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Volumn 65, Issue 19, 2008, Pages 3019-3027

Multi-layered regulation of intestinal antimicrobial defense

Author keywords

C type lectin; Cathelicidin; Defensin; Inflammatory bowel disease; Paneth cell

Indexed keywords

CATHELICIDIN; DEFENSIN; LECTIN; RIBONUCLEASE;

EID: 53049087417     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8182-3     Document Type: Review
Times cited : (114)

References (73)
  • 3
    • 0020710588 scopus 로고
    • Dietary intake, energy metabolism, and excretory losses of adult male germfree Wistar rats
    • Wostmann, B. S., Larkin, C., Moriarty, A. and Bruckner-Kardoss, E. (1983). Dietary intake, energy metabolism, and excretory losses of adult male germfree Wistar rats. Lab. Anim. Sci. 33, 46-50.
    • (1983) Lab. Anim. Sci , vol.33 , pp. 46-50
    • Wostmann, B.S.1    Larkin, C.2    Moriarty, A.3    Bruckner-Kardoss, E.4
  • 4
    • 0036399823 scopus 로고    scopus 로고
    • How host-microbial interactions shape the nutrient environment of the mammalian intestine
    • Hooper, L. V., Midtvedt, T. and Gordon, J. I. (2002). How host-microbial interactions shape the nutrient environment of the mammalian intestine. Annu. Rev. Nutr. 22, 283-307.
    • (2002) Annu. Rev. Nutr , vol.22 , pp. 283-307
    • Hooper, L.V.1    Midtvedt, T.2    Gordon, J.I.3
  • 7
    • 22144490199 scopus 로고    scopus 로고
    • An immunomodulatory molecule of symbiotic bacteria directs maturation of the host immune system
    • Mazmanian, S. K., Liu, C. H., Tzianabos, A. O. and Kasper, D. L. (2005). An immunomodulatory molecule of symbiotic bacteria directs maturation of the host immune system. Cell 122, 107-118.
    • (2005) Cell , vol.122 , pp. 107-118
    • Mazmanian, S.K.1    Liu, C.H.2    Tzianabos, A.O.3    Kasper, D.L.4
  • 8
    • 0037180433 scopus 로고    scopus 로고
    • Developmental regulation of intestinal angiogenesis by indigenous microbes via Paneth cells
    • Stappenbeck, T. S., Hooper, L. V. and Gordon, J. I. (2002). Developmental regulation of intestinal angiogenesis by indigenous microbes via Paneth cells. Proc. Natl. Acad. Sci. USA 99, 15451-15455.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15451-15455
    • Stappenbeck, T.S.1    Hooper, L.V.2    Gordon, J.I.3
  • 12
    • 34249313567 scopus 로고    scopus 로고
    • Paneth cells, defensins, and the commensal microbiota: A hypothesis on intimate interplay at the intestinal mucosa
    • Salzman, N. H., Underwood, M. A. and Bevins, C. L. (2007). Paneth cells, defensins, and the commensal microbiota: a hypothesis on intimate interplay at the intestinal mucosa. Semin. Immunol. 19, 70-83.
    • (2007) Semin. Immunol , vol.19 , pp. 70-83
    • Salzman, N.H.1    Underwood, M.A.2    Bevins, C.L.3
  • 13
    • 0842304596 scopus 로고    scopus 로고
    • Antimicrobial polypeptides
    • Ganz, T. (2004). Antimicrobial polypeptides. J. Leukoc. Biol. 75, 34-38.
    • (2004) J. Leukoc. Biol , vol.75 , pp. 34-38
    • Ganz, T.1
  • 14
    • 0347298784 scopus 로고    scopus 로고
    • Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus
    • Koprivnjak, T., Peschel, A., Gelb, M. H., Liang, N. S. and Weiss, J. P. (2002). Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus. J. Biol. Chem. 277, 47636-47644.
    • (2002) J. Biol. Chem , vol.277 , pp. 47636-47644
    • Koprivnjak, T.1    Peschel, A.2    Gelb, M.H.3    Liang, N.S.4    Weiss, J.P.5
  • 15
    • 0037127316 scopus 로고    scopus 로고
    • The antibacterial properties of secreted phospholipases A2: A major physiological role for the group IIA enzyme that depends on the very high pI of the enzyme to allow penetration of the bacterial cell wall
    • Beers, S. A., Buckland, A. G., Koduri, R. S., Cho, W., Gelb, M. H. and Wilton, D. C. (2002). The antibacterial properties of secreted phospholipases A2: a major physiological role for the group IIA enzyme that depends on the very high pI of the enzyme to allow penetration of the bacterial cell wall. J. Biol. Chem. 277, 1788-1793.
    • (2002) J. Biol. Chem , vol.277 , pp. 1788-1793
    • Beers, S.A.1    Buckland, A.G.2    Koduri, R.S.3    Cho, W.4    Gelb, M.H.5    Wilton, D.C.6
  • 17
    • 0027330333 scopus 로고
    • Extracellular phospholipase A2 expression and inflammation: The relationship with associated disease states
    • Vadas, P., Browning, J., Edelson, J. and Pruzanski, W. (1993). Extracellular phospholipase A2 expression and inflammation: the relationship with associated disease states. J. Lipid. Mediat. 8, 1-30.
    • (1993) J. Lipid. Mediat , vol.8 , pp. 1-30
    • Vadas, P.1    Browning, J.2    Edelson, J.3    Pruzanski, W.4
  • 18
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. (2005). Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 19
    • 20644462344 scopus 로고    scopus 로고
    • Selsted, M. E. and Ouellette, A. J. (2005). Mammalian defensins in the antimicrobial immune response. Nat. Immuno.l 6, 551-557.
    • Selsted, M. E. and Ouellette, A. J. (2005). Mammalian defensins in the antimicrobial immune response. Nat. Immuno.l 6, 551-557.
  • 20
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., Selsted, M. E., Ganz, T. and Lehrer, R. I. (1990). Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA 87, 210-214.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 21
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B. and Lohner, K. (2006). Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta. 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 22
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H.W. (2000). Action of antimicrobial peptides: two-state model. Biochemistry 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 23
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002). Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 24
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman, N. H., Ghosh, D., Huttner, K. M., Paterson, Y. and Bevins, C. L. (2003). Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature 422, 522-526.
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 25
    • 4444246183 scopus 로고    scopus 로고
    • Increased diversity of intestinal antimicrobial peptides by covalent dimer formation
    • Hornef, M. W., Putsep, K., Karlsson, J., Refai, E. and Andersson, M. (2004). Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. Nat. Immunol. 5, 836-483.
    • (2004) Nat. Immunol , vol.5 , pp. 836-483
    • Hornef, M.W.1    Putsep, K.2    Karlsson, J.3    Refai, E.4    Andersson, M.5
  • 26
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium
    • O'Neil, D. A., Porter, E. M., Elewaut, D., Anderson, G. M., Eckmann, L., Ganz, T. and Kagnoff, M. F. (1999). Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium. J. Immunol. 163, 6718-6724.
    • (1999) J. Immunol , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1    Porter, E.M.2    Elewaut, D.3    Anderson, G.M.4    Eckmann, L.5    Ganz, T.6    Kagnoff, M.F.7
  • 28
    • 0037234635 scopus 로고    scopus 로고
    • Increased expression of antimicrobial peptides and lysozyme in colonic epithelial cells of patients with ulcerative colitis
    • Fahlgren, A., Hammarstrom, S., Danielsson, A. and Hammarstrom, M. L. (2003). Increased expression of antimicrobial peptides and lysozyme in colonic epithelial cells of patients with ulcerative colitis. Clin. Exp. Immunol. 131, 90-101.
    • (2003) Clin. Exp. Immunol , vol.131 , pp. 90-101
    • Fahlgren, A.1    Hammarstrom, S.2    Danielsson, A.3    Hammarstrom, M.L.4
  • 30
    • 0033855720 scopus 로고    scopus 로고
    • Regulation of human β-defensins by gastric epithelial cells in response to infection with Helicobacter pylori or stimulation with interleukin-1
    • O'Neil, D. A., Cole, S. P., Martin-Porter, E., Housley, M. P., Liu, L., Ganz, T. and Kagnoff, M. F. (2000). Regulation of human β-defensins by gastric epithelial cells in response to infection with Helicobacter pylori or stimulation with interleukin-1. Infect. Immun. 68, 5412-5415.
    • (2000) Infect. Immun , vol.68 , pp. 5412-5415
    • O'Neil, D.A.1    Cole, S.P.2    Martin-Porter, E.3    Housley, M.P.4    Liu, L.5    Ganz, T.6    Kagnoff, M.F.7
  • 32
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jornvall, H., Wigzell, H. and Gudmundsson, G. H. (2000). The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations. Blood 96, 3086-3093.
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3    Olsson, B.4    Idali, F.5    Lindbom, L.6    Kiessling, R.7    Jornvall, H.8    Wigzell, H.9    Gudmundsson, G.H.10
  • 33
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo, D., Skerlavaj, B., Bolognesi, M. and Gennaro, R. (1988). Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J Biol. Chem. 263, 9573-9575.
    • (1988) J Biol. Chem , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 34
    • 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., Eckmann, L., Leopard, J. D., Varki, N. and Kagnoff, M. F. (2002). 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) Infect. Immun , vol.70 , pp. 953-963
    • Hase, K.1    Eckmann, L.2    Leopard, J.D.3    Varki, N.4    Kagnoff, M.F.5
  • 35
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • Bals, R., Wang, X., Zasloff, M. and Wilson, J. M. (1998). The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc. Natl. Acad. Sci. USA 95, 9541-9546.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 36
    • 25444491974 scopus 로고    scopus 로고
    • Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens
    • Braff, M. H., Zaiou, M., Fierer, J., Nizet, V. and Gallo, R. L. (2005). Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens. Infect. Immun. 73, 6771-6781.
    • (2005) Infect. Immun , vol.73 , pp. 6771-6781
    • Braff, M.H.1    Zaiou, M.2    Fierer, J.3    Nizet, V.4    Gallo, R.L.5
  • 38
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins-a family of multifunctional antimicrobial peptides
    • Bals, R. and Wilson, J. M. (2003). Cathelicidins-a family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 60, 711-720.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 40
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson, D. J., Currie, A. J., Reid, G. S., Bowdish, D. M., MacDonald, K. L., Ma, R. C., Hancock, R. E. and Speert, D. P. (2004). The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J. Immunol. 172, 1146-1156.
    • (2004) J. Immunol , vol.172 , pp. 1146-1156
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.3    Bowdish, D.M.4    MacDonald, K.L.5    Ma, R.C.6    Hancock, R.E.7    Speert, D.P.8
  • 41
    • 0037340434 scopus 로고    scopus 로고
    • Angiogenins: A new class of microbicidal proteins involved in innate immunity
    • Hooper, L. V., Stappenbeck, T. S., Hong, C. V. and Gordon, J. I. (2003). Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nat. Immunol. 4, 269-273.
    • (2003) Nat. Immunol , vol.4 , pp. 269-273
    • Hooper, L.V.1    Stappenbeck, T.S.2    Hong, C.V.3    Gordon, J.I.4
  • 42
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder, J. and Schroder, J. M. (2002). RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277, 46779-46784.
    • (2002) J. Biol. Chem , vol.277 , pp. 46779-46784
    • Harder, J.1    Schroder, J.M.2
  • 43
    • 0028931427 scopus 로고
    • Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity
    • Rosenberg, H. F. (1995). Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity. J. Biol. Chem. 270, 7876-7881.
    • (1995) J. Biol. Chem , vol.270 , pp. 7876-7881
    • Rosenberg, H.F.1
  • 44
    • 33748039462 scopus 로고    scopus 로고
    • Symbiotic bacteria direct expression of an intestinal bactericidal lectin
    • Cash, H. L., Whitham, C. V., Behrendt, C. L. and Hooper, L. V. (2006). Symbiotic bacteria direct expression of an intestinal bactericidal lectin. Science 313, 1126-1130.
    • (2006) Science , vol.313 , pp. 1126-1130
    • Cash, H.L.1    Whitham, C.V.2    Behrendt, C.L.3    Hooper, L.V.4
  • 46
    • 0036840337 scopus 로고    scopus 로고
    • Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity
    • Dieckgraefe, B. K., Crimmins, D. L., Landt, V., Houchen, C., Anant, S., Porche-Sorbet, R. and Ladenson, J. H. (2002). Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity. J. Invest. Med. 50, 421-434.
    • (2002) J. Invest. Med , vol.50 , pp. 421-434
    • Dieckgraefe, B.K.1    Crimmins, D.L.2    Landt, V.3    Houchen, C.4    Anant, S.5    Porche-Sorbet, R.6    Ladenson, J.H.7
  • 47
    • 0031768678 scopus 로고    scopus 로고
    • Creating and maintaining the gastrointestinal ecosystem: What we know and need to know from gnotobiology
    • Falk, P. G., Hooper, L. V., Midtvedt, T. and Gordon, J. I. (1998). Creating and maintaining the gastrointestinal ecosystem: what we know and need to know from gnotobiology. Microbiol. Mol. Biol. Rev. 62, 1157-1170.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 1157-1170
    • Falk, P.G.1    Hooper, L.V.2    Midtvedt, T.3    Gordon, J.I.4
  • 49
    • 0035793372 scopus 로고    scopus 로고
    • Molecular analysis of commensal host-microbial relationships in the intestine
    • Hooper, L. V., Wong, M. H., Thelin, A., Hansson, L., Falk, P. G. and Gordon, J. I. (2001). Molecular analysis of commensal host-microbial relationships in the intestine. Science 291, 881-884.
    • (2001) Science , vol.291 , pp. 881-884
    • Hooper, L.V.1    Wong, M.H.2    Thelin, A.3    Hansson, L.4    Falk, P.G.5    Gordon, J.I.6
  • 50
    • 1542380052 scopus 로고    scopus 로고
    • Innate immunity and mucosal bacterial interactions in the intestine
    • Eckmann, L. (2004). Innate immunity and mucosal bacterial interactions in the intestine. Curr. Opin. Gastroenterol. 20, 82-88.
    • (2004) Curr. Opin. Gastroenterol , vol.20 , pp. 82-88
    • Eckmann, L.1
  • 55
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S. and Takeuchi, O. (2006). Pathogen recognition and innate immunity. Cell 124, 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 57
    • 0346881404 scopus 로고    scopus 로고
    • Innate immune response of oral and foreskin keratinocytes: Utilization of different signaling pathways by various bacterial species
    • Chung, W. O. and Dale, B. A. (2004). Innate immune response of oral and foreskin keratinocytes: utilization of different signaling pathways by various bacterial species. Infect. Immun. 72, 352-358.
    • (2004) Infect. Immun , vol.72 , pp. 352-358
    • Chung, W.O.1    Dale, B.A.2
  • 58
    • 34547762705 scopus 로고    scopus 로고
    • MyD88-mediated signals induce the bactericidal lectin RegIIIγ and protect mice against intestinal Listeria monocytogenes infection
    • Brandl, K., Plitas, G., Schnabl, B., Dematteo, R. P. and Pamer, E. G. (2007). MyD88-mediated signals induce the bactericidal lectin RegIIIγ and protect mice against intestinal Listeria monocytogenes infection. J. Exp. Med. 204, 1891-1900.
    • (2007) J. Exp. Med , vol.204 , pp. 1891-1900
    • Brandl, K.1    Plitas, G.2    Schnabl, B.3    Dematteo, R.P.4    Pamer, E.G.5
  • 59
    • 34447296425 scopus 로고    scopus 로고
    • Regulation of spontaneous intestinal tumorigenesis through the adaptor protein MyD88
    • Rakoff-Nahoum, S. and Medzhitov, R. (2007). Regulation of spontaneous intestinal tumorigenesis through the adaptor protein MyD88. Science 317, 124-127.
    • (2007) Science , vol.317 , pp. 124-127
    • Rakoff-Nahoum, S.1    Medzhitov, R.2
  • 61
    • 0038529691 scopus 로고    scopus 로고
    • Interactions of mouse Paneth cell α-defensins and α-defensin precursors with membranes. Prosegment inhibition of peptide association with biomimetic membranes
    • Satchell, D. P., Sheynis, T., Shirafuji, Y., Kolusheva, S., Ouellette, A. J. and Jelinek, R. (2003). Interactions of mouse Paneth cell α-defensins and α-defensin precursors with membranes. Prosegment inhibition of peptide association with biomimetic membranes. J. Biol. Chem. 278, 13838-13846.
    • (2003) J. Biol. Chem , vol.278 , pp. 13838-13846
    • Satchell, D.P.1    Sheynis, T.2    Shirafuji, Y.3    Kolusheva, S.4    Ouellette, A.J.5    Jelinek, R.6
  • 64
    • 0035128862 scopus 로고    scopus 로고
    • Human defensin 5 is stored in precursor form in normal Paneth cells and is expressed by some villous epithelial cells and by metaplastic Paneth cells in the colon in inflammatory bowel disease
    • Cunliffe, R. N., Rose, F. R., Keyte, J., Abberley, L., Chan, W. C. and Mahida, Y. R. (2001). Human defensin 5 is stored in precursor form in normal Paneth cells and is expressed by some villous epithelial cells and by metaplastic Paneth cells in the colon in inflammatory bowel disease. Gut 48, 176-185.
    • (2001) Gut , vol.48 , pp. 176-185
    • Cunliffe, R.N.1    Rose, F.R.2    Keyte, J.3    Abberley, L.4    Chan, W.C.5    Mahida, Y.R.6
  • 65
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S. and Borregaard, N. (2001). Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97, 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 66
  • 67
    • 0034252293 scopus 로고    scopus 로고
    • Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria
    • Ayabe, T., Satchell, D. P., Wilson, C. L., Parks, W. C., Selsted, M. E. and Ouellette, A. J. (2000). Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 1, 113-118.
    • (2000) Nat. Immunol , vol.1 , pp. 113-118
    • Ayabe, T.1    Satchell, D.P.2    Wilson, C.L.3    Parks, W.C.4    Selsted, M.E.5    Ouellette, A.J.6
  • 68
    • 0034938204 scopus 로고    scopus 로고
    • Intestinal microflora in human and experimental inflammatory bowel disease
    • Sartor, R. B. (2001). Intestinal microflora in human and experimental inflammatory bowel disease. Curr. Opin. Gastroenterol. 17, 324-330.
    • (2001) Curr. Opin. Gastroenterol , vol.17 , pp. 324-330
    • Sartor, R.B.1


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