메뉴 건너뛰기




Volumn 30, Issue 3, 2009, Pages 131-141

AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 61349169039     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2008.12.003     Document Type: Review
Times cited : (1006)

References (116)
  • 1
    • 33748094122 scopus 로고    scopus 로고
    • Antimicrobial peptides: an essential component of the skin defensive barrier
    • Braff M.H., and Gallo R.L. Antimicrobial peptides: an essential component of the skin defensive barrier. Curr. Top. Microbiol. Immunol. 306 (2006) 91-110
    • (2006) Curr. Top. Microbiol. Immunol. , vol.306 , pp. 91-110
    • Braff, M.H.1    Gallo, R.L.2
  • 2
    • 52449125862 scopus 로고    scopus 로고
    • Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics
    • Wang Y., et al. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS One 3 (2008) e3217
    • (2008) PLoS One , vol.3
    • Wang, Y.1
  • 3
    • 52049112301 scopus 로고    scopus 로고
    • Identification and characterization of novel reptile cathelicidins from elapid snakes
    • Zhao H., et al. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides 29 (2008) 1685-1691
    • (2008) Peptides , vol.29 , pp. 1685-1691
    • Zhao, H.1
  • 4
    • 20444488832 scopus 로고    scopus 로고
    • CMAP27, a novel chicken cathelicidin-like antimicrobial protein
    • van Dijk A., et al. CMAP27, a novel chicken cathelicidin-like antimicrobial protein. Vet. Immunol. Immunopathol. 106 (2005) 321-327
    • (2005) Vet. Immunol. Immunopathol. , vol.106 , pp. 321-327
    • van Dijk, A.1
  • 5
    • 1042290514 scopus 로고    scopus 로고
    • Hagfish intestinal antimicrobial peptides are ancient cathelicidins
    • Uzzell T., et al. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides 24 (2003) 1655-1667
    • (2003) Peptides , vol.24 , pp. 1655-1667
    • Uzzell, T.1
  • 6
    • 0028844134 scopus 로고
    • Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M., et al. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374 (1995) 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1
  • 7
    • 0037039376 scopus 로고    scopus 로고
    • Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor
    • Sanchez J.F., et al. Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor. Biochemistry 41 (2002) 21-30
    • (2002) Biochemistry , vol.41 , pp. 21-30
    • Sanchez, J.F.1
  • 8
    • 0030057777 scopus 로고    scopus 로고
    • Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides
    • Storici P., et al. Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. Eur. J. Biochem. 238 (1996) 769-776
    • (1996) Eur. J. Biochem. , vol.238 , pp. 769-776
    • Storici, P.1
  • 9
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence
    • Zaiou M., et al. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J. Invest. Dermatol. 120 (2003) 810-816
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 810-816
    • Zaiou, M.1
  • 10
    • 0030805339 scopus 로고    scopus 로고
    • An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma
    • Sorensen O., et al. An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma. J. Immunol. Methods 206 (1997) 53-59
    • (1997) J. Immunol. Methods , vol.206 , pp. 53-59
    • Sorensen, O.1
  • 11
    • 11144320719 scopus 로고    scopus 로고
    • Expression and secretion of cathelicidin antimicrobial peptides in murine mammary glands and human milk
    • Murakami M., et al. Expression and secretion of cathelicidin antimicrobial peptides in murine mammary glands and human milk. Pediatr. Res. 57 (2005) 10-15
    • (2005) Pediatr. Res. , vol.57 , pp. 10-15
    • Murakami, M.1
  • 12
    • 1342282224 scopus 로고    scopus 로고
    • Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami M., et al. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J. Immunol. 172 (2004) 3070-3077
    • (2004) J. Immunol. , vol.172 , pp. 3070-3077
    • Murakami, M.1
  • 13
    • 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., et al. 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. U. S. A. 95 (1998) 9541-9546
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9541-9546
    • Bals, R.1
  • 14
    • 0033918174 scopus 로고    scopus 로고
    • The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa
    • Malm J., et al. The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa. Infect. Immun. 68 (2000) 4297-4302
    • (2000) Infect. Immun. , vol.68 , pp. 4297-4302
    • Malm, J.1
  • 15
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75 (2004) 39-48
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 16
    • 0035163451 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds
    • Cole A.M., et al. Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 97 (2001) 297-304
    • (2001) Blood , vol.97 , pp. 297-304
    • Cole, A.M.1
  • 17
    • 33750139445 scopus 로고    scopus 로고
    • Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin
    • Yamasaki K., et al. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. FASEB J. 20 (2006) 2068-2080
    • (2006) FASEB J. , vol.20 , pp. 2068-2080
    • Yamasaki, K.1
  • 18
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen O., et al. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90 (1997) 2796-2803
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1
  • 19
    • 33646597266 scopus 로고    scopus 로고
    • Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region
    • Li X., et al. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J. Am. Chem. Soc. 128 (2006) 5776-5785
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5776-5785
    • Li, X.1
  • 20
    • 22144457975 scopus 로고    scopus 로고
    • Cutaneous defense mechanisms by antimicrobial peptides
    • Braff M.H., et al. Cutaneous defense mechanisms by antimicrobial peptides. J. Invest. Dermatol. 125 (2005) 9-13
    • (2005) J. Invest. Dermatol. , vol.125 , pp. 9-13
    • Braff, M.H.1
  • 21
    • 48149089791 scopus 로고    scopus 로고
    • Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor?
    • Zhu S. Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor?. Trends Microbiol 16 (2008) 353-360
    • (2008) Trends Microbiol , vol.16 , pp. 353-360
    • Zhu, S.1
  • 22
    • 0036040263 scopus 로고    scopus 로고
    • Expression of beta-defensin 1 and 2 mRNA by human monocytes, macrophages and dendritic cells
    • Duits L.A., et al. Expression of beta-defensin 1 and 2 mRNA by human monocytes, macrophages and dendritic cells. Immunology 106 (2002) 517-525
    • (2002) Immunology , vol.106 , pp. 517-525
    • Duits, L.A.1
  • 23
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson C.L., et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 286 (1999) 113-117
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1
  • 24
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang D., et al. Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22 (2004) 181-215
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 181-215
    • Yang, D.1
  • 25
    • 38749117873 scopus 로고    scopus 로고
    • Developmental switch of intestinal antimicrobial peptide expression
    • Menard S., et al. Developmental switch of intestinal antimicrobial peptide expression. J. Exp. Med. 205 (2008) 183-193
    • (2008) J. Exp. Med. , vol.205 , pp. 183-193
    • Menard, S.1
  • 26
    • 0035793879 scopus 로고    scopus 로고
    • An antimicrobial peptide gene found in the male reproductive system of rats
    • Li P., et al. An antimicrobial peptide gene found in the male reproductive system of rats. Science 291 (2001) 1783-1785
    • (2001) Science , vol.291 , pp. 1783-1785
    • Li, P.1
  • 27
    • 2342666235 scopus 로고    scopus 로고
    • An epididymis-specific beta-defensin is important for the initiation of sperm maturation
    • Zhou C.X., et al. An epididymis-specific beta-defensin is important for the initiation of sperm maturation. Nat. Cell Biol. 6 (2004) 458-464
    • (2004) Nat. Cell Biol. , vol.6 , pp. 458-464
    • Zhou, C.X.1
  • 28
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted M.E., and Ouellette A.J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6 (2005) 551-557
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 29
    • 33645046361 scopus 로고    scopus 로고
    • Sodium butyrate up-regulates cathelicidin gene expression via activator protein-1 and histone acetylation at the promoter region in a human lung epithelial cell line, EBC-1
    • Kida Y., et al. Sodium butyrate up-regulates cathelicidin gene expression via activator protein-1 and histone acetylation at the promoter region in a human lung epithelial cell line, EBC-1. Mol. Immunol. 43 (2006) 1972-1981
    • (2006) Mol. Immunol. , vol.43 , pp. 1972-1981
    • Kida, Y.1
  • 30
    • 3142592392 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells
    • Schauber J., et al. Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells. Mol. Immunol. 41 (2004) 847-854
    • (2004) Mol. Immunol. , vol.41 , pp. 847-854
    • Schauber, J.1
  • 31
    • 4344665018 scopus 로고    scopus 로고
    • Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression
    • Wang T.T., et al. Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression. J. Immunol. 173 (2004) 2909-2912
    • (2004) J. Immunol. , vol.173 , pp. 2909-2912
    • Wang, T.T.1
  • 32
    • 21744438757 scopus 로고    scopus 로고
    • Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3
    • Gombart A.F., et al. Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB J. 19 (2005) 1067-1077
    • (2005) FASEB J. , vol.19 , pp. 1067-1077
    • Gombart, A.F.1
  • 33
    • 18244394526 scopus 로고    scopus 로고
    • Vitamin D induces the antimicrobial protein hCAP18 in human skin
    • Weber G., et al. Vitamin D induces the antimicrobial protein hCAP18 in human skin. J. Invest. Dermatol. 124 (2005) 1080-1082
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 1080-1082
    • Weber, G.1
  • 34
    • 40649127503 scopus 로고    scopus 로고
    • Histone acetylation in keratinocytes enables control of the expression of cathelicidin and CD14 by 1,25-dihydroxyvitamin D3
    • Schauber J., et al. Histone acetylation in keratinocytes enables control of the expression of cathelicidin and CD14 by 1,25-dihydroxyvitamin D3. J. Invest. Dermatol. 128 (2008) 816-824
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 816-824
    • Schauber, J.1
  • 35
    • 33847220444 scopus 로고    scopus 로고
    • Injury enhances TLR2 function and antimicrobial peptide expression through a vitamin D-dependent mechanism
    • Schauber J., et al. Injury enhances TLR2 function and antimicrobial peptide expression through a vitamin D-dependent mechanism. J. Clin. Invest. 117 (2007) 803-811
    • (2007) J. Clin. Invest. , vol.117 , pp. 803-811
    • Schauber, J.1
  • 36
    • 33645224419 scopus 로고    scopus 로고
    • Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response
    • Liu P.T., et al. Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response. Science 311 (2006) 1770-1773
    • (2006) Science , vol.311 , pp. 1770-1773
    • Liu, P.T.1
  • 37
    • 36048989909 scopus 로고    scopus 로고
    • Psychological stress downregulates epidermal antimicrobial peptide expression and increases severity of cutaneous infections in mice
    • Aberg K.M., et al. Psychological stress downregulates epidermal antimicrobial peptide expression and increases severity of cutaneous infections in mice. J. Clin. Invest. 117 (2007) 3339-3349
    • (2007) J. Clin. Invest. , vol.117 , pp. 3339-3349
    • Aberg, K.M.1
  • 38
    • 35848930094 scopus 로고    scopus 로고
    • In vitro activity of human beta-defensin 2 against Pseudomonas aeruginosa in the presence of tear fluid
    • Huang L.C., et al. In vitro activity of human beta-defensin 2 against Pseudomonas aeruginosa in the presence of tear fluid. Antimicrob. Agents Chemother. 51 (2007) 3853-3860
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3853-3860
    • Huang, L.C.1
  • 39
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer R.I., and Ganz T. Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11 (1999) 23-27
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 40
    • 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 (2001) 454-457
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1
  • 41
    • 14844351540 scopus 로고    scopus 로고
    • Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection
    • Lee P.H., et al. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 3750-3755
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3750-3755
    • Lee, P.H.1
  • 42
    • 33646482761 scopus 로고    scopus 로고
    • Cathelicidin deficiency predisposes to eczema herpeticum
    • Howell M.D., et al. Cathelicidin deficiency predisposes to eczema herpeticum. J. Allergy Clin. Immunol. 117 (2006) 836-841
    • (2006) J. Allergy Clin. Immunol. , vol.117 , pp. 836-841
    • Howell, M.D.1
  • 43
    • 33744986714 scopus 로고    scopus 로고
    • The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection
    • Chromek M., et al. The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Nat. Med. 12 (2006) 636-641
    • (2006) Nat. Med. , vol.12 , pp. 636-641
    • Chromek, M.1
  • 44
    • 1642484970 scopus 로고    scopus 로고
    • Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum
    • Howell M.D., et al. Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum. J. Immunol. 172 (2004) 1763-1767
    • (2004) J. Immunol. , vol.172 , pp. 1763-1767
    • Howell, M.D.1
  • 45
    • 0036259798 scopus 로고    scopus 로고
    • beta-Defensin 1 contributes to pulmonary innate immunity in mice
    • Moser C., et al. beta-Defensin 1 contributes to pulmonary innate immunity in mice. Infect. Immun. 70 (2002) 3068-3072
    • (2002) Infect. Immun. , vol.70 , pp. 3068-3072
    • Moser, C.1
  • 46
    • 0036259887 scopus 로고    scopus 로고
    • Characterization of the mouse beta defensin 1, Defb1, mutant mouse model
    • Morrison G., et al. Characterization of the mouse beta defensin 1, Defb1, mutant mouse model. Infect. Immun. 70 (2002) 3053-3060
    • (2002) Infect. Immun. , vol.70 , pp. 3053-3060
    • Morrison, G.1
  • 47
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 (2005) 238-250
    • (2005) Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 48
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 49
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 50
    • 0023644485 scopus 로고
    • Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly)
    • Nakajima Y., et al. Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly). J. Biol. Chem. 262 (1987) 1665-1669
    • (1987) J. Biol. Chem. , vol.262 , pp. 1665-1669
    • Nakajima, Y.1
  • 51
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462 (1999) 1-10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 52
    • 0033529627 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma
    • Sorensen O., et al. The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma. J. Biol. Chem. 274 (1999) 22445-22451
    • (1999) J. Biol. Chem. , vol.274 , pp. 22445-22451
    • Sorensen, O.1
  • 53
    • 37249076371 scopus 로고    scopus 로고
    • Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3
    • Maisetta G., et al. Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3. Peptides 29 (2008) 1-6
    • (2008) Peptides , vol.29 , pp. 1-6
    • Maisetta, G.1
  • 54
    • 30744475282 scopus 로고    scopus 로고
    • The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides
    • Dorschner R.A., et al. The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides. FASEB J. 20 (2006) 35-42
    • (2006) FASEB J. , vol.20 , pp. 35-42
    • Dorschner, R.A.1
  • 55
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J., et al. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273 (1998) 3718-3724
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1
  • 56
    • 34848838572 scopus 로고    scopus 로고
    • Functional analysis of the host defense peptide Human Beta Defensin-1: new insight into its potential role in cancer
    • Bullard R.S., et al. Functional analysis of the host defense peptide Human Beta Defensin-1: new insight into its potential role in cancer. Mol. Immunol. 45 (2008) 839-848
    • (2008) Mol. Immunol. , vol.45 , pp. 839-848
    • Bullard, R.S.1
  • 57
    • 53049088890 scopus 로고    scopus 로고
    • Tumors sound the alarmin(s)
    • Coffelt S.B., and Scandurro A.B. Tumors sound the alarmin(s). Cancer Res. 68 (2008) 6482-6485
    • (2008) Cancer Res. , vol.68 , pp. 6482-6485
    • Coffelt, S.B.1    Scandurro, A.B.2
  • 58
    • 33749036894 scopus 로고    scopus 로고
    • Human beta-defensin-1, a potential chromosome 8p tumor suppressor: control of transcription and induction of apoptosis in renal cell carcinoma
    • Sun C.Q., et al. Human beta-defensin-1, a potential chromosome 8p tumor suppressor: control of transcription and induction of apoptosis in renal cell carcinoma. Cancer Res. 66 (2006) 8542-8549
    • (2006) Cancer Res. , vol.66 , pp. 8542-8549
    • Sun, C.Q.1
  • 59
    • 42649142893 scopus 로고    scopus 로고
    • The role of the multifunctional peptide LL-37 in host defense
    • Kai-Larsen Y., and Agerberth B. The role of the multifunctional peptide LL-37 in host defense. Front. Biosci. 13 (2008) 3760-3767
    • (2008) Front. Biosci. , vol.13 , pp. 3760-3767
    • Kai-Larsen, Y.1    Agerberth, B.2
  • 60
    • 0034946907 scopus 로고    scopus 로고
    • Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus
    • Dorschner R.A., et al. Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J. Invest. Dermatol. 117 (2001) 91-97
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 91-97
    • Dorschner, R.A.1
  • 61
    • 0024797674 scopus 로고
    • Monocyte-chemotactic activity of defensins from human neutrophils
    • Territo M.C., et al. Monocyte-chemotactic activity of defensins from human neutrophils. J. Clin. Invest. 84 (1989) 2017-2020
    • (1989) J. Clin. Invest. , vol.84 , pp. 2017-2020
    • Territo, M.C.1
  • 62
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: more than just microbicidal
    • Yang D., et al. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23 (2002) 291-296
    • (2002) Trends Immunol. , vol.23 , pp. 291-296
    • Yang, D.1
  • 63
    • 0036208192 scopus 로고    scopus 로고
    • Epithelial cell-derived human beta-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase C-dependent pathway
    • Niyonsaba F., et al. Epithelial cell-derived human beta-defensin-2 acts as a chemotaxin for mast cells through a pertussis toxin-sensitive and phospholipase C-dependent pathway. Int. Immunol. 14 (2002) 421-426
    • (2002) Int. Immunol. , vol.14 , pp. 421-426
    • Niyonsaba, F.1
  • 64
    • 0034998629 scopus 로고    scopus 로고
    • Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37)
    • Yang D., et al. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J. Leukoc. Biol. 69 (2001) 691-697
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 691-697
    • Yang, D.1
  • 65
    • 0033569408 scopus 로고    scopus 로고
    • Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6
    • Yang D., et al. Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. Science 286 (1999) 525-528
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1
  • 66
    • 0042808526 scopus 로고    scopus 로고
    • Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3
    • Wu Z., et al. Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8880-8885
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8880-8885
    • Wu, Z.1
  • 67
    • 43749116000 scopus 로고    scopus 로고
    • Analysis and separation of residues important for the chemoattractant and antimicrobial activities of beta-defensin 3
    • Taylor K., et al. Analysis and separation of residues important for the chemoattractant and antimicrobial activities of beta-defensin 3. J. Biol. Chem. 283 (2008) 6631-6639
    • (2008) J. Biol. Chem. , vol.283 , pp. 6631-6639
    • Taylor, K.1
  • 68
    • 34548772992 scopus 로고    scopus 로고
    • beta-Defensins chemoattract macrophages and mast cells but not lymphocytes and dendritic cells: CCR6 is not involved
    • Soruri A., et al. beta-Defensins chemoattract macrophages and mast cells but not lymphocytes and dendritic cells: CCR6 is not involved. Eur. J. Immunol. 37 (2007) 2474-2486
    • (2007) Eur. J. Immunol. , vol.37 , pp. 2474-2486
    • Soruri, A.1
  • 69
    • 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., 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 (2000) 1069-1074
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • Yang, D.1
  • 70
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K., et al. Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J. Immunol. 174 (2005) 6257-6265
    • (2005) J. Immunol. , vol.174 , pp. 6257-6265
    • Kurosaka, K.1
  • 71
    • 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., et al. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J. Immunol. 172 (2004) 4987-4994
    • (2004) J. Immunol. , vol.172 , pp. 4987-4994
    • Elssner, A.1
  • 72
    • 38849088077 scopus 로고    scopus 로고
    • Host defense peptide LL-37, in synergy with inflammatory mediator IL-1beta, augments immune responses by multiple pathways
    • Yu J., et al. Host defense peptide LL-37, in synergy with inflammatory mediator IL-1beta, augments immune responses by multiple pathways. J. Immunol. 179 (2007) 7684-7691
    • (2007) J. Immunol. , vol.179 , pp. 7684-7691
    • Yu, J.1
  • 73
    • 36749042671 scopus 로고    scopus 로고
    • Human -defensin-3 activates professional antigen-presenting cells via Toll-like receptors 1 and 2
    • Funderburg N., et al. Human -defensin-3 activates professional antigen-presenting cells via Toll-like receptors 1 and 2. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 18631-18635
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18631-18635
    • Funderburg, N.1
  • 74
    • 22544457464 scopus 로고    scopus 로고
    • The human beta-defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes
    • Niyonsaba F., et al. The human beta-defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes. J. Immunol. 175 (2005) 1776-1784
    • (2005) J. Immunol. , vol.175 , pp. 1776-1784
    • Niyonsaba, F.1
  • 75
    • 33847040438 scopus 로고    scopus 로고
    • Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines
    • Niyonsaba F., et al. Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines. J. Invest. Dermatol. 127 (2007) 594-604
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 594-604
    • Niyonsaba, F.1
  • 76
    • 5844310778 scopus 로고    scopus 로고
    • IL-18 induction of IgE: dependence on CD4+ T cells, IL-4 and STAT6
    • Yoshimoto T., et al. IL-18 induction of IgE: dependence on CD4+ T cells, IL-4 and STAT6. Nat. Immunol. 1 (2000) 132-137
    • (2000) Nat. Immunol. , vol.1 , pp. 132-137
    • Yoshimoto, T.1
  • 77
    • 0035059368 scopus 로고    scopus 로고
    • Interleukin-18 regulates both Th1 and Th2 responses
    • Nakanishi K., et al. Interleukin-18 regulates both Th1 and Th2 responses. Annu. Rev. Immunol. 19 (2001) 423-474
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 423-474
    • Nakanishi, K.1
  • 78
    • 33846549311 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides block dendritic cell TLR4 activation and allergic contact sensitization
    • Di Nardo A., et al. Cathelicidin antimicrobial peptides block dendritic cell TLR4 activation and allergic contact sensitization. J. Immunol. 178 (2007) 1829-1834
    • (2007) J. Immunol. , vol.178 , pp. 1829-1834
    • Di Nardo, A.1
  • 79
    • 56149103147 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides inhibit hyaluronan-induced cytokine release and modulate chronic allergic dermatitis
    • Morioka Y., et al. Cathelicidin antimicrobial peptides inhibit hyaluronan-induced cytokine release and modulate chronic allergic dermatitis. J. Immunol. 181 (2008) 3915-3922
    • (2008) J. Immunol. , vol.181 , pp. 3915-3922
    • Morioka, Y.1
  • 80
    • 30044433704 scopus 로고    scopus 로고
    • Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37
    • Mookherjee N., et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J. Immunol. 176 (2006) 2455-2464
    • (2006) J. Immunol. , vol.176 , pp. 2455-2464
    • Mookherjee, N.1
  • 81
    • 33845383026 scopus 로고    scopus 로고
    • Bovine and human cathelicidin cationic host defense peptides similarly suppress transcriptional responses to bacterial lipopolysaccharide
    • Mookherjee N., et al. Bovine and human cathelicidin cationic host defense peptides similarly suppress transcriptional responses to bacterial lipopolysaccharide. J. Leukoc. Biol. 80 (2006) 1563-1574
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 1563-1574
    • Mookherjee, N.1
  • 82
    • 30744475689 scopus 로고    scopus 로고
    • Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties
    • Tydell C.C., et al. Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties. J. Immunol. 176 (2006) 1154-1162
    • (2006) J. Immunol. , vol.176 , pp. 1154-1162
    • Tydell, C.C.1
  • 83
    • 20444438391 scopus 로고    scopus 로고
    • A synthesized cationic tetradecapeptide from hornet venom kills bacteria and neutralizes lipopolysaccharide in vivo and in vitro
    • Yibin G., et al. A synthesized cationic tetradecapeptide from hornet venom kills bacteria and neutralizes lipopolysaccharide in vivo and in vitro. Biochem. Pharmacol. 70 (2005) 209-219
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 209-219
    • Yibin, G.1
  • 84
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action
    • Rosenfeld Y., et al. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem. 281 (2006) 1636-1643
    • (2006) J. Biol. Chem. , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1
  • 85
    • 33846027521 scopus 로고    scopus 로고
    • Topomimetics of amphipathic beta-sheet and helix-forming bactericidal peptides neutralize lipopolysaccharide endotoxins
    • Chen X., et al. Topomimetics of amphipathic beta-sheet and helix-forming bactericidal peptides neutralize lipopolysaccharide endotoxins. J. Med. Chem. 49 (2006) 7754-7765
    • (2006) J. Med. Chem. , vol.49 , pp. 7754-7765
    • Chen, X.1
  • 86
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • Heilborn J.D., et al. The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J. Invest. Dermatol. 120 (2003) 379-389
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 379-389
    • Heilborn, J.D.1
  • 87
    • 58149526865 scopus 로고    scopus 로고
    • Antimicrobial human beta-defensin-2 stimulates migration, proliferation and tube formation of human umbilical vein endothelial cells
    • Baroni A., et al. Antimicrobial human beta-defensin-2 stimulates migration, proliferation and tube formation of human umbilical vein endothelial cells. Peptides 32 (2009) 267-272
    • (2009) Peptides , vol.32 , pp. 267-272
    • Baroni, A.1
  • 88
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds
    • Gallo R.L., et al. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 11035-11039
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 11035-11039
    • Gallo, R.L.1
  • 89
    • 25444468300 scopus 로고    scopus 로고
    • Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37
    • Tokumaru S., et al. Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. J. Immunol. 175 (2005) 4662-4668
    • (2005) J. Immunol. , vol.175 , pp. 4662-4668
    • Tokumaru, S.1
  • 90
    • 37049030173 scopus 로고    scopus 로고
    • In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37
    • Carretero M., et al. In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37. J. Invest. Dermatol. 128 (2008) 223-236
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 223-236
    • Carretero, M.1
  • 91
    • 0038142308 scopus 로고    scopus 로고
    • An angiogenic role for the human peptide antibiotic LL-37/hCAP-18
    • Koczulla R., et al. An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. J. Clin. Invest. 111 (2003) 1665-1672
    • (2003) J. Clin. Invest. , vol.111 , pp. 1665-1672
    • Koczulla, R.1
  • 92
    • 63149113381 scopus 로고    scopus 로고
    • Park, H. J. et al. (2008) Collagen synthesis is suppressed in dermal fibroblasts by the human antimicrobial peptide LL-37. J. Invest. Dermatol. DOI: 10.1038/jid.2008.320 (in press)
    • Park, H. J. et al. (2008) Collagen synthesis is suppressed in dermal fibroblasts by the human antimicrobial peptide LL-37. J. Invest. Dermatol. DOI: 10.1038/jid.2008.320 (in press)
  • 93
    • 0037057645 scopus 로고    scopus 로고
    • Endogenous antimicrobial peptides and skin infections in atopic dermatitis
    • Ong P.Y., et al. Endogenous antimicrobial peptides and skin infections in atopic dermatitis. N. Engl. J. Med. 347 (2002) 1151-1160
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1151-1160
    • Ong, P.Y.1
  • 94
    • 33748558056 scopus 로고    scopus 로고
    • A chromosome 8 gene-cluster polymorphism with low human beta-defensin 2 gene copy number predisposes to Crohn disease of the colon
    • Fellermann K., et al. A chromosome 8 gene-cluster polymorphism with low human beta-defensin 2 gene copy number predisposes to Crohn disease of the colon. Am. J. Hum. Genet. 79 (2006) 439-448
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 439-448
    • Fellermann, K.1
  • 95
    • 29144457296 scopus 로고    scopus 로고
    • Human defensin gene copy number polymorphisms: comprehensive analysis of independent variation in alpha- and beta-defensin regions at 8p22-p23
    • Linzmeier R.M., and Ganz T. Human defensin gene copy number polymorphisms: comprehensive analysis of independent variation in alpha- and beta-defensin regions at 8p22-p23. Genomics 86 (2005) 423-430
    • (2005) Genomics , vol.86 , pp. 423-430
    • Linzmeier, R.M.1    Ganz, T.2
  • 96
    • 34547660319 scopus 로고    scopus 로고
    • Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea
    • Yamasaki K., et al. Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea. Nat. Med. 13 (2007) 975-980
    • (2007) Nat. Med. , vol.13 , pp. 975-980
    • Yamasaki, K.1
  • 97
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • Lande R., et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 449 (2007) 564-569
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1
  • 98
    • 38849187386 scopus 로고    scopus 로고
    • IL-22 is required for Th17 cell-mediated pathology in a mouse model of psoriasis-like skin inflammation
    • Ma H.L., et al. IL-22 is required for Th17 cell-mediated pathology in a mouse model of psoriasis-like skin inflammation. J. Clin. Invest. 118 (2008) 597-607
    • (2008) J. Clin. Invest. , vol.118 , pp. 597-607
    • Ma, H.L.1
  • 99
    • 34548133583 scopus 로고    scopus 로고
    • Development, cytokine profile and function of human interleukin 17-producing helper T cells
    • Wilson N.J., et al. Development, cytokine profile and function of human interleukin 17-producing helper T cells. Nat. Immunol. 8 (2007) 950-957
    • (2007) Nat. Immunol. , vol.8 , pp. 950-957
    • Wilson, N.J.1
  • 100
    • 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., et al. Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7 (2001) 180-185
    • (2001) Nat. Med. , vol.7 , pp. 180-185
    • Islam, D.1
  • 101
    • 9644255763 scopus 로고    scopus 로고
    • Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases
    • Sieprawska-Lupa M., et al. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases. Antimicrob. Agents Chemother. 48 (2004) 4673-4679
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4673-4679
    • Sieprawska-Lupa, M.1
  • 102
    • 33846079739 scopus 로고    scopus 로고
    • The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci
    • Lai Y., et al. The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol. Microbiol. 63 (2007) 497-506
    • (2007) Mol. Microbiol. , vol.63 , pp. 497-506
    • Lai, Y.1
  • 103
    • 0035821289 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine
    • Peschel A., et al. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. J. Exp. Med. 193 (2001) 1067-1076
    • (2001) J. Exp. Med. , vol.193 , pp. 1067-1076
    • Peschel, A.1
  • 104
    • 36148999436 scopus 로고    scopus 로고
    • The antimicrobial peptide-sensing system aps of Staphylococcus aureus
    • Li M., et al. The antimicrobial peptide-sensing system aps of Staphylococcus aureus. Mol. Microbiol. 66 (2007) 1136-1147
    • (2007) Mol. Microbiol. , vol.66 , pp. 1136-1147
    • Li, M.1
  • 105
    • 34547201058 scopus 로고    scopus 로고
    • Gram-positive three-component antimicrobial peptide-sensing system
    • Li M., et al. Gram-positive three-component antimicrobial peptide-sensing system. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 9469-9474
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9469-9474
    • Li, M.1
  • 106
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium
    • Gunn J.S., et al. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium. Infect. Immun. 68 (2000) 6139-6146
    • (2000) Infect. Immun. , vol.68 , pp. 6139-6146
    • Gunn, J.S.1
  • 107
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
    • Weidenmaier C., and Peschel A. Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nat. Rev. Microbiol. 6 (2008) 276-287
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 108
    • 25144519572 scopus 로고    scopus 로고
    • D-alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion
    • Kristian S.A., et al. D-alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion. J. Bacteriol. 187 (2005) 6719-6725
    • (2005) J. Bacteriol. , vol.187 , pp. 6719-6725
    • Kristian, S.A.1
  • 109
    • 23744504984 scopus 로고    scopus 로고
    • Recognition of antimicrobial peptides by a bacterial sensor kinase
    • Bader M.W., et al. Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122 (2005) 461-472
    • (2005) Cell , vol.122 , pp. 461-472
    • Bader, M.W.1
  • 110
    • 33645002216 scopus 로고    scopus 로고
    • Anti-inflammatory activity of cationic peptides: application to the treatment of acne vulgaris
    • Marta Guarna M., et al. Anti-inflammatory activity of cationic peptides: application to the treatment of acne vulgaris. FEMS Microbiol. Lett. 257 (2006) 1-6
    • (2006) FEMS Microbiol. Lett. , vol.257 , pp. 1-6
    • Marta Guarna, M.1
  • 111
    • 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., et al. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272 (1997) 15258-15263
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258-15263
    • Frohm, M.1
  • 112
    • 3542990948 scopus 로고    scopus 로고
    • beta-Defensin-3 and -4 in intestinal epithelial cells display increased mRNA expression in ulcerative colitis
    • Fahlgren A., et al. beta-Defensin-3 and -4 in intestinal epithelial cells display increased mRNA expression in ulcerative colitis. Clin. Exp. Immunol. 137 (2004) 379-385
    • (2004) Clin. Exp. Immunol. , vol.137 , pp. 379-385
    • Fahlgren, A.1
  • 113
    • 0142026070 scopus 로고    scopus 로고
    • Inducible and constitutive beta-defensins are differentially expressed in Crohn's disease and ulcerative colitis
    • Wehkamp J., et al. Inducible and constitutive beta-defensins are differentially expressed in Crohn's disease and ulcerative colitis. Inflamm. Bowel Dis. 9 (2003) 215-223
    • (2003) Inflamm. Bowel Dis. , vol.9 , pp. 215-223
    • Wehkamp, J.1
  • 114
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman H.G. Innate immunity and the normal microflora. Immunol. Rev. 173 (2000) 5-16
    • (2000) Immunol. Rev. , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 115
    • 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 (2002) 583-590
    • (2002) Nat. Immunol. , vol.3 , pp. 583-590
    • Ghosh, D.1
  • 116
    • 0033981142 scopus 로고    scopus 로고
    • Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells
    • Diamond G., et al. Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells. Infect. Immun. 68 (2000) 113-119
    • (2000) Infect. Immun. , vol.68 , pp. 113-119
    • Diamond, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.