메뉴 건너뛰기




Volumn 306, Issue , 2006, Pages 67-90

Host antimicrobial defence peptides in human disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; ANTIBIOTIC AGENT; BETA DEFENSIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; GRANULOCYTE COLONY STIMULATING FACTOR; INTERLEUKIN 8; LACTOFERRIN; LYSOZYME; MITOGEN ACTIVATED PROTEIN KINASE; TOLL LIKE RECEPTOR 2; TRANSMEMBRANE CONDUCTANCE REGULATOR; ANTIMICROBIAL CATIONIC PEPTIDE; CAP18 LIPOPOLYSACCHARIDE BINDING PROTEIN; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN; DEFENSIN; IMMUNOLOGIC FACTOR;

EID: 33748109943     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/3-540-29916-5_3     Document Type: Review
Times cited : (55)

References (112)
  • 5
    • 1042269503 scopus 로고    scopus 로고
    • Innate immunity in the lung: How epithelial cells fight against respiratory pathogens
    • Bals R, Hiemstra PS (2004) Innate immunity in the lung: how epithelial cells fight against respiratory pathogens. Eur Respir J 23:327-333
    • (2004) Eur Respir J , vol.23 , pp. 327-333
    • Bals, R.1    Hiemstra, P.S.2
  • 6
    • 0034914909 scopus 로고    scopus 로고
    • Salt-independent abnormality of antimicrobial activity in cystic fibrosis airway surface fluid
    • Bals R, Weiner DJ, Meegalla RL, Accurso F, Wilson JM (2001) Salt-independent abnormality of antimicrobial activity in cystic fibrosis airway surface fluid. Am J Respir Cell Mol Biol 25:21-25
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 21-25
    • Bals, R.1    Weiner, D.J.2    Meegalla, R.L.3    Accurso, F.4    Wilson, J.M.5
  • 7
    • 0033560645 scopus 로고    scopus 로고
    • Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model
    • Bals R, Weiner DJ, Meegalla RL, Wilson JM (1999) Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model. J Clin Invest 103:1113-1117
    • (1999) J Clin Invest , vol.103 , pp. 1113-1117
    • Bals, R.1    Weiner, D.J.2    Meegalla, R.L.3    Wilson, J.M.4
  • 10
    • 7444239122 scopus 로고    scopus 로고
    • The Paneth cell and the innate immune response
    • Bevins CL (2004) The Paneth cell and the innate immune response. Curr Opin Gastroenterol 20:572-580
    • (2004) Curr Opin Gastroenterol , vol.20 , pp. 572-580
    • Bevins, C.L.1
  • 12
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A (1993) Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect Immun 61:2978-2984
    • (1993) Infect Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 13
    • 1542724426 scopus 로고    scopus 로고
    • The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes
    • Bowdish DM, Davidson DJ, Speert DP, Hancock RE (2004) The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes. J Immunol 172:3758-3765
    • (2004) J Immunol , vol.172 , pp. 3758-3765
    • Bowdish, D.M.1    Davidson, D.J.2    Speert, D.P.3    Hancock, R.E.4
  • 16
    • 3843064497 scopus 로고    scopus 로고
    • A single-nucleotide polymorphism in the human beta-defensin 1 gene is associated with HIV-1 infection in Italian children
    • Braida L, Boniotto M, Pontillo A, Tovo PA, Amoroso A, Crovella S (2004) A single-nucleotide polymorphism in the human beta-defensin 1 gene is associated with HIV-1 infection in Italian children. Aids 18:1598-1600
    • (2004) Aids , vol.18 , pp. 1598-1600
    • Braida, L.1    Boniotto, M.2    Pontillo, A.3    Tovo, P.A.4    Amoroso, A.5    Crovella, S.6
  • 17
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA (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
    • 1642405248 scopus 로고    scopus 로고
    • Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen CI, Schaller-Bals S, Paul KP, Wahn U, Bals R (2004) Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. J Cyst Fibros 3:45-50
    • (2004) J Cyst Fibros , vol.3 , pp. 45-50
    • Chen, C.I.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 20
    • 0030038197 scopus 로고    scopus 로고
    • Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
    • Chertov O, Michiel DF, Xu L, Wang JM, Tani K, Murphy WJ, Longo DL, Taub DD, Oppenheim JJ (1996) Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J Biol Chem 271:2935-2940
    • (1996) J Biol Chem , vol.271 , pp. 2935-2940
    • Chertov, O.1    Michiel, D.F.2    Xu, L.3    Wang, J.M.4    Tani, K.5    Murphy, W.J.6    Longo, D.L.7    Taub, D.D.8    Oppenheim, J.J.9
  • 21
    • 0346881404 scopus 로고    scopus 로고
    • Innate immune response of oral and foreskin keratinocytes: Utilization of different signaling pathways by various bacterial species
    • Chung WO, Dale BA (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
  • 24
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson DJ, Currie AJ, Reid GS, Bowdish DM, MacDonald KL, Ma RC, Hancock RE, Speert DP (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
  • 25
    • 0142010657 scopus 로고    scopus 로고
    • Update on pathogenesis of cystic fibrosis lung disease
    • Donaldson SH, Boucher RC (2003) Update on pathogenesis of cystic fibrosis lung disease. Curr Opin Pulm Med 9:486-491
    • (2003) Curr Opin Pulm Med , vol.9 , pp. 486-491
    • Donaldson, S.H.1    Boucher, R.C.2
  • 27
    • 0038142315 scopus 로고    scopus 로고
    • What is the real role of antimicrobial polypeptides that can mediate several other inflammatory responses?
    • Elsbach P (2003) What is the real role of antimicrobial polypeptides that can mediate several other inflammatory responses? J Clin Invest 111:1643-1645
    • (2003) J Clin Invest , vol.111 , pp. 1643-1645
    • Elsbach, P.1
  • 28
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner A, Duncan M, Gavrilin M, Wewers MD (2004) A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J Immunol 172:4987-4994
    • (2004) J Immunol , vol.172 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 29
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm M, Agerberth B, Ahangari G, Stahle-Backdahl M, Liden S, Wigzell H, Gudmundsson GH (1997) The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J Biol Chem 272:15258-15263
    • (1997) J Biol Chem , vol.272 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 30
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T (2003) Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 3:710-720
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 31
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz T, Lehrer RI (1997) Antimicrobial peptides of leukocytes. Curr Opin Hematol 4:53-58
    • (1997) Curr Opin Hematol , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 32
    • 0023812897 scopus 로고
    • Microbicidal/cytotoxic proteins of neutrophils are deficient in two disorders: Chediak-Higashi syndrome and "specific" granule deficiency
    • Ganz T, Metcalf JA, Gallin JI, Boxer LA, Lehrer RI (1988) Microbicidal/cytotoxic proteins of neutrophils are deficient in two disorders: Chediak-Higashi syndrome and "specific" granule deficiency. J Clin Invest 82:552-556
    • (1988) J Clin Invest , vol.82 , pp. 552-556
    • Ganz, T.1    Metcalf, J.A.2    Gallin, J.I.3    Boxer, L.A.4    Lehrer, R.I.5
  • 34
    • 0036252094 scopus 로고    scopus 로고
    • Pro-rich antimicrobial peptides from animals: Structure, biological functions and mechanism of action
    • Gennaro R, Zanetti M, Benincasa M, Podda E, Miani M (2002) Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr Pharm Des 8:763-778
    • (2002) Curr Pharm Des , vol.8 , pp. 763-778
    • Gennaro, R.1    Zanetti, M.2    Benincasa, M.3    Podda, E.4    Miani, M.5
  • 36
    • 0345303939 scopus 로고    scopus 로고
    • Lessons from Nod2 studies: Towards a link between Crohn's disease and bacterial sensing
    • Girardin SE, Hugot JP, Sansonetti PJ (2003) Lessons from Nod2 studies: towards a link between Crohn's disease and bacterial sensing. Trends Immunol 24:652-658
    • (2003) Trends Immunol , vol.24 , pp. 652-658
    • Girardin, S.E.1    Hugot, J.P.2    Sansonetti, P.J.3
  • 38
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • Gudmundsson GH, Agerberth B (1999) Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J Immunol Methods 232:45-54
    • (1999) J Immunol Methods , vol.232 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 40
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock RE, Scott MG (2000) The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci U S A 97:8856-8861
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 41
    • 16844370194 scopus 로고    scopus 로고
    • Psoriatic scales: A promising source for the isolation of human skin-derived antimicrobial proteins
    • Harder J, Schroder JM (2005) Psoriatic scales: a promising source for the isolation of human skin-derived antimicrobial proteins. J Leukoc Biol 77:476-486
    • (2005) J Leukoc Biol , vol.77 , pp. 476-486
    • Harder, J.1    Schroder, J.M.2
  • 43
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic
    • Harder J, Bartels J, Christophers E, Schroder JM (2001) Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J Biol Chem 276:5707-5713
    • (2001) J Biol Chem , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 44
    • 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 JD, Varki N, Kagnoff MF (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
  • 46
    • 0346366980 scopus 로고    scopus 로고
    • Activation of Toll-like receptor 2 on human tracheobronchial epithelial cells induces the antimicrobial peptide human beta defensin-2
    • Hertz CJ, Wu Q, Porter EM, Zhang YJ, Weismuller KH, Godowski PJ, Ganz T, Randell SH, Modlin RL (2003) Activation of Toll-like receptor 2 on human tracheobronchial epithelial cells induces the antimicrobial peptide human beta defensin-2. J Immunol 171:6820-6826
    • (2003) J Immunol , vol.171 , pp. 6820-6826
    • Hertz, C.J.1    Wu, Q.2    Porter, E.M.3    Zhang, Y.J.4    Weismuller, K.H.5    Godowski, P.J.6    Ganz, T.7    Randell, S.H.8    Modlin, R.L.9
  • 49
    • 0142157000 scopus 로고    scopus 로고
    • Intracellular recognition of lipopolysaccharide by toll-like receptor 4 in intestinal epithelial cells
    • Hornef MW, Normark BH, Vandewalle A, Normark S (2003) Intracellular recognition of lipopolysaccharide by toll-like receptor 4 in intestinal epithelial cells. J Exp Med 198:1225-1235
    • (2003) J Exp Med , vol.198 , pp. 1225-1235
    • Hornef, M.W.1    Normark, B.H.2    Vandewalle, A.3    Normark, S.4
  • 51
    • 10244222822 scopus 로고    scopus 로고
    • Correlation of HDEFB1 polymorphism and susceptibility to chronic obstructive pulmonary disease in Chinese Han population
    • Hu RC, Xu YJ, Zhang ZX, Ni W, Chen SX (2004) Correlation of HDEFB1 polymorphism and susceptibility to chronic obstructive pulmonary disease in Chinese Han population. Chin Med J (Engl) 117:1637-1641
    • (2004) Chin Med J (Engl) , vol.117 , pp. 1637-1641
    • Hu, R.C.1    Xu, Y.J.2    Zhang, Z.X.3    Ni, W.4    Chen, S.X.5
  • 53
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam D, Bandholtz L, Nilsson J, Wigzell H, Christensson B, Agerberth B, Gudmundsson G (2001) Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat Med 7:180-185
    • (2001) Nat Med , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 54
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B (1998) Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J Biol Chem 273:3718-3724
    • (1998) J Biol Chem , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 55
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones DE, Bevins CL (1992) Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem 267:23216-23225
    • (1992) J Biol Chem , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 56
    • 0027390031 scopus 로고
    • Defensin-6 mRNA in human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel
    • Jones DE, Bevins CL (1993) Defensin-6 mRNA in human Paneth cells: implications for antimicrobial peptides in host defense of the human bowel. FEBS Lett 315:187-192
    • (1993) FEBS Lett , vol.315 , pp. 187-192
    • Jones, D.E.1    Bevins, C.L.2
  • 57
    • 1642267482 scopus 로고    scopus 로고
    • Histatins: Antimicrobial peptides with therapeutic potential
    • Kavanagh K, Dowd S (2004) Histatins: antimicrobial peptides with therapeutic potential. J Pharm Pharmacol 56:285-289
    • (2004) J Pharm Pharmacol , vol.56 , pp. 285-289
    • Kavanagh, K.1    Dowd, S.2
  • 60
    • 0034020351 scopus 로고    scopus 로고
    • Inducible expression of human beta-defensin 2 by Fusobacterium nucleatum in oral epithelial cells: Multiple signaling pathways and role of commensal bacteria in innateimmunity and the epithelial barrier
    • Krisanaprakornkit S, Kimball JR, Weinberg A, Darveau RP, Bainbridge BW, Dale BA (2000) Inducible expression of human beta-defensin 2 by Fusobacterium nucleatum in oral epithelial cells: multiple signaling pathways and role of commensal bacteria in innateimmunity and the epithelial barrier. Infect Immun 68:2907-2915
    • (2000) Infect Immun , vol.68 , pp. 2907-2915
    • Krisanaprakornkit, S.1    Kimball, J.R.2    Weinberg, A.3    Darveau, R.P.4    Bainbridge, B.W.5    Dale, B.A.6
  • 62
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer RI, Lichtenstein AK, Ganz T (1993) Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu Rev Immunol 11:105-128
    • (1993) Annu Rev Immunol , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 65
    • 0036259887 scopus 로고    scopus 로고
    • Characterization of the mouse beta defensin 1, Defb1, mutant mouse model
    • Morrison G, Kilanowski F, Davidson D, Dorin J (2002) Characterization of the mouse beta defensin 1, Defb1, mutant mouse model. Infect Immun 70:3053-3060
    • (2002) Infect Immun , vol.70 , pp. 3053-3060
    • Morrison, G.1    Kilanowski, F.2    Davidson, D.3    Dorin, J.4
  • 68
    • 0036891933 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva
    • Murakami M, Ohtake T, Dorschner RA, Gallo RL (2002) Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. J Dent Res 81:845-850
    • (2002) J Dent Res , vol.81 , pp. 845-850
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.A.3    Gallo, R.L.4
  • 69
    • 1342282224 scopus 로고    scopus 로고
    • Post-secretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL (2004) Post-secretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J Immunol 172:3070-3077
    • (2004) J Immunol , vol.172 , pp. 3070-3077
    • Murakami, M.1    Lopez-Garcia, B.2    Braff, M.3    Dorschner, R.A.4    Gallo, R.L.5
  • 71
    • 14944341462 scopus 로고    scopus 로고
    • Innate host defense of the lung: Effects of lung-lining fluid pH
    • Ng AW, Bidani A, Heming TA (2004) Innate host defense of the lung: effects of lung-lining fluid pH. Lung 182:297-317
    • (2004) Lung , vol.182 , pp. 297-317
    • AW, N.1    Bidani, A.2    Heming, T.A.3
  • 74
    • 0033855720 scopus 로고    scopus 로고
    • Regulation of human beta-defensins by gastric epithelial cells in response to infection with Helicobacter pylori or stimulation with interleukin-1
    • O'Neil DA, Cole SP, Martin-Porter E, Housley MP, Liu L, Ganz T, Kagnoff MF (2000) Regulation of human beta-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
  • 77
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linearamphipathic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y (1998)Mode of action of linearamphipathic alpha-helical antimicrobial peptides. Biopolymers 47:451-463
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 78
    • 1842453218 scopus 로고    scopus 로고
    • Defensin-mediated innate immunity in the small intestine
    • Ouellette AJ (2004) Defensin-mediated innate immunity in the small intestine. Best Pract Res Clin Gastroenterol 18:405-419
    • (2004) Best Pract Res Clin Gastroenterol , vol.18 , pp. 405-419
    • Ouellette, A.J.1
  • 79
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • Putsep K, Carlsson G, Boman HG, Andersson M (2002) Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360:1144-1149
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 81
    • 0037372643 scopus 로고    scopus 로고
    • Enteric salmonella infection inhibits Paneth cell antimicrobial peptide expression
    • Salzman NH, Chou MM, de Jong H, Liu L, Porter EM and Paterson Y (2003b) Enteric salmonella infection inhibits Paneth cell antimicrobial peptide expression. Infect Immun 71:1109-1115
    • (2003) Infect Immun , vol.71 , pp. 1109-1115
    • Salzman, N.H.1    Chou, M.M.2    de Jong, H.3    Liu, L.4    Porter, E.M.5    Paterson, Y.6
  • 82
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman NH, Ghosh D, Huttner KM, Paterson Y, Bevins CL (2003a) 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
  • 84
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen A, Frick IM, Andersson E, Tapper H, Bjorck L (2002) Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol Microbiol 46:157-168
    • (2002) Mol Microbiol , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 86
    • 0026739037 scopus 로고
    • Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins
    • Scocchi M, Skerlavaj B, Romeo D, Gennaro R (1992) Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins. Eur J Biochem 209:589-595
    • (1992) Eur J Biochem , vol.209 , pp. 589-595
    • Scocchi, M.1    Skerlavaj, B.2    Romeo, D.3    Gennaro, R.4
  • 87
    • 4444341077 scopus 로고    scopus 로고
    • Theta-defensins: Cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins
    • Selsted ME (2004) Theta-defensins: cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins. Curr Protein Pept Sci 5:365-371
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 365-371
    • Selsted, M.E.1
  • 88
    • 0021032178 scopus 로고
    • Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages
    • Selsted ME, Brown DM, DeLange RJ, Lehrer RI (1983) Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J Biol Chem 258:14485-14489
    • (1983) J Biol Chem , vol.258 , pp. 14485-14489
    • Selsted, M.E.1    Brown, D.M.2    DeLange, R.J.3    Lehrer, R.I.4
  • 89
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer WM, Qu X, Waring AJ, Lehrer RI (1998) Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc Natl Acad Sci U S A 95:1829-1833
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 90
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai Y (1995) Molecular recognition between membrane-spanning polypeptides. Trends Biochem Sci 20:460-464
    • (1995) Trends Biochem Sci , vol.20 , pp. 460-464
    • Shai, Y.1
  • 92
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith JJ, Travis SM, Greenberg EP, Welsh MJ (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85:229-236
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 93
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, Hiemstra PS, 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
  • 94
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 95
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME (1999) A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 286:498-502
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 96
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa GS, Aarbiou J, Ninaber DK, Drijfhout JW, Sorensen OE, Borregaard N, Rabe KF, Hiemstra PS (2003) The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J Immunol 171:6690-6696
    • (2003) J Immunol , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3    Drijfhout, J.W.4    Sorensen, O.E.5    Borregaard, N.6    Rabe, K.F.7    Hiemstra, P.S.8
  • 97
    • 0036479317 scopus 로고    scopus 로고
    • Homodimeric theta-defensins from rhesus macaque leukocytes: Isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides
    • Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME (2002) Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. J Biol Chem 277:3079-3084
    • (2002) J Biol Chem , vol.277 , pp. 3079-3084
    • Tran, D.1    Tran, P.A.2    Tang, Y.Q.3    Yuan, J.4    Cole, T.5    Selsted, M.E.6
  • 98
    • 0035142621 scopus 로고    scopus 로고
    • Antimicrobial peptides and proteins in the innate defense of the airway surface
    • Travis SM, Singh PK, Welsh MJ (2001) Antimicrobial peptides and proteins in the innate defense of the airway surface. Curr Opin Immunol 13:89-95
    • (2001) Curr Opin Immunol , vol.13 , pp. 89-95
    • Travis, S.M.1    Singh, P.K.2    Welsh, M.J.3
  • 101
    • 0032313341 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides: Review and significance for oral applications
    • Weinberg A, Krisanaprakornkit S, Dale BA (1998) Epithelial antimicrobial peptides: review and significance for oral applications. Crit Rev Oral Biol Med 9:399-414
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 399-414
    • Weinberg, A.1    Krisanaprakornkit, S.2    Dale, B.A.3
  • 104
    • 0033844287 scopus 로고    scopus 로고
    • Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells
    • Yang D, Chen Q, Chertov O, Oppenheim JJ (2000a) Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells. J Leukoc Biol 68:9-14
    • (2000) J Leukoc Biol , vol.68 , pp. 9-14
    • Yang, D.1    Chen, Q.2    Chertov, O.3    Oppenheim, J.J.4
  • 105
    • 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
    • Yang D, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, Oppenheim JJ, Chertov O (2000b) 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) J Exp Med , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 106
    • 0034960109 scopus 로고    scopus 로고
    • The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity
    • Yang D, Chertov O, Oppenheim JJ (2001)The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity. Cell Mol Life Sci 58:978-989
    • (2001) Cell Mol Life Sci , vol.58 , pp. 978-989
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 108
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence
    • Zaiou M, Nizet V, Gallo RL (2003) Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J Invest Dermatol 120:810-816
    • (2003) J Invest Dermatol , vol.120 , pp. 810-816
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 109
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M (2004) Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 75:39-48
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 110
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D (1995) Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett 374:1-5
    • (1995) FEBS Lett , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 111
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A 84:5449-5453
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 112
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.