메뉴 건너뛰기




Volumn 12, Issue 7, 2012, Pages 503-516

Epithelial antimicrobial defence of the skin and intestine

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; ANTIMICROBIAL PROTEIN; BETA DEFENSIN; CALGRANULIN A; CALGRANULIN B; CATHELICIDIN; GALECTIN; LECTIN; LIPOCALIN; LYSOZYME; PEPTIDOGLYCAN RECOGNITION PROTEIN; PHOSPHOLIPASE A2; PROTEIN; PSORIASIN; RIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 84862862332     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3228     Document Type: Review
Times cited : (699)

References (139)
  • 1
    • 0036214923 scopus 로고    scopus 로고
    • The gut microflora and intestinal epithelial cells: A continuing dialogue
    • Neish, A. S. The gut microflora and intestinal epithelial cells: a continuing dialogue. Microbes Infect. 4, 309-317 (2002).
    • (2002) Microbes Infect. , vol.4 , pp. 309-317
    • Neish, A.S.1
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395 (2002).
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 53049087417 scopus 로고    scopus 로고
    • Multi-layered regulation of intestinal antimicrobial defense
    • Mukherjee, S., Vaishnava, S. & Hooper, L. V. Multi-layered regulation of intestinal antimicrobial defense. Cell. Mol. Life Sci. 65, 3019-3027 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3019-3027
    • Mukherjee, S.1    Vaishnava, S.2    Hooper, L.V.3
  • 5
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y. & Gallo, R. L. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30, 131-141 (2009).
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 6
    • 12344302254 scopus 로고    scopus 로고
    • Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection
    • Gler, R. et al. Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection. Nature Immunol. 6, 57-64 (2005).
    • (2005) Nature Immunol. , vol.6 , pp. 57-64
    • Gler, R.1
  • 7
    • 0035198723 scopus 로고    scopus 로고
    • Dermcidin: A novel human antibiotic peptide secreted by sweat glands
    • Schittek, B. et al. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nature Immunol. 2, 1133-1137 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 1133-1137
    • Schittek, B.1
  • 8
    • 79960940581 scopus 로고    scopus 로고
    • Paneth cell α-defensins in enteric innate immunity
    • Ouellette, A. J. Paneth cell α-defensins in enteric innate immunity. Cell. Mol. Life Sci. 68, 2215-2229 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2215-2229
    • Ouellette, A.J.1
  • 9
    • 4243210396 scopus 로고    scopus 로고
    • HIP/PAP is an adhesive protein expressed in hepatocarcinoma, normal Paneth, and pancreatic cells
    • Christa, L. et al. HIP/PAP is an adhesive protein expressed in hepatocarcinoma, normal Paneth, and pancreatic cells. Am. J. Physiol. 271, G993-G1002 (1996).
    • (1996) Am. J. Physiol. , vol.271
    • Christa, L.1
  • 10
    • 0038731075 scopus 로고    scopus 로고
    • Increased expression of HIP/PAP and regenerating gene III in human inflammatory bowel disease and a murine bacterial reconstitution model
    • Ogawa, H. et al. Increased expression of HIP/PAP and regenerating gene III in human inflammatory bowel disease and a murine bacterial reconstitution model. Inflamm. Bowel Dis. 9, 162-170 (2003).
    • (2003) Inflamm. Bowel Dis. , vol.9 , pp. 162-170
    • Ogawa, H.1
  • 11
    • 33748039462 scopus 로고    scopus 로고
    • Symbiotic bacteria direct expression of an intestinal bactericidal lectin
    • Cash, H. L., Whitham, C. V., Behrendt, C. L. & Hooper, L. V. Symbiotic bacteria direct expression of an intestinal bactericidal lectin. Science 313, 1126-1130 (2006).
    • (2006) Science , vol.313 , pp. 1126-1130
    • Cash, H.L.1    Whitham, C.V.2    Behrendt, C.L.3    Hooper, L.V.4
  • 12
    • 77952359819 scopus 로고    scopus 로고
    • Molecular basis for peptidoglycan recognition by a bactericidal lectin
    • Lehotzky, R. E. et al. Molecular basis for peptidoglycan recognition by a bactericidal lectin. Proc. Natl Acad. Sci. USA 107, 7722-7727 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 7722-7727
    • Lehotzky, R.E.1
  • 13
    • 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. USA 91, 11035-11039 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11035-11039
    • Gallo, R.L.1
  • 15
    • 0030602220 scopus 로고    scopus 로고
    • Structural, functional analysis and localization of the human CAP18 gene
    • Larrick, J. W. et al. Structural, functional analysis and localization of the human CAP18 gene. FEBS Lett. 398, 74-80 (1996).
    • (1996) FEBS Lett. , vol.398 , pp. 74-80
    • Larrick, J.W.1
  • 16
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson, G. H. et al. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238, 325-332 (1996).
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1
  • 17
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo, R. L. et al. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272, 13088-13093 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13088-13093
    • Gallo, R.L.1
  • 18
    • 0345074069 scopus 로고    scopus 로고
    • Cutting edge: Mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide
    • Di Nardo, A., Vitiello, A. & Gallo, R. L. Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide. J. Immunol. 170, 2274-2278 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 2274-2278
    • Di Nardo, A.1    Vitiello, A.2    Gallo, R.L.3
  • 19
    • 0036450262 scopus 로고    scopus 로고
    • Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin
    • Murakami, M. et al. Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin. J. Invest. Dermatol. 119, 1090-1095 (2002).
    • (2002) J. Invest. Dermatol. , vol.119 , pp. 1090-1095
    • Murakami, M.1
  • 20
    • 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, 15258-15263 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258-15263
    • Frohm, M.1
  • 21
    • 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, 91-97 (2001).
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 91-97
    • Dorschner, R.A.1
  • 22
    • 58549111588 scopus 로고    scopus 로고
    • Paneth cells directly sense gut commensals and maintain homeostasis at the intestinal host-microbial interface
    • Vaishnava, S., Behrendt, C. L., Ismail, A. S., Eckmann, L. & Hooper, L. V. Paneth cells directly sense gut commensals and maintain homeostasis at the intestinal host-microbial interface. Proc. Natl Acad. Sci. USA 105, 20858-20863 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20858-20863
    • Vaishnava, S.1    Behrendt, C.L.2    Ismail, A.S.3    Eckmann, L.4    Hooper, L.V.5
  • 23
    • 80054122238 scopus 로고    scopus 로고
    • The antibacterial lectin RegIIIγ promotes the spatial segregation of microbiota and host in the intestine
    • Vaishnava, S. et al. The antibacterial lectin RegIIIγ promotes the spatial segregation of microbiota and host in the intestine. Science 334, 255-258 (2011).
    • (2011) Science , vol.334 , pp. 255-258
    • Vaishnava, S.1
  • 24
    • 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. et al. Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium. J. Immunol. 163, 6718-6724 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1
  • 25
    • 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. & Kagnoff, M. F. Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. Infect. Immun. 70, 953-963 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 953-963
    • Hase, K.1    Eckmann, L.2    Leopard, J.D.3    Varki, N.4    Kagnoff, M.F.5
  • 26
    • 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. & Gordon, J. I. Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nature Immunol. 4, 269-273 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 269-273
    • Hooper, L.V.1    Stappenbeck, T.S.2    Hong, C.V.3    Gordon, J.I.4
  • 27
    • 54449083567 scopus 로고    scopus 로고
    • The inner of the two Muc2 mucin-dependent mucus layers in colon is devoid of bacteria
    • Johansson, M. E. V. et al. The inner of the two Muc2 mucin-dependent mucus layers in colon is devoid of bacteria. Proc. Natl Acad. Sci. USA 105, 15064-15069 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15064-15069
    • Johansson, M.E.V.1
  • 28
    • 44149126798 scopus 로고    scopus 로고
    • Secreted enteric antimicrobial activity localises to the mucus surface layer
    • Meyer-Hoffert, U. et al. Secreted enteric antimicrobial activity localises to the mucus surface layer. Gut 57, 764-771 (2008).
    • (2008) Gut , vol.57 , pp. 764-771
    • Meyer-Hoffert, U.1
  • 29
    • 84860331724 scopus 로고    scopus 로고
    • Immunohistological pointers to a possible role for excessive cathelicidin (LL-37) expression by apocrine sweat glands in the pathogenesis of hidradenitis suppurativa/acne inversa
    • Emelianov, V. U. et al. Immunohistological pointers to a possible role for excessive cathelicidin (LL-37) expression by apocrine sweat glands in the pathogenesis of hidradenitis suppurativa/acne inversa. Br. J. Dermatol. 166, 1023-1034 (2012).
    • (2012) Br. J. Dermatol. , vol.166 , pp. 1023-1034
    • Emelianov, V.U.1
  • 30
    • 0032903987 scopus 로고    scopus 로고
    • The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6
    • Frohm Nilsson, M. et al. The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6. Infect. Immun. 67, 2561-2566 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 2561-2566
    • Frohm Nilsson, M.1
  • 31
    • 0038189571 scopus 로고    scopus 로고
    • Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors
    • Sψrensen, O. E. et al. Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors. J. Immunol. 170, 5583-5589 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 5583-5589
    • Srensen, O.E.1
  • 32
    • 84855415476 scopus 로고    scopus 로고
    • Skin mast cells protect mice against vaccinia virus by triggering mast cell receptor S1PR2 and releasing antimicrobial peptides
    • Wang, Z. et al. Skin mast cells protect mice against vaccinia virus by triggering mast cell receptor S1PR2 and releasing antimicrobial peptides. J. Immunol. 188, 345-357 (2012).
    • (2012) J. Immunol. , vol.188 , pp. 345-357
    • Wang, Z.1
  • 33
    • 0028872519 scopus 로고
    • Bactericidal properties of murine intestinal phospholipase A2
    • Harwig, S. S. et al. Bactericidal properties of murine intestinal phospholipase A2. J. Clin. Invest. 95, 603-610 (1995).
    • (1995) J. Clin. Invest. , vol.95 , pp. 603-610
    • Harwig, S.S.1
  • 34
    • 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. & Weiss, J. P. 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).
    • (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
  • 35
    • 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. & Lehrer, R. I. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl Acad. Sci. USA 87, 210-214 (1990).
    • (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
  • 36
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins-a family of multifunctional antimicrobial peptides
    • Bals, R. & Wilson, J. M. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 60, 711-720 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 37
    • 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. Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr. Pharm. Des. 8, 763-778 (2002).
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 763-778
    • Gennaro, R.1    Zanetti, M.2    Benincasa, M.3    Podda, E.4    Miani, M.5
  • 38
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder, J. & Schroder, J.-M. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277, 46779-46784 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46779-46784
    • Harder, J.1    Schroder, J.-M.2
  • 39
    • 39349117867 scopus 로고    scopus 로고
    • Metal chelation and inhibition of bacterial growth in tissue abscesses
    • Corbin, B. D. et al. Metal chelation and inhibition of bacterial growth in tissue abscesses. Science 319, 962-965 (2008).
    • (2008) Science , vol.319 , pp. 962-965
    • Corbin, B.D.1
  • 40
    • 80051898476 scopus 로고    scopus 로고
    • Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus
    • Kehl-Fie, T. E. et al. Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus. Cell Host Microbe 10, 158-164 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 158-164
    • Kehl-Fie, T.E.1
  • 41
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De Yang. et al. LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192, 1069-1074 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • De Yang1
  • 42
    • 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., Chen, Q., Yarovinsky, F., Oppenheim, J. J. & Yang, D. 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, 6257-6265 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 43
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • Yang, D., Biragyn, A., Kwak, L. W. & Oppenheim, J. J. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23, 291-296 (2002).
    • (2002) Trends Immunol. , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 44
    • 0036240209 scopus 로고    scopus 로고
    • A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis
    • Niyonsaba, F. et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 106, 20-26 (2002).
    • (2002) Immunology , vol.106 , pp. 20-26
    • Niyonsaba, F.1
  • 45
    • 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., Chertov, O. & Oppenheim, J. J. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J. Leukoc. Biol. 69, 691-697 (2001).
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 691-697
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 46
    • 0033569408 scopus 로고    scopus 로고
    • β-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • Yang, D. et al. β-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. Science 286, 525-528 (1999).
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1
  • 47
    • 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, 4662-4668 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 4662-4668
    • Tokumaru, S.1
  • 48
    • 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. Nature Med. 13, 975-980 (2007).
    • (2007) Nature Med. , vol.13 , pp. 975-980
    • Yamasaki, K.1
  • 49
    • 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, 1829-1834 (2007).
    • (2007) J. Immunol. , vol.178 , pp. 1829-1834
    • Di Nardo, A.1
  • 50
    • 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, 564-569 (2007).
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1
  • 51
    • 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. & Gordon, J. I. Creating and maintaining the gastrointestinal ecosystem: what we know and need to know from gnotobiology. Microbiol. Mol. Biol. Rev. 62, 1157-1170 (1998).
    • (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
  • 52
    • 20244364236 scopus 로고    scopus 로고
    • Wnt signalling induces maturation of Paneth cells in intestinal crypts
    • van Es, J. H. et al. Wnt signalling induces maturation of Paneth cells in intestinal crypts. Nature Cell Biol. 7, 381-386 (2005).
    • (2005) Nature Cell Biol. , vol.7 , pp. 381-386
    • Van Es, J.H.1
  • 53
    • 0034704102 scopus 로고    scopus 로고
    • Germ-free and colonized mice generate the same products from enteric prodefensins
    • Putsep, K. et al. Germ-free and colonized mice generate the same products from enteric prodefensins. J. Biol. Chem. 275, 40478-40482 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 40478-40482
    • Putsep, K.1
  • 54
    • 0035793372 scopus 로고    scopus 로고
    • Molecular analysis of commensal host-microbial relationships in the intestine
    • Hooper, L. V. et al. Molecular analysis of commensal host-microbial relationships in the intestine. Science 291, 881-884 (2001).
    • (2001) Science , vol.291 , pp. 881-884
    • Hooper, L.V.1
  • 55
    • 46749113417 scopus 로고    scopus 로고
    • Flagellin is the principal inducer of the antimicrobial peptide S100A7c (psoriasin) in human epidermal keratinocytes exposed to Escherichia coli
    • Abtin, A. et al. Flagellin is the principal inducer of the antimicrobial peptide S100A7c (psoriasin) in human epidermal keratinocytes exposed to Escherichia coli. FASEB J. 22, 2168-2176 (2008).
    • (2008) FASEB J. , vol.22 , pp. 2168-2176
    • Abtin, A.1
  • 56
    • 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. & Pamer, E. G. MyD88-mediated signals induce the bactericidal lectin RegIIIγ and protect mice against intestinal Listeria monocytogenes infection. J. Exp. Med. 204, 1891-1900 (2007).
    • (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
  • 57
    • 34447296425 scopus 로고    scopus 로고
    • Regulation of spontaneous intestinal tumorigenesis through the adaptor protein MyD88
    • Rakoff-Nahoum, S. & Medzhitov, R. Regulation of spontaneous intestinal tumorigenesis through the adaptor protein MyD88. Science 317, 124-127 (2007).
    • (2007) Science , vol.317 , pp. 124-127
    • Rakoff-Nahoum, S.1    Medzhitov, R.2
  • 58
    • 75749133608 scopus 로고    scopus 로고
    • Bacterial flagellin stimulates Toll-like receptor 5-dependent defense against vancomycin-resistant Enterococcus infection
    • Kinnebrew, M. A. et al. Bacterial flagellin stimulates Toll-like receptor 5-dependent defense against vancomycin-resistant Enterococcus infection. J. Infect. Dis. 201, 534-543 (2010).
    • (2010) J. Infect. Dis. , vol.201 , pp. 534-543
    • Kinnebrew, M.A.1
  • 59
    • 0038523850 scopus 로고    scopus 로고
    • Expression of the cathelicidin LL-37 is modulated by short chain fatty acids in colonocytes: Relevance of signalling pathways
    • Schauber, J. et al. Expression of the cathelicidin LL-37 is modulated by short chain fatty acids in colonocytes: relevance of signalling pathways. Gut 52, 735-741 (2003).
    • (2003) Gut , vol.52 , pp. 735-741
    • Schauber, J.1
  • 61
    • 4143095716 scopus 로고    scopus 로고
    • IL-22 increases the innate immunity of tissues
    • Wolk, K. et al. IL-22 increases the innate immunity of tissues. Immunity 21, 241-254 (2004).
    • (2004) Immunity , vol.21 , pp. 241-254
    • Wolk, K.1
  • 63
    • 10744222688 scopus 로고    scopus 로고
    • Expression of NOD2 in Paneth cells: A possible link to Crohn's ileitis
    • Ogura, Y. et al. Expression of NOD2 in Paneth cells: a possible link to Crohn's ileitis. Gut 52, 1591-1597 (2003).
    • (2003) Gut , vol.52 , pp. 1591-1597
    • Ogura, Y.1
  • 64
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin, S. E. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278, 8869-8872 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 8869-8872
    • Girardin, S.E.1
  • 65
    • 70349468054 scopus 로고    scopus 로고
    • Nod2 is required for the regulation of commensal microbiota in the intestine
    • Petnicki-Ocwieja, T. et al. Nod2 is required for the regulation of commensal microbiota in the intestine. Proc. Natl Acad. Sci. USA 106, 15813-15818 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15813-15818
    • Petnicki-Ocwieja, T.1
  • 66
    • 13244292161 scopus 로고    scopus 로고
    • Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract
    • Kobayashi, K. S. et al. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307, 731-734 (2005).
    • (2005) Science , vol.307 , pp. 731-734
    • Kobayashi, K.S.1
  • 67
    • 0032956143 scopus 로고    scopus 로고
    • Developmental microbial ecology of the neonatal gastrointestinal tract
    • Mackie, R. I., Sghir, A. & Gaskins, H. R. Developmental microbial ecology of the neonatal gastrointestinal tract. Am. J. Clin. Nutr. 69, 1035S-1045S (1999).
    • (1999) Am. J. Clin. Nutr. , vol.69
    • MacKie, R.I.1    Sghir, A.2    Gaskins, H.R.3
  • 68
    • 38749117873 scopus 로고    scopus 로고
    • Developmental switch of intestinal antimicrobial peptide expression
    • Mnard, S. et al. Developmental switch of intestinal antimicrobial peptide expression. J. Exp. Med. 205, 183-193 (2008).
    • (2008) J. Exp. Med. , vol.205 , pp. 183-193
    • Mnard, S.1
  • 69
    • 17044404692 scopus 로고    scopus 로고
    • Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens
    • Iimura, M. et al. Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens. J. Immunol. 174, 4901-4907 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 4901-4907
    • Iimura, M.1
  • 70
    • 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. 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. USA 84, 5449-5453 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 71
    • 20244363184 scopus 로고
    • Insect immunity: Isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides
    • Lambert, J. et al. Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc. Natl Acad. Sci. USA 86, 262-266 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 262-266
    • Lambert, J.1
  • 72
    • 40649124294 scopus 로고    scopus 로고
    • Co-regulation and interdependence of the mammalian epidermal permeability and antimicrobial barriers
    • Aberg, K. M. et al. Co-regulation and interdependence of the mammalian epidermal permeability and antimicrobial barriers. J. Invest. Dermatol. 128, 917-925 (2008).
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 917-925
    • Aberg, K.M.1
  • 73
    • 33745849146 scopus 로고    scopus 로고
    • Injury-induced innate immune response in human skin mediated by transactivation of the epidermal growth factor receptor
    • Sψrensen, O. E. et al. Injury-induced innate immune response in human skin mediated by transactivation of the epidermal growth factor receptor. J. Clin. Invest. 116, 1878-1885 (2006).
    • (2006) J. Clin. Invest. , vol.116 , pp. 1878-1885
    • Srensen, O.E.1
  • 74
    • 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, 2909-2912 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 2909-2912
    • Wang, T.-T.1
  • 75
    • 21744438757 scopus 로고    scopus 로고
    • 3
    • Gombart, A. F., Borregaard, N. & Koeffler, H. P. 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, 1067-1077 (2005).
    • (2005) FASEB J. , vol.19 , pp. 1067-1077
    • Gombart, A.F.1    Borregaard, N.2    Koeffler, H.P.3
  • 76
    • 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, 1770-1773 (2006).
    • (2006) Science , vol.311 , pp. 1770-1773
    • Liu, P.T.1
  • 77
    • 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, 803-811 (2007).
    • (2007) J. Clin. Invest. , vol.117 , pp. 803-811
    • Schauber, J.1
  • 78
    • 53049094390 scopus 로고    scopus 로고
    • Administration of oral vitamin D induces cathelicidin production in atopic individuals
    • Hata, T. R. et al. Administration of oral vitamin D induces cathelicidin production in atopic individuals. J. Allergy Clin. Immunol. 122, 829-831 (2008).
    • (2008) J. Allergy Clin. Immunol. , vol.122 , pp. 829-831
    • Hata, T.R.1
  • 79
    • 57349167517 scopus 로고    scopus 로고
    • Biopositive effects of low-dose UVB on epidermis: Coordinate upregulation of antimicrobial peptides and permeability barrier reinforcement
    • Hong, S. P. et al. Biopositive effects of low-dose UVB on epidermis: coordinate upregulation of antimicrobial peptides and permeability barrier reinforcement. J. Invest. Dermatol. 128, 2880-2887 (2008).
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 2880-2887
    • Hong, S.P.1
  • 80
    • 0022886732 scopus 로고
    • In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes
    • Lichtenstein, A., Ganz, T., Selsted, M. E. & Lehrer, R. I. In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes. Blood 68, 1407-1410 (1986).
    • (1986) Blood , vol.68 , pp. 1407-1410
    • Lichtenstein, A.1    Ganz, T.2    Selsted, M.E.3    Lehrer, R.I.4
  • 81
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson, C. L. et al. Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 286, 113-117 (1999).
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1
  • 82
    • 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. Nature Immunol. 3, 583-590 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 583-590
    • Ghosh, D.1
  • 83
    • 64149129422 scopus 로고    scopus 로고
    • Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment
    • Mukherjee, S. et al. Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. J. Biol. Chem. 284, 4881-4888 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4881-4888
    • Mukherjee, S.1
  • 84
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sψrensen, O., Arnljots, K., Cowland, J. B., Bainton, D. F. & Borregaard, N. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90, 2796-2803 (1997).
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Srensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 85
    • 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, 2068-2080 (2006).
    • (2006) FASEB J. , vol.20 , pp. 2068-2080
    • Yamasaki, K.1
  • 86
    • 0036197412 scopus 로고    scopus 로고
    • β-defensins in lung host defense
    • Schutte, B. C. & McCray, P. B. β-defensins in lung host defense. Annu. Rev. Physiol. 64, 709-748 (2002).
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 709-748
    • Schutte, B.C.1    McCray, P.B.2
  • 87
    • 78751653584 scopus 로고    scopus 로고
    • Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1
    • Schroeder, B. O. et al. Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1. Nature 469, 419-423 (2011).
    • (2011) Nature , vol.469 , pp. 419-423
    • Schroeder, B.O.1
  • 88
    • 0034252293 scopus 로고    scopus 로고
    • Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria
    • Ayabe, T. et al. Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nature Immunol. 1, 113-118 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 113-118
    • Ayabe, T.1
  • 89
    • 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. & Bevins, C. L. Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature 422, 522-526 (2003).
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 90
    • 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, 1763-1767 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 1763-1767
    • Howell, M.D.1
  • 91
    • 79955971446 scopus 로고    scopus 로고
    • Mammalian antimicrobial peptide influences control of cutaneous Leishmania infection
    • Kulkarni, M. M. et al. Mammalian antimicrobial peptide influences control of cutaneous Leishmania infection. Cell. Microbiol. 13, 913-923 (2011).
    • (2011) Cell. Microbiol. , vol.13 , pp. 913-923
    • Kulkarni, M.M.1
  • 92
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet, V. et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414, 454-457 (2001).
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1
  • 93
    • 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. Nature Med. 12, 636-641 (2006).
    • (2006) Nature Med. , vol.12 , pp. 636-641
    • Chromek, M.1
  • 94
    • 35748985576 scopus 로고    scopus 로고
    • Cathelicidin-deficient (Cnlp-/-) mice show increased susceptibility to Pseudomonas aeruginosa keratitis
    • Huang, L. C., Reins, R. Y., Gallo, R. L. & McDermott, A. M. Cathelicidin-deficient (Cnlp-/-) mice show increased susceptibility to Pseudomonas aeruginosa keratitis. Invest. Ophthalmol. Vis. Sci. 48, 4498-4508 (2007).
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 4498-4508
    • Huang, L.C.1    Reins, R.Y.2    Gallo, R.L.3    McDermott, A.M.4
  • 95
    • 53649098280 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococci exploit antibiotic-induced innate immune deficits
    • Brandl, K. et al. Vancomycin-resistant enterococci exploit antibiotic-induced innate immune deficits. Nature 455, 804-807 (2008).
    • (2008) Nature , vol.455 , pp. 804-807
    • Brandl, K.1
  • 96
    • 74049122536 scopus 로고    scopus 로고
    • Enteric defensins are essential regulators of intestinal microbial ecology
    • Salzman, N. H. et al. Enteric defensins are essential regulators of intestinal microbial ecology. Nature Immunol. 11, 76-83 (2010).
    • (2010) Nature Immunol. , vol.11 , pp. 76-83
    • Salzman, N.H.1
  • 97
    • 70350343544 scopus 로고    scopus 로고
    • Induction of intestinal Th17 cells by segmented filamentous bacteria
    • Ivanov, I. I. et al. Induction of intestinal Th17 cells by segmented filamentous bacteria. Cell 139, 485-498 (2009).
    • (2009) Cell , vol.139 , pp. 485-498
    • Ivanov, I.I.1
  • 98
    • 72049093749 scopus 로고    scopus 로고
    • Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin
    • Cogen, A. L. et al. Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin. J. Invest. Dermatol. 130, 192-200 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , pp. 192-200
    • Cogen, A.L.1
  • 99
    • 77952723375 scopus 로고    scopus 로고
    • Staphylococcus epidermidis Esp. inhibits Staphylococcus aureus biofilm formation and nasal colonization
    • Iwase, T. et al. Staphylococcus epidermidis Esp. inhibits Staphylococcus aureus biofilm formation and nasal colonization. Nature 465, 346-349 (2010).
    • (2010) Nature , vol.465 , pp. 346-349
    • Iwase, T.1
  • 100
    • 0344915178 scopus 로고    scopus 로고
    • Inhibition of virulence factor expression in Staphylococcus aureus by the Staphylococcus epidermidis agr pheromone and derivatives
    • Otto, M., Sssmuth, R., Vuong, C., Jung, G. & Gφtz, F. Inhibition of virulence factor expression in Staphylococcus aureus by the Staphylococcus epidermidis agr pheromone and derivatives. FEBS Lett. 450, 257-262 (1999).
    • (1999) FEBS Lett. , vol.450 , pp. 257-262
    • Otto, M.1    Sssmuth, R.2    Vuong, C.3    Jung, G.4    Gtz, F.5
  • 101
    • 34547176642 scopus 로고    scopus 로고
    • Unravelling the pathogenesis of inflammatory bowel disease
    • Xavier, R. J. & Podolsky, D. K. Unravelling the pathogenesis of inflammatory bowel disease. Nature 448, 427-434 (2007).
    • (2007) Nature , vol.448 , pp. 427-434
    • Xavier, R.J.1    Podolsky, D.K.2
  • 102
    • 22144476548 scopus 로고    scopus 로고
    • Spatial organization and composition of the mucosal flora in patients with inflammatory bowel disease
    • Swidsinski, A., Weber, J., Loening-Baucke, V., Hale, L. P. & Lochs, H. Spatial organization and composition of the mucosal flora in patients with inflammatory bowel disease. J. Clin. Microbiol. 43, 3380-3389 (2005).
    • (2005) J. Clin. Microbiol. , vol.43 , pp. 3380-3389
    • Swidsinski, A.1    Weber, J.2    Loening-Baucke, V.3    Hale, L.P.4    Lochs, H.5
  • 103
    • 84887212530 scopus 로고    scopus 로고
    • Genetic variants of Wnt transcription factor TCF-4 (TCF7L2) putative promoter region are associated with small intestinal Crohn's disease
    • Koslowski, M. J. et al. Genetic variants of Wnt transcription factor TCF-4 (TCF7L2) putative promoter region are associated with small intestinal Crohn's disease. PLoS ONE 4, e4496 (2009).
    • (2009) PLoS ONE , vol.4
    • Koslowski, M.J.1
  • 104
    • 84859196359 scopus 로고    scopus 로고
    • Association of a functional variant in the Wnt co-receptor LRP6 with early onset ileal Crohn's disease
    • Koslowski, M. J. et al. Association of a functional variant in the Wnt co-receptor LRP6 with early onset ileal Crohn's disease. PLoS Genet. 8, e1002523 (2012).
    • (2012) PLoS Genet. , vol.8
    • Koslowski, M.J.1
  • 105
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • Hugot, J. P. et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411, 599-603 (2001).
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1
  • 106
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • Ogura, Y. et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411, 603-606 (2001).
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1
  • 107
    • 29144483937 scopus 로고    scopus 로고
    • Reduced Paneth cell α-defensins in ileal Crohn's disease
    • Wehkamp, J. et al. Reduced Paneth cell α-defensins in ileal Crohn's disease. Proc. Natl Acad. Sci. USA 102, 18129-18134 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18129-18134
    • Wehkamp, J.1
  • 108
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell, K. et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 456, 259-263 (2008).
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1
  • 109
    • 50249086073 scopus 로고    scopus 로고
    • XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease
    • Kaser, A. et al. XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell 134, 743-756 (2008).
    • (2008) Cell , vol.134 , pp. 743-756
    • Kaser, A.1
  • 110
    • 0030863618 scopus 로고    scopus 로고
    • Examining the role of Paneth cells in the small intestine by lineage ablation in transgenic mice
    • Garabedian, E. M., Roberts, L. J., McNevin, M. S. & Gordon, J. I. Examining the role of Paneth cells in the small intestine by lineage ablation in transgenic mice. J. Biol. Chem. 272, 23729-23740 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23729-23740
    • Garabedian, E.M.1    Roberts, L.J.2    McNevin, M.S.3    Gordon, J.I.4
  • 111
    • 71949105323 scopus 로고    scopus 로고
    • Constitutive expression of the antimicrobial peptide RNase 7 is associated with Staphylococcus aureus infection of the skin
    • Zanger, P. et al. Constitutive expression of the antimicrobial peptide RNase 7 is associated with Staphylococcus aureus infection of the skin. J. Infect. Dis. 200, 1907-1915 (2009).
    • (2009) J. Infect. Dis. , vol.200 , pp. 1907-1915
    • Zanger, P.1
  • 112
    • 77953953928 scopus 로고    scopus 로고
    • Severity of Staphylococcus aureus infection of the skin is associated with inducibility of human β-defensin 3 but not human β-defensin 2
    • Zanger, P. et al. Severity of Staphylococcus aureus infection of the skin is associated with inducibility of human β-defensin 3 but not human β-defensin 2. Infect. Immun. 78, 3112-3117 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 3112-3117
    • Zanger, P.1
  • 113
    • 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, 1151-1160 (2002).
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1151-1160
    • Ong, P.Y.1
  • 114
    • 33644831004 scopus 로고    scopus 로고
    • High expression levels of keratinocyte antimicrobial proteins in psoriasis compared with atopic dermatitis
    • de Jongh, G. J. et al. High expression levels of keratinocyte antimicrobial proteins in psoriasis compared with atopic dermatitis. J. Invest. Dermatol. 125, 1163-1173 (2005).
    • (2005) J. Invest. Dermatol. , vol.125 , pp. 1163-1173
    • De Jongh, G.J.1
  • 115
    • 46049112666 scopus 로고    scopus 로고
    • Defective killing of Staphylococcus aureus in atopic dermatitis is associated with reduced mobilization of human β-defensin-3
    • Kisich, K. O., Carspecken, C. W., Fiιve, S., Boguniewicz, M. & Leung, D. Y. M. Defective killing of Staphylococcus aureus in atopic dermatitis is associated with reduced mobilization of human β-defensin-3. J. Allergy Clin. Immunol. 122, 62-68 (2008).
    • (2008) J. Allergy Clin. Immunol. , vol.122 , pp. 62-68
    • Kisich, K.O.1    Carspecken, C.W.2    Five, S.3    Boguniewicz, M.4    Leung, D.Y.M.5
  • 116
    • 77955894822 scopus 로고    scopus 로고
    • History of eczema herpeticum is associated with the inability to induce human β-defensin (HBD)-2 HBD-3 and cathelicidin in the skin of patients with atopic dermatitis
    • Hata, T. R. et al. History of eczema herpeticum is associated with the inability to induce human β-defensin (HBD)-2, HBD-3 and cathelicidin in the skin of patients with atopic dermatitis. Br. J. Dermatol. 163, 659-661 (2010).
    • (2010) Br. J. Dermatol. , vol.163 , pp. 659-661
    • Hata, T.R.1
  • 117
    • 33644973071 scopus 로고    scopus 로고
    • Cytokine milieu of atopic dermatitis skin subverts the innate immune response to vaccinia virus
    • Howell, M. D. et al. Cytokine milieu of atopic dermatitis skin subverts the innate immune response to vaccinia virus. Immunity 24, 341-348 (2006).
    • (2006) Immunity , vol.24 , pp. 341-348
    • Howell, M.D.1
  • 118
    • 79951516747 scopus 로고    scopus 로고
    • TLR2 expression is increased in rosacea and stimulates enhanced serine protease production by keratinocytes
    • Yamasaki, K. et al. TLR2 expression is increased in rosacea and stimulates enhanced serine protease production by keratinocytes. J. Invest. Dermatol. 131, 688-697 (2011).
    • (2011) J. Invest. Dermatol. , vol.131 , pp. 688-697
    • Yamasaki, K.1
  • 119
    • 1842787415 scopus 로고    scopus 로고
    • BsmI polymorphism of the vitamin D receptor gene in patients with the fulminant course of rosacea conglobata (rosacea fulminans)
    • Jansen, T., Krug, S., Kind, P., Plewig, G. & Messer, G. BsmI polymorphism of the vitamin D receptor gene in patients with the fulminant course of rosacea conglobata (rosacea fulminans). J. Dermatol. 31, 244-246 (2004).
    • (2004) J. Dermatol. , vol.31 , pp. 244-246
    • Jansen, T.1    Krug, S.2    Kind, P.3    Plewig, G.4    Messer, G.5
  • 120
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel, A. et al. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274, 8405-8410 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1
  • 121
    • 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., Ryan, S. S., Van Velkinburgh, J. C., Ernst, R. K. & Miller, S. I. 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, 6139-6146 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 122
    • 0034972212 scopus 로고    scopus 로고
    • Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection
    • Robey, M., O'Connell, W. & Cianciotto, N. P. Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection. Infect. Immun. 69, 4276-4286 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 4276-4286
    • Robey, M.1    O'Connell, W.2    Cianciotto, N.P.3
  • 123
    • 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, 4673-4679 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4673-4679
    • Sieprawska-Lupa, M.1
  • 124
    • 11144237617 scopus 로고    scopus 로고
    • α2-macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37
    • Nyberg, P., Rasmussen, M. & Björck, L. α2-macroglobulin- proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37. J. Biol. Chem. 279, 52820-52823 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 52820-52823
    • Nyberg, P.1    Rasmussen, M.2    Björck, L.3
  • 125
    • 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, W. M., Qu, X., Waring, A. J. & Lehrer, R. I. 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. USA 95, 1829-1833 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 126
    • 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. Nature Med. 7, 180-185 (2001).
    • (2001) Nature Med. , vol.7 , pp. 180-185
    • Islam, D.1
  • 127
    • 79960938721 scopus 로고    scopus 로고
    • Bacterial resistance mechanisms against host defense peptides
    • Koprivnjak, T. & Peschel, A. Bacterial resistance mechanisms against host defense peptides. Cell. Mol. Life Sci. 68, 2243-2254 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2243-2254
    • Koprivnjak, T.1    Peschel, A.2
  • 128
    • 34250860681 scopus 로고    scopus 로고
    • Understanding how leading bacterial pathogens subvert innate immunity to reveal novel therapeutic targets
    • Nizet, V. Understanding how leading bacterial pathogens subvert innate immunity to reveal novel therapeutic targets. J. Allergy Clin. Immunol. 120, 13-22 (2007).
    • (2007) J. Allergy Clin. Immunol. , vol.120 , pp. 13-22
    • Nizet, V.1
  • 129
    • 20544444045 scopus 로고    scopus 로고
    • Diversity of the human intestinal microbial flora
    • Eckburg, P. B. et al. Diversity of the human intestinal microbial flora. Science 308, 1635-1638 (2005).
    • (2005) Science , vol.308 , pp. 1635-1638
    • Eckburg, P.B.1
  • 130
    • 46249085739 scopus 로고    scopus 로고
    • Evolution of mammals and their gut microbes
    • Ley, R. E. et al. Evolution of mammals and their gut microbes. Science 320, 1647-1651 (2008).
    • (2008) Science , vol.320 , pp. 1647-1651
    • Ley, R.E.1
  • 131
    • 72949091232 scopus 로고    scopus 로고
    • Bacterial community variation in human body habitats across space and time
    • Costello, E. K. et al. Bacterial community variation in human body habitats across space and time. Science 326, 1694-1697 (2009).
    • (2009) Science , vol.326 , pp. 1694-1697
    • Costello, E.K.1
  • 132
    • 33746889083 scopus 로고    scopus 로고
    • Induction of β-defensin 3 in keratinocytes stimulated by bacterial lipopeptides through toll-like receptor 2
    • Sumikawa, Y. et al. Induction of β-defensin 3 in keratinocytes stimulated by bacterial lipopeptides through toll-like receptor 2. Microbes Infect. 8, 1513-1521 (2006).
    • (2006) Microbes Infect. , vol.8 , pp. 1513-1521
    • Sumikawa, Y.1
  • 133
    • 77952693839 scopus 로고    scopus 로고
    • Human β-defensin 3 inhibits cell wall biosynthesis in Staphylococci
    • Sass, V. et al. Human β-defensin 3 inhibits cell wall biosynthesis in Staphylococci. Infect. Immun. 78, 2793-2800 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 2793-2800
    • Sass, V.1
  • 134
    • 77749239686 scopus 로고    scopus 로고
    • Innate immune lectins kill bacteria expressing blood group antigen
    • Stowell, S. R. et al. Innate immune lectins kill bacteria expressing blood group antigen. Nature Med. 16, 295-302 (2010).
    • (2010) Nature Med. , vol.16 , pp. 295-302
    • Stowell, S.R.1
  • 135
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T. H. et al. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432, 917-921 (2004).
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1
  • 136
    • 65549099573 scopus 로고    scopus 로고
    • Lipocalin-2 resistance confers an advantage to Salmonella enterica serotype typhimurium for growth and survival in the inflamed intestine
    • Raffatellu, M. et al. Lipocalin-2 resistance confers an advantage to Salmonella enterica serotype typhimurium for growth and survival in the inflamed intestine. Cell Host Microbe 5, 476-486 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 476-486
    • Raffatellu, M.1
  • 137
    • 20744443283 scopus 로고    scopus 로고
    • Innate defenses of the intestinal epithelial barrier
    • Mller, C. A., Autenrieth, I. B. & Peschel, A. Innate defenses of the intestinal epithelial barrier. Cell. Mol. Life Sci. 62, 1297-1307 (2005).
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1297-1307
    • Mller, C.A.1    Autenrieth, I.B.2    Peschel, A.3
  • 138
    • 85027958029 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: Modulators of the microbiome and inflammation
    • Royet, J., Gupta, D. & Dziarski, R. Peptidoglycan recognition proteins: modulators of the microbiome and inflammation. Nature Rev. Immunol. 11, 837-851 (2011).
    • (2011) Nature Rev. Immunol. , vol.11 , pp. 837-851
    • Royet, J.1    Gupta, D.2    Dziarski, R.3
  • 139
    • 0031596818 scopus 로고    scopus 로고
    • Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears
    • Qu, X. D. & Lehrer, R. I. Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears. Infect. Immun. 66, 2791-2797 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 2791-2797
    • Qu, X.D.1    Lehrer, R.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.