mol Biol Cell , vol.20 , pp. 3930-3940
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 8
    • 77149179101 scopus 로고    scopus 로고
    • Adherens junction: Molecular architecture and regulation
    • W. Meng, and M. Takeichi Adherens junction: molecular architecture and regulation Cold Spring Harb Perspect Biol 1 2009 a002899
    • (2009) Cold Spring Harb Perspect Biol , vol.1 , pp. 002899
    • Meng, W.1    Takeichi, M.2
  • 9
    • 52049116495 scopus 로고    scopus 로고
    • Actin motors that drive formation and disassembly of epithelial apical junctions
    • A.I. Ivanov Actin motors that drive formation and disassembly of epithelial apical junctions Front Biosci 13 2008 6662 6681
    • (2008) Front Biosci , vol.13 , pp. 6662-6681
    • Ivanov, A.I.1
  • 10
    • 36849031788 scopus 로고    scopus 로고
    • Epithelium dysfunction in asthma
    • S.T. Holgate Epithelium dysfunction in asthma J Allergy Clin Immunol 120 2007 1233 1246
    • (2007) J Allergy Clin Immunol , vol.120 , pp. 1233-1246
    • Holgate, S.T.1
  • 14
    • 34250159407 scopus 로고    scopus 로고
    • Down-regulation of E-cadherin in human bronchial epithelial cells leads to epidermal growth factor receptor-dependent Th2 cell-promoting activity
    • I.H. Heijink, P.M. Kies, H.F. Kauffman, D.S. Postma, A.J. van Oosterhout, and E. Vellenga Down-regulation of E-cadherin in human bronchial epithelial cells leads to epidermal growth factor receptor-dependent Th2 cell-promoting activity J Immunol 178 2007 7678 7685 (Pubitemid 46898038)
    • (2007) Journal of Immunology , vol.178 , Issue.12 , pp. 7678-7685
    • Heijink, I.H.1    Kies, P.M.2    Kauffman, H.F.3    Postma, D.S.4    Van Oosterhout, A.J.M.5    Vellenga, E.6
  • 17
    • 33645734929 scopus 로고    scopus 로고
    • Toll-dependent selection of microbial antigens for presentation by dendritic cells
    • J.M. Blander, and R. Medzhitov Toll-dependent selection of microbial antigens for presentation by dendritic cells Nature 440 2006 808 812
    • (2006) Nature , vol.440 , pp. 808-812
    • Blander, J.M.1    Medzhitov, R.2
  • 18
    • 67650445798 scopus 로고    scopus 로고
    • Dendritic cells require a systemic type i interferon response to mature and induce CD4+ Th1 immunity with poly IC as adjuvant
    • M.P. Longhi, C. Trumpfheller, J. Idoyaga, M. Caskey, I. Matos, and C. Kluger Dendritic cells require a systemic type I interferon response to mature and induce CD4+ Th1 immunity with poly IC as adjuvant J Exp Med 206 2009 1589 1602
    • (2009) J Exp Med , vol.206 , pp. 1589-1602
    • Longhi, M.P.1    Trumpfheller, C.2    Idoyaga, J.3    Caskey, M.4    Matos, I.5    Kluger, C.6
  • 19
    • 84868547474 scopus 로고    scopus 로고
    • Synthetic double-stranded RNAs are adjuvants for the induction of T helper 1 and humoral immune responses to human papillomavirus in rhesus macaques
    • C. Stahl-Hennig, M. Eisenblatter, E. Jasny, T. Rzehak, K. Tenner-Racz, and C. Trumpfheller Synthetic double-stranded RNAs are adjuvants for the induction of T helper 1 and humoral immune responses to human papillomavirus in rhesus macaques PLoS Pathog 5 2009 e1000373
    • (2009) PLoS Pathog , vol.5 , pp. 1000373
    • Stahl-Hennig, C.1    Eisenblatter, M.2    Jasny, E.3    Rzehak, T.4    Tenner-Racz, K.5    Trumpfheller, C.6
  • 21
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • DOI 10.1126/science.1155406
    • L. Liu, I. Botos, Y. Wang, J.N. Leonard, J. Shiloach, and D.M. Segal Structural basis of toll-like receptor 3 signaling with double-stranded RNA Science 320 2008 379 381 (Pubitemid 351555661)
    • (2008) Science , vol.320 , Issue.5874 , pp. 379-381
    • Liu, L.1    Botos, I.2    Wang, Y.3    Leonard, J.N.4    Shiloach, J.5    Segal, D.M.6    Davies, D.R.7
  • 22
    • 23044445303 scopus 로고    scopus 로고
    • Structural biology: Crystal structure of human toll-like receptor 3 (TLR3) ectodomain
    • DOI 10.1126/science.1115253
    • J. Choe, M.S. Kelker, and I.A. Wilson Crystal structure of human toll-like receptor 3 (TLR3) ectodomain Science 309 2005 581 585 (Pubitemid 41033635)
    • (2005) Science , vol.309 , Issue.5734 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 25
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • W. Zeng, L. Sun, X. Jiang, X. Chen, F. Hou, and A. Adhikari Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity Cell 141 2010 315 330
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1    Sun, L.2    Jiang, X.3    Chen, X.4    Hou, F.5    Adhikari, A.6
  • 26
  • 27
    • 52049095466 scopus 로고    scopus 로고
    • Mechanisms of intestinal tight junctional disruption during infection
    • J.R. O'Hara, and A.G. Buret Mechanisms of intestinal tight junctional disruption during infection Front Biosci 13 2008 7008 7021
    • (2008) Front Biosci , vol.13 , pp. 7008-7021
    • O'Hara, J.R.1    Buret, A.G.2
  • 28
    • 63249123919 scopus 로고    scopus 로고
    • Cytokine regulation of tight junctions
    • C.T. Capaldo, and A. Nusrat Cytokine regulation of tight junctions Biochim Biophys Acta 1788 2009 864 871
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 864-871
    • Capaldo, C.T.1    Nusrat, A.2
  • 29
    • 39849084350 scopus 로고    scopus 로고
    • Structural and functional associations of apical junctions with cytoskeleton
    • J. Miyoshi, and Y. Takai Structural and functional associations of apical junctions with cytoskeleton Biochim Biophys Acta 1778 2008 670 691
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 670-691
    • Miyoshi, J.1    Takai, Y.2
  • 30
    • 70350509805 scopus 로고    scopus 로고
    • Intestinal mucosal barrier function in health and disease
    • J.R. Turner Intestinal mucosal barrier function in health and disease Nat Rev Immunol 9 2009 799 809
    • (2009) Nat Rev Immunol , vol.9 , pp. 799-809
    • Turner, J.R.1
  • 31
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor
    • DOI 10.1126/science.1081412
    • A.F. Straight, A. Cheung, J. Limouze, I. Chen, N.J. Westwood, and J.R. Sellers Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor Science 299 2003 1743 1747 (Pubitemid 36337202)
    • (2003) Science , vol.299 , Issue.5613 , pp. 1743-1747
    • Straight, A.F.1    Cheung, A.2    Limouze, J.3    Chen, I.4    Westwood, N.J.5    Sellers, J.R.6    Mitchison, T.J.7
  • 32
    • 18744393735 scopus 로고    scopus 로고
    • The structural basis of blebbistatin inhibition and specificity for myosin II
    • DOI 10.1038/nsmb908
    • J.S. Allingham, R. Smith, and I. Rayment The structural basis of blebbistatin inhibition and specificity for myosin II Nat Struct Mol Biol 12 2005 378 379 (Pubitemid 43093094)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.4 , pp. 378-379
    • Allingham, J.S.1    Smith, R.2    Rayment, I.3
  • 35
    • 0023644877 scopus 로고
    • Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase
    • M. Saitoh, T. Ishikawa, S. Matsushima, M. Naka, and H. Hidaka Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase J Biol Chem 262 1987 7796 7801
    • (1987) J Biol Chem , vol.262 , pp. 7796-7801
    • Saitoh, M.1    Ishikawa, T.2    Matsushima, S.3    Naka, M.4    Hidaka, H.5
  • 36
    • 75149162956 scopus 로고    scopus 로고
    • PKC-alpha controls MYD88-dependent TLR/IL-1R signaling and cytokine production in mouse and human dendritic cells
    • C. Langlet, C. Springael, J. Johnson, S. Thomas, V. Flamand, and M. Leitges PKC-alpha controls MYD88-dependent TLR/IL-1R signaling and cytokine production in mouse and human dendritic cells Eur J Immunol 40 2010 505 515
    • (2010) Eur J Immunol , vol.40 , pp. 505-515
    • Langlet, C.1    Springael, C.2    Johnson, J.3    Thomas, S.4    Flamand, V.5    Leitges, M.6
  • 37
    • 49349103910 scopus 로고    scopus 로고
    • Toll-like receptor 3 triggers apoptosis of human prostate cancer cells through a PKC-alpha-dependent mechanism
    • A. Paone, D. Starace, R. Galli, F. Padula, P. De Cesaris, and A. Filippini Toll-like receptor 3 triggers apoptosis of human prostate cancer cells through a PKC-alpha-dependent mechanism Carcinogenesis 29 2008 1334 1342
    • (2008) Carcinogenesis , vol.29 , pp. 1334-1342
    • Paone, A.1    Starace, D.2    Galli, R.3    Padula, F.4    De Cesaris, P.5    Filippini, A.6
  • 38
    • 34447504038 scopus 로고    scopus 로고
    • Protein kinase Cα is involved in interferon regulatory factor 3 activation and type I interferon-β synthesis
    • DOI 10.1074/jbc.M700421200
    • J. Johnson, V. Albarani, M. Nguyen, M. Goldman, F. Willems, and E. Aksoy Protein kinase Calpha is involved in interferon regulatory factor 3 activation and type I interferon-beta synthesis J Biol Chem 282 2007 15022 15032 (Pubitemid 47093374)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 15022-15032
    • Johnson, J.1    Albarani, V.2    Nguyen, M.3    Goldman, M.4    Willems, F.5    Aksoy, E.6
  • 41
    • 66749172932 scopus 로고    scopus 로고
    • Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility
    • A.I. Ivanov, S.N. Samarin, M. Bachar, C.A. Parkos, and A. Nusrat Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility BMC Cell Biol 10 2009 36
    • (2009) BMC Cell Biol , vol.10 , pp. 36
    • Ivanov, A.I.1    Samarin, S.N.2    Bachar, M.3    Parkos, C.A.4    Nusrat, A.5
  • 44
  • 45
    • 0032538539 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites required for protein kinase D activation
    • DOI 10.1074/jbc.273.42.27662
    • T. Iglesias, R.T. Waldron, and E. Rozengurt Identification of in vivo phosphorylation sites required for protein kinase D activation J Biol Chem 273 1998 27662 27667 (Pubitemid 28500491)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27662-27667
    • Iglesias, T.1    Waldron, R.T.2    Rozengurt, E.3
  • 48
    • 80052060270 scopus 로고    scopus 로고
    • Rhinovirus-induced barrier dysfunction in polarized airway epithelial cells is mediated by NADPH oxidase 1
    • A.T. Comstock, S. Ganesan, A. Chattoraj, A.N. Faris, B.L. Margolis, and M.B. Hershenson Rhinovirus-induced barrier dysfunction in polarized airway epithelial cells is mediated by NADPH oxidase 1 J Virol 85 2011 6795 6808
    • (2011) J Virol , vol.85 , pp. 6795-6808
    • Comstock, A.T.1    Ganesan, S.2    Chattoraj, A.3    Faris, A.N.4    Margolis, B.L.5    Hershenson, M.B.6
  • 49
    • 78649630659 scopus 로고    scopus 로고
    • Poly(I: C) reduces expression of JAM-A and induces secretion of IL-8 and TNF-alpha via distinct NF-kappaB pathways in human nasal epithelial cells
    • T. Ohkuni, T. Kojima, N. Ogasawara, T. Masaki, J. Fuchimoto, and R. Kamekura Poly(I: C) reduces expression of JAM-A and induces secretion of IL-8 and TNF-alpha via distinct NF-kappaB pathways in human nasal epithelial cells Toxicol Appl Pharmacol 250 2011 29 38
    • (2011) Toxicol Appl Pharmacol , vol.250 , pp. 29-38
    • Ohkuni, T.1    Kojima, T.2    Ogasawara, N.3    Masaki, T.4    Fuchimoto, J.5    Kamekura, R.6
  • 50
    • 70749116345 scopus 로고    scopus 로고
    • Double-stranded RNA activates type i interferon secretion in glomerular endothelial cells via retinoic acid-inducible gene (RIG)-1
    • H. Hagele, R. Allam, R.D. Pawar, and H.J. Anders Double-stranded RNA activates type I interferon secretion in glomerular endothelial cells via retinoic acid-inducible gene (RIG)-1 Nephrol Dial Transplant 24 2009 3312 3318
    • (2009) Nephrol Dial Transplant , vol.24 , pp. 3312-3318
    • Hagele, H.1    Allam, R.2    Pawar, R.D.3    Anders, H.J.4
  • 53
    • 0035665517 scopus 로고    scopus 로고
    • Lung epithelial barrier function and wound healing are decreased by IL-4 and IL-13 and enhanced by IFN-gamma
    • M. Ahdieh, T. Vandenbos, and A. Youakim Lung epithelial barrier function and wound healing are decreased by IL-4 and IL-13 and enhanced by IFN-gamma Am J Physiol Cell Physiol 281 2001 C2029 C2038
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Ahdieh, M.1    Vandenbos, T.2    Youakim, A.3
  • 55
    • 0033754902 scopus 로고    scopus 로고
    • The polymerization motor
    • J.A. Theriot The polymerization motor Traffic 1 2000 19 28
    • (2000) Traffic , vol.1 , pp. 19-28
    • Theriot, J.A.1
  • 57
    • 0036789132 scopus 로고    scopus 로고
    • Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion
    • K.G. Scott, J.B. Meddings, D.R. Kirk, S.P. Lees-Miller, and A.G. Buret Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion Gastroenterology 123 2002 1179 1190
    • (2002) Gastroenterology , vol.123 , pp. 1179-1190
    • Scott, K.G.1    Meddings, J.B.2    Kirk, D.R.3    Lees-Miller, S.P.4    Buret, A.G.5
  • 59
    • 26244442836 scopus 로고    scopus 로고
    • Mechanism of IFN-γ-induced endocytosis of tight junction proteins: Myosin II-dependent vacuolarization of the apical plasma membrane
    • DOI 10.1091/mbc.E05-03-0193
    • M. Utech, A.I. Ivanov, S.N. Samarin, M. Bruewer, J.R. Turner, and R.J. Mrsny Mechanism of IFN-gamma-induced endocytosis of tight junction proteins: myosin II-dependent vacuolarization of the apical plasma membrane Mol Biol Cell 16 2005 5040 5052 (Pubitemid 41416480)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 5040-5052
    • Utech, M.1    Ivanov, A.I.2    Samarin, S.N.3    Bruewer, M.4    Turner, J.R.5    Mrsny, R.J.6    Parkos, C.A.7    Nusrat, A.8
  • 60
    • 77951895550 scopus 로고    scopus 로고
    • Protein kinase D1 is essential for the proinflammatory response induced by hypersensitivity pneumonitis-causing thermophilic actinomycetes Saccharopolyspora rectivirgula
    • Y.I. Kim, J.E. Park, D.D. Brand, E.A. Fitzpatrick, and A.K. Yi Protein kinase D1 is essential for the proinflammatory response induced by hypersensitivity pneumonitis-causing thermophilic actinomycetes Saccharopolyspora rectivirgula J Immunol 184 2010 3145 3156
    • (2010) J Immunol , vol.184 , pp. 3145-3156
    • Kim, Y.I.1    Park, J.E.2    Brand, D.D.3    Fitzpatrick, E.A.4    Yi, A.K.5
  • 61
    • 64049100454 scopus 로고    scopus 로고
    • Protein kinase D is an essential regulator of C. elegans innate immunity
    • M. Ren, H. Feng, Y. Fu, M. Land, and C.S. Rubin Protein kinase D is an essential regulator of C. elegans innate immunity Immunity 30 2009 521 532
    • (2009) Immunity , vol.30 , pp. 521-532
    • Ren, M.1    Feng, H.2    Fu, Y.3    Land, M.4    Rubin, C.S.5
  • 63
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • DOI 10.1016/j.cellsig.2005.07.010, PII S089865680500183X
    • C. Larsson Protein kinase C and the regulation of the actin cytoskeleton Cell Signal 18 2006 276 284 (Pubitemid 41661343)
    • (2006) Cellular Signalling , vol.18 , Issue.3 , pp. 276-284
    • Larsson, C.1


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