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Volumn 29, Issue 1, 2006, Pages 16-26

Epithelial cells as sentinels in mucosal immune barrier

Author keywords

Antimicrobial peptide; Chemokine; Epithelial cells; M cells; Mucosal immunity

Indexed keywords

ANTIGEN; ANTIMICROBIAL CATIONIC PEPTIDE; CHEMOKINE; FC RECEPTOR; FC RECEPTOR, NEONATAL; HLA ANTIGEN CLASS 1;

EID: 33645452204     PISSN: 09114300     EISSN: 13497413     Source Type: Journal    
DOI: 10.2177/jsci.29.16     Document Type: Article
Times cited : (10)

References (91)
  • 1
    • 0035320037 scopus 로고    scopus 로고
    • Multifunctional strands in tight junctions
    • Tsukita S, et al.: Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol 2: 285–293, 2001.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 285-293
    • Tsukita, S.1
  • 2
    • 0029133784 scopus 로고
    • Trefoil peptide protection of intestinal epithelial barrier function: Cooperative interaction with mucin glycoprotein
    • Kindon H, et al.: Trefoil peptide protection of intestinal epithelial barrier function: Cooperative interaction with mucin glycoprotein. Gastroenterology 109: 516–523, 1995.
    • (1995) Gastroenterology , vol.109 , pp. 516-523
    • Kindon, H.1
  • 3
    • 0001216086 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides in host defense against infection
    • Bals R: Epithelial antimicrobial peptides in host defense against infection. Respir Res 1: 141–150, 2000.
    • (2000) Respir Res , vol.1 , pp. 141-150
    • Bals, R.1
  • 4
    • 0027390031 scopus 로고
    • Defensin-6mRNAin human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel
    • Jones DE, Bevins CL: Defensin-6mRNAin human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel. FEBS Lett 315: 187–192, 1993.
    • (1993) FEBS Lett , vol.315 , pp. 187-192
    • Jones, D.E.1    Bevins, C.L.2
  • 5
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones DE, Bevins CL: Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem 267: 23216–23225, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 6
    • 0025281425 scopus 로고
    • A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin
    • Ouellette AJ, Lualdi JC: A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin. J Biol Chem 265: 9831–9837, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 9831-9837
    • Ouellette, A.J.1    Lualdi, J.C.2
  • 7
    • 0034252293 scopus 로고    scopus 로고
    • Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria
    • Ayabe T, et al.: Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nat Immunol 1: 113–118, 2000.
    • (2000) Nat Immunol , vol.1 , pp. 113-118
    • Ayabe, T.1
  • 8
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson CL, et al.: Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 286: 113–117, 1999.
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1
  • 9
    • 0036079594 scopus 로고    scopus 로고
    • Paneth cell trypsin is the processing enzyme for human defensin-5
    • Ghosh D, et al.: Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol 3: 583–590, 2002.
    • (2002) Nat Immunol , vol.3 , pp. 583-590
    • Ghosh, D.1
  • 10
    • 0015063086 scopus 로고
    • The cytochemical localization of lysozyme in Paneth cell granules
    • Ghoos Y, Vantrappen G: The cytochemical localization of lysozyme in Paneth cell granules. Histochem J 3: 175–178, 1971.
    • (1971) Histochem J , vol.3 , pp. 175-178
    • Ghoos, Y.1    Vantrappen, G.2
  • 11
    • 1542644985 scopus 로고    scopus 로고
    • Bactericidal properties of group IIa secreted phospholipase A (2) against Pseudomonas aeruginosa clinical isolates
    • Dubouix A, et al.: Bactericidal properties of group IIa secreted phospholipase A (2) against Pseudomonas aeruginosa clinical isolates. J Med Microbiol 52: 1039–1045, 2003.
    • (2003) J Med Microbiol , vol.52 , pp. 1039-1045
    • Dubouix, A.1
  • 12
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human β-defensins hBD-l and hBD-2in intestinal epithelium
    • O’Neil DA, et al.: Expression and regulation of the human β-defensins hBD-l and hBD-2in intestinal epithelium. J Immunol 163: 6718–6724, 1999.
    • (1999) J Immunol , vol.163 , pp. 6718-6724
    • O’Neil, D.A.1
  • 13
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic
    • Harder J, et al.: Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic. J Biol Chem 276: 5707–5713, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 5707-5713
    • Harder, J.1
  • 14
    • 0035430147 scopus 로고    scopus 로고
    • Human β-defensin 4: A novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity
    • Garcia JR, et al.: Human β-defensin 4: A novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity. Faseb J 15: 1819–1821, 2001.
    • (2001) Faseb J , vol.15 , pp. 1819-1821
    • Garcia, J.R.1
  • 15
    • 0036151109 scopus 로고    scopus 로고
    • Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium
    • Hase K, et al.: Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. Infect Immun 70: 953–963, 2002.
    • (2002) Infect Immun , vol.70 , pp. 953-963
    • Hase, K.1
  • 16
    • 10744224946 scopus 로고    scopus 로고
    • Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori
    • Hase K, et al.: Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori. Gastroenterology 125: 1613–1625, 2003.
    • (2003) Gastroenterology , vol.125 , pp. 1613-1625
    • Hase, K.1
  • 17
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman NH, et al.: Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature 422: 522–526, 2003.
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1
  • 18
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet V, et al.: Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414: 454–457, 2001.
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1
  • 19
    • 17044404692 scopus 로고    scopus 로고
    • Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens
    • Iimura M, et al.: Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens. J Immunol 174: 4901–4907, 2005.
    • (2005) J Immunol , vol.174 , pp. 4901-4907
    • Iimura, M.1
  • 20
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith J J, et al.: Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85: 229–236, 1996.
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1
  • 21
    • 0030949875 scopus 로고    scopus 로고
    • Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman MJ, et al.: Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88: 553–560, 1997.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1
  • 22
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in N0D2 associated with susceptibility to Crohn's disease
    • Ogura Y, et al.: A frameshift mutation in N0D2 associated with susceptibility to Crohn's disease. Nature 411: 603–606, 2001.
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1
  • 23
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucinerich repeat variants with susceptibility to Crohn's disease
    • Hugot JP, et al.: Association of NOD2 leucinerich repeat variants with susceptibility to Crohn's disease. Nature 411: 599–603, 2001.
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1
  • 24
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease
    • Inohara N, et al.: Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J Biol Chem 278: 5509–5512, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1
  • 25
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin SE, et al.: Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem 278: 8869–8872, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 8869-8872
    • Girardin, S.E.1
  • 26
    • 10744222688 scopus 로고    scopus 로고
    • Expression of NOD2 in Paneth cells: A possible link to Crohn's ileitis
    • Ogura Y, et al.: Expression of NOD2 in Paneth cells: A possible link to Crohn's ileitis. Gut 52: 1591–1597, 2003.
    • (2003) Gut , vol.52 , pp. 1591-l597
    • Ogura, Y.1
  • 27
    • 0038109983 scopus 로고    scopus 로고
    • Crohn's disease and the NOD2 gene: A role for paneth cells
    • Lala S, et al.: Crohn's disease and the NOD2 gene: A role for paneth cells. Gastroenterology 125: 47–57, 2003.
    • (2003) Gastroenterology , vol.125 , pp. 47-57
    • Lala, S.1
  • 28
    • 13244292161 scopus 로고    scopus 로고
    • Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract
    • Kobayashi KS, et al.: Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307: 731–734, 2005.
    • (2005) Science , vol.307 , pp. 731-734
    • Kobayashi, K.S.1
  • 29
    • 4444253690 scopus 로고    scopus 로고
    • N0D2 is a negative regulator of Toll-like receptor 2-mediated T helper type 1 responses
    • Watanabe T, et al.: N0D2 is a negative regulator of Toll-like receptor 2-mediated T helper type 1 responses. Nat Immunol 5: 800–808, 2004.
    • (2004) Nat Immunol , vol.5 , pp. 800-808
    • Watanabe, T.1
  • 30
    • 13244277880 scopus 로고    scopus 로고
    • Nod2 mutation in Crohn's disease potentiates NF-kB activity and IL-lβ processing
    • Maeda S, et al.: Nod2 mutation in Crohn's disease potentiates NF-kB activity and IL-lβ processing. Science 307: 734–738, 2005.
    • (2005) Science , vol.307 , pp. 734-738
    • Maeda, S.1
  • 31
    • 0030870251 scopus 로고    scopus 로고
    • Differential and regulated expression of C-X-C, C-C, and C-chemokines by human colon epithelial cells
    • Yang SK, et al.: Differential and regulated expression of C-X-C, C-C, and C-chemokines by human colon epithelial cells. Gastroenterology 113: 1214–1223, 1997.
    • (1997) Gastroenterology , vol.113 , pp. 1214-1223
    • Yang, S.K.1
  • 32
    • 0027428365 scopus 로고
    • Salmonella typhimurium attachment to human intestinal epithelial monolayers: Transcellular signalling to subepithelial neutrophils
    • McCormick BA, et al.: Salmonella typhimurium attachment to human intestinal epithelial monolayers: Transcellular signalling to subepithelial neutrophils. J Cell Biol 123: 895–907, 1993.
    • (1993) J Cell Biol , vol.123 , pp. 895-907
    • McCormick, B.A.1
  • 33
    • 0028864991 scopus 로고
    • A distinct array of proinflammatory cytokines is expressed in human colon epithelial cells in response to bacterial invasion
    • Jung HC, et al.: A distinct array of proinflammatory cytokines is expressed in human colon epithelial cells in response to bacterial invasion. J Clin Invest 95: 55–65, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 55-65
    • Jung, H.C.1
  • 34
    • 0033569408 scopus 로고    scopus 로고
    • β-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • Yang D, et al.: β-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6. Science 286: 525–528, 1999.
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1
  • 35
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De Y, et al.: LL-37, the neutrophil granule and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med 192: 1069–1074, 2000.
    • (2000) J Exp Med , vol.192 , pp. 1069-1074
    • De, Y.1
  • 36
    • 0035879198 scopus 로고    scopus 로고
    • Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity
    • Cole AM, et al.: Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity. J Immunol 167: 623–627, 2001.
    • (2001) J Immunol , vol.167 , pp. 623-627
    • Cole, A.M.1
  • 37
    • 0010109877 scopus 로고    scopus 로고
    • Apoptosis of human intestinal epithelial cells after bacterial invasion
    • Kim JM, et al.: Apoptosis of human intestinal epithelial cells after bacterial invasion. J Clin Invest 102: 1815–1823, 1998.
    • (1998) J Clin Invest , vol.102 , pp. 1815-1823
    • Kim, J.M.1
  • 38
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky A, et al.: Shigella flexneri induces apoptosis in infected macrophages. Nature 358: 167–169, 1992.
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1
  • 39
    • 0029793103 scopus 로고    scopus 로고
    • Salmonella typhimurium invasion induces apoptosis in infected macro-phages
    • Monack DM, et al.: Salmonella typhimurium invasion induces apoptosis in infected macro-phages. Proc Natl Acad Sci USA 93: 9833–9838, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9833-9838
    • Monack, D.M.1
  • 40
    • 0036166387 scopus 로고    scopus 로고
    • Chemokines and the tissue-specific migration of lymphocytes
    • Kunkel EJ, Butcher EC: Chemokines and the tissue-specific migration of lymphocytes. Immunity 16: 1–4, 2002.
    • (2002) Immunity , vol.16 , pp. 1-4
    • Kunkel, E.J.1    Butcher, E.C.2
  • 41
    • 29644439799 scopus 로고    scopus 로고
    • The Membrane-Bound Chemokine CXCL16 Expressed on Follicle-Associated Epithelium and M Cells Mediates Lympho-Epithelial Interaction in GALT
    • Hase K, et al.: The Membrane-Bound Chemokine CXCL16 Expressed on Follicle-Associated Epithelium and M Cells Mediates Lympho-Epithelial Interaction in GALT. J Immunol 176: 43–51, 2006.
    • (2006) J Immunol , vol.176 , pp. 43-51
    • Hase, K.1
  • 42
    • 0042834355 scopus 로고    scopus 로고
    • CCL9 is secreted by the follicle-associated epithelium and recruits dome region Peyer's patch CD11b+ dendritic cells
    • Zhao X, et al.: CCL9 is secreted by the follicle-associated epithelium and recruits dome region Peyer's patch CD11b+ dendritic cells. J Immunol 171: 2797–2803, 2003.
    • (2003) J Immunol , vol.171 , pp. 2797-2803
    • Zhao, X.1
  • 43
    • 0034678392 scopus 로고    scopus 로고
    • Localization of distinct Peyer's patch dendritic cell subsets and their recruitment by chemokines macrophage inflammatory protein (MIP)-3α, MIP-3β, and secondary lymphoid organ chemokine
    • Iwasaki A, Kelsall BL: Localization of distinct Peyer's patch dendritic cell subsets and their recruitment by chemokines macrophage inflammatory protein (MIP)-3α, MIP-3β, and secondary lymphoid organ chemokine. J Exp Med 191: 1381–1394, 2000.
    • (2000) J Exp Med , vol.191 , pp. 1381-1394
    • Iwasaki, A.1    Kelsall, B.L.2
  • 44
    • 2442527640 scopus 로고    scopus 로고
    • The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNF-α and shed by the activity of the disintegrin-like metalloproteinase ADAM10
    • Abel S, et al.: The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNF-α and shed by the activity of the disintegrin-like metalloproteinase ADAM10. J Immunol 172: 6362–6372, 2004.
    • (2004) J Immunol , vol.172 , pp. 6362-6372
    • Abel, S.1
  • 45
    • 1542724429 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16
    • Gough PJ, et al.: A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16. J Immunol 172: 3678–3685, 2004.
    • (2004) J Immunol , vol.172 , pp. 3678-3685
    • Gough, P.J.1
  • 46
    • 27744498868 scopus 로고    scopus 로고
    • Follicular B helper T cells in antibody responses and autoimmunity
    • Vinuesa CG, et al.: Follicular B helper T cells in antibody responses and autoimmunity. Nat Rev Immunol 5: 853–865, 2005.
    • (2005) Nat Rev Immunol , vol.5 , pp. 853-865
    • Vinuesa, C.G.1
  • 47
    • 0034605043 scopus 로고    scopus 로고
    • Lymphocyte CC chemokine receptor 9 and epithelial thymus-expressed chemokine (TECK) expression distinguish the small intestinal immune compartment: Epithelial expression of tissue-specific chemokines as an organizing principle in regional immunity
    • Kunkel EJ, et al.: Lymphocyte CC chemokine receptor 9 and epithelial thymus-expressed chemokine (TECK) expression distinguish the small intestinal immune compartment: Epithelial expression of tissue-specific chemokines as an organizing principle in regional immunity. J Exp Med 192: 761–768, 2000.
    • (2000) J Exp Med , vol.192 , pp. 761-768
    • Kunkel, E.J.1
  • 48
    • 0036802422 scopus 로고    scopus 로고
    • CCL25 mediates the localization of recently activated CD8αβ (+) lymphocytes to the small-intestinal mucosa
    • Svensson M, et al.: CCL25 mediates the localization of recently activated CD8αβ (+) lymphocytes to the small-intestinal mucosa. J Clin Invest 110: 1113–1121, 2002.
    • (2002) J Clin Invest , vol.110 , pp. 1113-1121
    • Svensson, M.1
  • 49
    • 0037148514 scopus 로고    scopus 로고
    • The intestinal chemokine thymus-expressed chemokine (CCL25) attracts IgA antibody-secreting cells
    • Bowman EP, et al.: The intestinal chemokine thymus-expressed chemokine (CCL25) attracts IgA antibody-secreting cells. J Exp Med 195: 269–275, 2002.
    • (2002) J Exp Med , vol.195 , pp. 269-275
    • Bowman, E.P.1
  • 50
    • 0346665751 scopus 로고    scopus 로고
    • A common mucosal chemokine (mucosae-associated epithelial chemokine/CCL28) selectively attracts IgA plasmablasts
    • Lazarus NH, et al.: A common mucosal chemokine (mucosae-associated epithelial chemokine/CCL28) selectively attracts IgA plasmablasts. J Immunol 170: 3799–3805, 2003.
    • (2003) J Immunol , vol.170 , pp. 3799-3805
    • Lazarus, N.H.1
  • 51
    • 0037382166 scopus 로고    scopus 로고
    • CCR10 expression is a common feature of circulating and mucosal epithelial tissue IgA Ab-secreting cells
    • Kunkel EJ, et al.: CCR10 expression is a common feature of circulating and mucosal epithelial tissue IgA Ab-secreting cells. J Clin Invest 111: 1001–1010, 2003.
    • (2003) J Clin Invest , vol.111 , pp. 1001-1010
    • Kunkel, E.J.1
  • 52
    • 0034959553 scopus 로고    scopus 로고
    • Short-chain fatty acids and human colonic function: Roles of resistant starch and nonstarch polysaccharides
    • Topping DL, Clifton PM: Short-chain fatty acids and human colonic function: Roles of resistant starch and nonstarch polysaccharides. Physiol Rev 81: 1031–1064, 2001.
    • (2001) Physiol Rev , vol.81 , pp. 1031-1064
    • Topping, D.L.1    Clifton, P.M.2
  • 53
    • 0042866144 scopus 로고    scopus 로고
    • Trophic and cytoprotective nutrition for intestinal adaptation, mucosal repair, and barrier function
    • Ziegler TR, et al.: Trophic and cytoprotective nutrition for intestinal adaptation, mucosal repair, and barrier function. Annu Rev Nutr 23: 229–261, 2003.
    • (2003) Annu Rev Nutr , vol.23 , pp. 229-261
    • Ziegler, T.R.1
  • 54
    • 0024321629 scopus 로고
    • Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide
    • Weintraub A, et al.: Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide. Eur J Biochem 183: 425–431, 1989.
    • (1989) Eur J Biochem , vol.183 , pp. 425-431
    • Weintraub, A.1
  • 55
    • 0026088437 scopus 로고
    • Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes
    • Golenbock DT, et al.: Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes. J Biol Chem 266: 19490–19498, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 19490-19498
    • Golenbock, D.T.1
  • 56
    • 2142810997 scopus 로고    scopus 로고
    • DNA from probiotic bacteria modulates murine and human epithelial and immune function
    • Jijon H, et al.: DNA from probiotic bacteria modulates murine and human epithelial and immune function. Gastroenterology 126: 1358–1373, 2004.
    • (2004) Gastroenterology , vol.126 , pp. 1358-1373
    • Jijon, H.1
  • 57
    • 0347756655 scopus 로고    scopus 로고
    • Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-γ and RelA
    • Kelly D, et al.: Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-γ and RelA. Nat Immunol 5: 104-ll2, 2004.
    • (2004) Nat Immunol , vol.5 , pp. 104-ll2
    • Kelly, D.1
  • 58
    • 0035424901 scopus 로고    scopus 로고
    • Decreased expression of Toll-like receptor-4and MD-2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide
    • Abreu MT, et al.: Decreased expression of Toll-like receptor-4and MD-2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide. J Immunol 167: 1609–1616, 2001.
    • (2001) J Immunol , vol.167 , pp. 1609-1616
    • Abreu, M.T.1
  • 59
    • 0037018107 scopus 로고    scopus 로고
    • Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells
    • Hornef MW, et al.: Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells. J Exp Med 195: 559–570, 2002.
    • (2002) J Exp Med , vol.195 , pp. 559-570
    • Hornef, M.W.1
  • 60
    • 0037756822 scopus 로고    scopus 로고
    • Anti-inflammatory role for intracellular dimeric immunoglobulin a by neutralization of lipopolysaccharide in epithelial cells
    • Fernandez MI, et al.: Anti-inflammatory role for intracellular dimeric immunoglobulin a by neutralization of lipopolysaccharide in epithelial cells. Immunity 18: 739–749, 2003.
    • (2003) Immunity , vol.18 , pp. 739-749
    • Fernandez, M.I.1
  • 61
    • 0035881675 scopus 로고    scopus 로고
    • Cutting edge: Bacterial lagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression
    • Gewirtz AT, et al.: Cutting edge: Bacterial lagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression. J Immunol 167: 1882–1885, 2001.
    • (2001) J Immunol , vol.167 , pp. 1882-1885
    • Gewirtz, A.T.1
  • 62
    • 0035923513 scopus 로고    scopus 로고
    • Flagellin stimulation of intestinal epithelial cells triggers CCL20-mediated migration of dendritic cells
    • Sierro F, et al.: Flagellin stimulation of intestinal epithelial cells triggers CCL20-mediated migration of dendritic cells. Proc Natl Acad Sci USA 98: 13722–13727, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13722-13727
    • Sierro, F.1
  • 63
    • 0033591330 scopus 로고    scopus 로고
    • Nodl, an Apaf-1-like acti-vatorofcaspase-9 and nuclear factor-kB
    • Inohara N, et al.: Nodl, an Apaf-1-like acti-vatorofcaspase-9 and nuclear factor-kB. J Biol Chem 274: 14560–14567, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 14560-14567
    • Inohara, N.1
  • 64
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • Chamaillard M, et al.: An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol 4: 702–707, 2003.
    • (2003) Nat Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1
  • 65
    • 1342344961 scopus 로고    scopus 로고
    • Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors
    • Kim JG, et al.: Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors. Infect Immun 72: 1487–1495, 2004.
    • (2004) Infect Immun , vol.72 , pp. 1487-1495
    • Kim, J.G.1
  • 66
    • 17944380130 scopus 로고    scopus 로고
    • CARD4/Nodl mediates NF-kB and JNK activation by invasive Shigella flexneri
    • Girardin SE, et al.: CARD4/Nodl mediates NF-kB and JNK activation by invasive Shigella flexneri. EMBO Rep 2: 736–742, 2001.
    • (2001) EMBO Rep , vol.2 , pp. 736-742
    • Girardin, S.E.1
  • 67
    • 0031252807 scopus 로고    scopus 로고
    • Activation of NF-kBinin-testinal epithelial cells by enteropathogenic Es cherichia coli
    • Savkovic SD, et al.: Activation of NF-kBinin-testinal epithelial cells by enteropathogenic Es cherichia coli. Am J Physiol 273: C1160-C1167, 1997.
    • (1997) Am J Physiol , vol.273 , pp. C1160-C1167
    • Savkovic, S.D.1
  • 68
    • 0028961743 scopus 로고
    • Interleukin-8 response of gastric epithelial cell lines to Helicobacter pylori stimulation in vitro
    • Sharma SA, et al.: Interleukin-8 response of gastric epithelial cell lines to Helicobacter pylori stimulation in vitro. Infect Immun 63: 1681–1687, 1995.
    • (1995) Infect Immun , vol.63 , pp. 1681-1687
    • Sharma, S.A.1
  • 69
    • 0028911662 scopus 로고
    • Stimulation of interleukin-8 production in epithelial cell lines by Helicobacter pylori
    • Huang J, et al.: Stimulation of interleukin-8 production in epithelial cell lines by Helicobacter pylori. Infect Immun 63: 1732–1738, 1995.
    • (1995) Infect Immun , vol.63 , pp. 1732-1738
    • Huang, J.1
  • 70
    • 9244245293 scopus 로고    scopus 로고
    • Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island
    • Viala J, et al.: Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island. Nat Immunol 5: 1166–1174, 2004.
    • (2004) Nat Immunol , vol.5 , pp. 1166-1174
    • Viala, J.1
  • 71
    • 0034518342 scopus 로고    scopus 로고
    • Gut feelings: Enteropathogenic E. coli (EPEC) interactions with the host
    • Goosney DL, et al.: Gut feelings: Enteropathogenic E. coli (EPEC) interactions with the host. Annu Rev Cell Dev Biol 16: 173–189, 2000.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 173-189
    • Goosney, D.L.1
  • 72
    • 0036532450 scopus 로고    scopus 로고
    • Port of entry-the type III secretion translocon
    • Buttner D, Bonas U: Port of entry-the type III secretion translocon. Trends Microbiol 10: 186–192, 2002.
    • (2002) Trends Microbiol , vol.10 , pp. 186-192
    • Buttner, D.1    Bonas, U.2
  • 73
    • 0038316325 scopus 로고    scopus 로고
    • Anatomical basis of tolerance and immunity to intestinal antigens
    • Mowat AM: Anatomical basis of tolerance and immunity to intestinal antigens. Nat Rev Immunol 3: 331–341, 2003.
    • (2003) Nat Rev Immunol , vol.3 , pp. 331-341
    • Mowat, A.M.1
  • 74
    • 4544258068 scopus 로고    scopus 로고
    • NALT-versus Peyer’s-patch-mediated mucosal immunity
    • Kiyono H, Fukuyama S: NALT-versus Peyer’s-patch-mediated mucosal immunity. Nat Rev Immunol 4: 699–710, 2004.
    • (2004) Nat Rev Immunol , vol.4 , pp. 699-710
    • Kiyono, H.1    Fukuyama, S.2
  • 75
    • 0017341263 scopus 로고
    • Sequential uptake of horseradish peroxidase by lymphoid follicle epithelium of Peyer's patches in the normal unobstructed mouse intestine: An ultrastructural study
    • Owen RL: Sequential uptake of horseradish peroxidase by lymphoid follicle epithelium of Peyer's patches in the normal unobstructed mouse intestine: An ultrastructural study. Gastroenterology 72: 440–451, 1977.
    • (1977) Gastroenterology , vol.72 , pp. 440-451
    • Owen, R.L.1
  • 76
    • 0034518344 scopus 로고    scopus 로고
    • Epithelial M cells: Diferentiation and function
    • Kraehenbuhl JP, Neutra MR: Epithelial M cells: Diferentiation and function. Annu Rev Cell Dev Biol 16: 301–332, 2000.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 301-332
    • Kraehenbuhl, J.P.1    Neutra, M.R.2
  • 77
    • 0032794570 scopus 로고    scopus 로고
    • Uptake and transport of intestinal macromolecules and microorganisms by M cells in Peyer's patches-a personal and historical perspective
    • Owen RL: Uptake and transport of intestinal macromolecules and microorganisms by M cells in Peyer's patches-a personal and historical perspective. Semin Immunol 11: 157–163, 1999.
    • (1999) Semin Immunol , vol.11 , pp. 157-163
    • Owen, R.L.1
  • 78
    • 0023092367 scopus 로고
    • Transport of membrane-bound macromolecules by M cells in follicle-associated epithelium of rabbit Peyer's patch
    • Neutra MR, et al.: Transport of membrane-bound macromolecules by M cells in follicle-associated epithelium of rabbit Peyer's patch. Cell Tissue Res 247: 537–546, 1987.
    • (1987) Cell Tissue Res , vol.247 , pp. 537-546
    • Neutra, M.R.1
  • 79
    • 0037103328 scopus 로고    scopus 로고
    • Selective adherence of IgA to murine Peyer's patch M cells: Evidence for a novel IgA receptor
    • Mantis NJ, et al.: Selective adherence of IgA to murine Peyer's patch M cells: Evidence for a novel IgA receptor. J Immunol 169: 1844–1851, 2002.
    • (2002) J Immunol , vol.169 , pp. 1844-1851
    • Mantis, N.J.1
  • 80
    • 0029787628 scopus 로고    scopus 로고
    • Role of the glycocalyx in regulating access of microparticles to apical plasma membranes of intestinal epithelial cells: Implications for microbial attachment and oral vaccine targeting
    • Frey A, et al.: Role of the glycocalyx in regulating access of microparticles to apical plasma membranes of intestinal epithelial cells: Implications for microbial attachment and oral vaccine targeting. J Exp Med 184: 1045–1059, 1996.
    • (1996) J Exp Med , vol.184 , pp. 1045-1059
    • Frey, A.1
  • 81
    • 0032167625 scopus 로고    scopus 로고
    • Studying M cells and their role in infection
    • Jepson MA, Clark MA: Studying M cells and their role in infection. Trends Microbiol 6: 359–365, 1998.
    • (1998) Trends Microbiol , vol.6 , pp. 359-365
    • Jepson, M.A.1    Clark, M.A.2
  • 82
    • 11144358593 scopus 로고    scopus 로고
    • Intestinal villous M cells: An antigen entry site in the mucosal epithelium
    • Jang MH, et al.: Intestinal villous M cells: An antigen entry site in the mucosal epithelium. Proc Natl Acad Sci USA 101: 6110–6115, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6110-6115
    • Jang, M.H.1
  • 83
    • 24944576523 scopus 로고    scopus 로고
    • Distinct gene expression profiles characterize cellular phenotypes of follicle-associated epithelium and m cells
    • Hase K, et al.: Distinct gene expression profiles characterize cellular phenotypes of follicle-associated epithelium and m cells. DNA Res 12: 127–137, 2005.
    • (2005) DNA Res , vol.12 , pp. 127-137
    • Hase, K.1
  • 84
    • 0035321325 scopus 로고    scopus 로고
    • Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria
    • Rescigno M, et al.: Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nat Immunol 2: 361–367, 2001.
    • (2001) Nat Immunol , vol.2 , pp. 361-367
    • Rescigno, M.1
  • 85
    • 12244297799 scopus 로고    scopus 로고
    • CX3CRl-mediated dendritic cell access to the intestinal lumen and bacterial clearance
    • Niess JH, et al.: CX3CRl-mediated dendritic cell access to the intestinal lumen and bacterial clearance. Science 307: 254–258, 2005.
    • (2005) Science , vol.307 , pp. 254-258
    • Niess, J.H.1
  • 86
    • 18244387204 scopus 로고    scopus 로고
    • Intestinal immune homeostasis is regulated by the crosstalk between epithelial cells and dendritic cells
    • Rimoldi M, et al.: Intestinal immune homeostasis is regulated by the crosstalk between epithelial cells and dendritic cells. Nat Immunol 6: 507–514, 2005.
    • (2005) Nat Immunol , vol.6 , pp. 507-514
    • Rimoldi, M.1
  • 87
    • 0036301998 scopus 로고    scopus 로고
    • Human epithelial cells trigger dendritic cell mediated allergic inflammation by producing TSLP
    • Soumelis V, et al.: Human epithelial cells trigger dendritic cell mediated allergic inflammation by producing TSLP. Nat Immunol 3: 673–680, 2002.
    • (2002) Nat Immunol , vol.3 , pp. 673-680
    • Soumelis, V.1
  • 88
    • 0036902323 scopus 로고    scopus 로고
    • Immunoglobulin transport across polarized epithelial cells
    • Rojas R, Apodaca G: Immunoglobulin transport across polarized epithelial cells. Nat Rev Mol Cell Biol 3: 944–955, 2002.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 944-955
    • Rojas, R.1    Apodaca, G.2
  • 89
    • 0036337774 scopus 로고    scopus 로고
    • Secretory component: A new role in secretory IgA-mediated immune exclusion in vivo
    • Phalipon A, et al.: Secretory component: A new role in secretory IgA-mediated immune exclusion in vivo. Immunity 17: 107–115, 2002.
    • (2002) Immunity , vol.17 , pp. 107-115
    • Phalipon, A.1
  • 90
    • 0033523608 scopus 로고    scopus 로고
    • Absence of epithelial immunoglobulin A transport, with increased mucosal leakiness, in polymeric immunoglobulin receptor/secretory componentd-eficient mice
    • Johansen FE, et al.: Absence of epithelial immunoglobulin A transport, with increased mucosal leakiness, in polymeric immunoglobulin receptor/secretory componentd-eficient mice. J Exp Med 190: 915–922, 1999.
    • (1999) J Exp Med , vol.190 , pp. 915-922
    • Johansen, F.E.1
  • 91
    • 2942516894 scopus 로고    scopus 로고
    • Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells
    • Yoshida M, et al.: Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells. Immunity 20: 769–783, 2004.
    • (2004) Immunity , vol.20 , pp. 769-783
    • Yoshida, M.1


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