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Volumn 172, Issue 6, 2004, Pages 3758-3765

The Human Cationic Peptide LL-37 Induces Activation of the Extracellular Signal-Regulated Kinase and p38 Kinase Pathways in Primary Human Monocytes

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CELL PROTEIN; CHEMOKINE; COLONY STIMULATING FACTOR 1; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR 1; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 8; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; TRANSCRIPTION FACTOR ELK 1; UNCLASSIFIED DRUG;

EID: 1542724426     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.6.3758     Document Type: Article
Times cited : (216)

References (50)
  • 1
    • 0029900207 scopus 로고    scopus 로고
    • Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells
    • Diamond, G., J. P. Russell, and C. L. Bevins. 1996. Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells. Proc. Natl. Acad. Sci. USA 93:5156.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5156
    • Diamond, G.1    Russell, J.P.2    Bevins, C.L.3
  • 2
    • 0037218616 scopus 로고    scopus 로고
    • By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide
    • Liu, L., A. A. Roberts, and T. Ganz. 2003. By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide. J. Immunol. 170:575.
    • (2003) J. Immunol. , vol.170 , pp. 575
    • Liu, L.1    Roberts, A.A.2    Ganz, T.3
  • 4
    • 0032739820 scopus 로고    scopus 로고
    • In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa
    • Giacometti, A., O. Cirioni, F. Barchiesi, M. Fortuna, and G. Scalise. 1999. In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa. J. Antimicrob. Chemother. 44:641.
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 641
    • Giacometti, A.1    Cirioni, O.2    Barchiesi, F.3    Fortuna, M.4    Scalise, G.5
  • 5
    • 0034201213 scopus 로고    scopus 로고
    • Neutrophil α-defensin human neutrophil peptide modulates cytokine production in human monocytes and adhesion molecule expression in endothelial cells
    • Chaly, Y. V., E. M. Paleolog, T. S. Kolesnikova, Tikhonov, I. I., E. V. Petratchenko, and N. N. Voitenok. 2000. Neurrophil α-defensin human neutrophil peptide modulates cytokine production in human monocytes and adhesion molecule expression in endothelial cells. Eur. Cytokine Network. 11:257.
    • (2000) Eur. Cytokine Network. , vol.11 , pp. 257
    • Chaly, Y.V.1    Paleolog, E.M.2    Kolesnikova, T.S.3    Tikhonov, I.I.4    Petratchenko, E.V.5    Voitenok, N.N.6
  • 6
    • 0030038197 scopus 로고    scopus 로고
    • Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
    • Chertov, O., D. F. Michiel, L. Xu, J. M. Wang, K. Tani, W. J. Murphy, D. L. Longo, D. D. Taub, and J. J. Oppenheim. 1996. Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J. Biol. Chem. 271:2935.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2935
    • Chertov, O.1    Michiel, D.F.2    Xu, L.3    Wang, J.M.4    Tani, K.5    Murphy, W.J.6    Longo, D.L.7    Taub, D.D.8    Oppenheim, J.J.9
  • 7
    • 0031925180 scopus 로고    scopus 로고
    • Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia
    • Kirikae, T., M. Hirata, H. Yamasu, F. Kirikae, H. Tamura, F. Kayama, K. Nakatsuka, T. Yokochi, and M. Nakano. 1998. Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia. Infect. Immun. 66:1861.
    • (1998) Infect. Immun. , vol.66 , pp. 1861
    • Kirikae, T.1    Hirata, M.2    Yamasu, H.3    Kirikae, F.4    Tamura, H.5    Kayama, F.6    Nakatsuka, K.7    Yokochi, T.8    Nakano, M.9
  • 10
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer, R. I., and T. Ganz. 2002. Cathelicidins: a family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 9:18.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18
    • Lehrer, R.I.1    Ganz, T.2
  • 11
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock, R. E. W., and G. Diamond. 2000. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol. 3:402.
    • (2000) Trends Microbiol. , vol.3 , pp. 402
    • Hancock, R.E.W.1    Diamond, G.2
  • 12
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL 1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De, Y., Q. Chen, A. P. Schmidt, G. M. Anderson, J. M. Wang, J. Wooters, J. J. Oppenheim, and O. Chertov. 2000. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL 1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192:1069.
    • (2000) J. Exp. Med. , vol.192 , pp. 1069
    • De, Y.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 13
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott, M. G., D. J. Davidson, M. R. Gold, D. Bowdish, and R. E. W. Hancock, 2002. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J. Immunol. 169:3883.
    • (2002) J. Immunol. , vol.169 , pp. 3883
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.W.5
  • 15
    • 0032708355 scopus 로고    scopus 로고
    • Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide
    • Bals, R., D. J. Weiner, A. D. Moscioni, R. L. Meegalla, and J. M. Wilson. 1999. Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Infect. Immun. 67:6084.
    • (1999) Infect. Immun. , vol.67 , pp. 6084
    • Bals, R.1    Weiner, D.J.2    Moscioni, A.D.3    Meegalla, R.L.4    Wilson, J.M.5
  • 17
    • 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., M. F. Nilsson, G. Kratz, G. Weber, O. Sorensen, N. Borregaard, and M. Stahle-Backdahl, 2003. 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. 120:379.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 379
    • Heilborn, J.D.1    Nilsson, M.F.2    Kratz, G.3    Weber, G.4    Sorensen, O.5    Borregaard, N.6    Stahle-Backdahl, M.7
  • 19
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence
    • Zaiou, M., V. Nizet, and R. L. Gallo. 2003. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J. Invest. Dermatol. 120:810.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 810
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 21
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α
    • Sallusto, F., and A. Lanzavecchia. 1994. Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α. J. Exp. Med. 179:1109.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109
    • Sallusto, F.1    Lanzavecchia, A.2
  • 22
    • 0018889361 scopus 로고
    • Isolation of human T lymphocytes: Comparison between nylon wool filtration and rosetting with neuraminidase (VCN) and 2-aminoethylisothiouronium bromide (AET)-treated sheep red blood cells (SRBC)
    • Indiveri, F., J. Huddlestone, M. A. Pellegrino, and S. Ferrone. 1980. Isolation of human T lymphocytes: comparison between nylon wool filtration and rosetting with neuraminidase (VCN) and 2-aminoethylisothiouronium bromide (AET)-treated sheep red blood cells (SRBC). J. Immunol. Methods 34:107.
    • (1980) J. Immunol. Methods , vol.34 , pp. 107
    • Indiveri, F.1    Huddlestone, J.2    Pellegrino, M.A.3    Ferrone, S.4
  • 24
    • 0032509199 scopus 로고    scopus 로고
    • Apolipoprotein A-1 binds and inhibits the human antibacterial/cytotoxic peptide LL-37
    • Wang, Y., B. Agerberth, A. Lothgren, A. Almstedt, and J. Johansson. 1998. Apolipoprotein A-1 binds and inhibits the human antibacterial/cytotoxic peptide LL-37. J. Biol. Chem. 273:33115.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33115
    • Wang, Y.1    Agerberth, B.2    Lothgren, A.3    Almstedt, A.4    Johansson, J.5
  • 25
    • 0030805339 scopus 로고    scopus 로고
    • An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma
    • Soronsen, O., J. B. Cowland, J. Askaa, and N. Borregaard. 1997. An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma. J. Immunol. Methods 206:53.
    • (1997) J. Immunol. Methods , vol.206 , pp. 53
    • Soronsen, O.1    Cowland, J.B.2    Askaa, J.3    Borregaard, N.4
  • 26
    • 0036528903 scopus 로고    scopus 로고
    • Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection
    • Schaller-Bals, S., A. Schulze, and R. Bals. 2002. Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am. J. Respir. Crit. Care Med. 165:992.
    • (2002) Am. J. Respir. Crit. Care Med. , vol.165 , pp. 992
    • Schaller-Bals, S.1    Schulze, A.2    Bals, R.3
  • 27
    • 0026812989 scopus 로고
    • Human upper airway structural cell-derived cytokines support human peripheral blood monocyte survival: A potential mechanism for monocyte/macrophage accumulation in the tissue
    • Xing, Z., T. Ohtoshi, P. Ralph, J. Gauldie, and M. Jordana. 1992. Human upper airway structural cell-derived cytokines support human peripheral blood monocyte survival: a potential mechanism for monocyte/macrophage accumulation in the tissue. Am. J. Respir. Cell Mol. Biol. 6:212.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 212
    • Xing, Z.1    Ohtoshi, T.2    Ralph, P.3    Gauldie, J.4    Jordana, M.5
  • 28
    • 0036964712 scopus 로고    scopus 로고
    • Activation of the p38 MAPK and ERK1/2 pathways is required for Fas-induced IL-8 production in colonic epithelial cells
    • O'Brien, D., T. O'Connor, F. Shanahan, and J. O'Connell. 2002. Activation of the p38 MAPK and ERK1/2 pathways is required for Fas-induced IL-8 production in colonic epithelial cells. Ann. NY Acad. Sci. 973:161.
    • (2002) Ann. NY Acad. Sci. , vol.973 , pp. 161
    • O'Brien, D.1    O'Connor, T.2    Shanahan, F.3    O'Connell, J.4
  • 29
    • 0038819983 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding protein and activator protein-1 transcription factors regulate the expression of interleukin-8 through the mitogen-activated protein kinase pathways in response to mechanical stretch of human airway smooth muscle cells
    • Kumar, A., A. J. Knox, and A. M. Boriek. 2003. CCAAT/enhancer-binding protein and activator protein-1 transcription factors regulate the expression of interleukin-8 through the mitogen-activated protein kinase pathways in response to mechanical stretch of human airway smooth muscle cells. J. Biol. Chem. 278:8868.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8868
    • Kumar, A.1    Knox, A.J.2    Boriek, A.M.3
  • 30
    • 0037394607 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase regulates interleukin-1β -induced IL-8 expression via an effect on the IL-8 promoter in intestinal epithelial cells
    • Parhar, K., A. Ray, U. Steinbrecher, C. Nelson, and B. Salh. 2003. The p38 mitogen-activated protein kinase regulates interleukin-1β-induced IL-8 expression via an effect on the IL-8 promoter in intestinal epithelial cells. Immunology 108:502.
    • (2003) Immunology , vol.108 , pp. 502
    • Parhar, K.1    Ray, A.2    Steinbrecher, U.3    Nelson, C.4    Salh, B.5
  • 32
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J., G. H. Gudmundsson, M. E. Rottenberg, K. D. Berndt, and B. Agerberth. 1998. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273:3718.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 33
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z., J. C. Lerman, G. H. Gudmundsson, B. Agerberth, and Y. Shai. 1999. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341:501.
    • (1999) Biochem. J. , vol.341 , pp. 501
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 34
    • 12244280184 scopus 로고    scopus 로고
    • Effects of human cathelicidin antimicrobial peptide LL-37 on lipopolysaccharide-induced nitric oxide release from rat aorta in vitro
    • Ciornei, C. D., A. Egesten, and M. Bodelsson. 2003. Effects of human cathelicidin antimicrobial peptide LL-37 on lipopolysaccharide-induced nitric oxide release from rat aorta in vitro. Acta Anaesthesiol. Scand. 47:213.
    • (2003) Acta Anaesthesiol. Scand. , vol.47 , pp. 213
    • Ciornei, C.D.1    Egesten, A.2    Bodelsson, M.3
  • 35
    • 0031756277 scopus 로고    scopus 로고
    • Structure and activity of cathelicidin antibacterial proteins
    • Wang, Y., B. Agerberth, and J. Johansson. 1998. Structure and activity of cathelicidin antibacterial proteins. J. Protein Chem. 17:522.
    • (1998) J. Protein Chem. , vol.17 , pp. 522
    • Wang, Y.1    Agerberth, B.2    Johansson, J.3
  • 36
    • 0030775610 scopus 로고    scopus 로고
    • Effect of neutrophil serine proteinases and defensins on lung epithelial cells: Modulation of cytotoxicity and IL-8 production
    • Van Wetering, S., S. P. Mannesse-Lazeroms, J. H. Dijkman, and P. S. Hiemstra. 1997. Effect of neutrophil serine proteinases and defensins on lung epithelial cells: modulation of cytotoxicity and IL-8 production. J. Leukocyte Biol. 62:217.
    • (1997) J. Leukocyte Biol. , vol.62 , pp. 217
    • Van Wetering, S.1    Mannesse-Lazeroms, S.P.2    Dijkman, J.H.3    Hiemstra, P.S.4
  • 38
    • 0032753372 scopus 로고    scopus 로고
    • Migration of leukocytes across endothelium and beyond: Molecules involved in the transmigration and fate of monocytes
    • Muller, W. A., and G. J. Randolph. 1999. Migration of leukocytes across endothelium and beyond: molecules involved in the transmigration and fate of monocytes. J. Leukocyte Biol. 66:698.
    • (1999) J. Leukocyte Biol. , vol.66 , pp. 698
    • Muller, W.A.1    Randolph, G.J.2
  • 40
    • 0028278043 scopus 로고
    • Potentiation by granulocyte macrophage colony-stimulating factor of lipopolysaccharide toxicity in mice
    • Tiegs, G., J. Barsig, B. Matiba, S. Uhlig, and A. Wendel, 1994. Potentiation by granulocyte macrophage colony-stimulating factor of lipopolysaccharide toxicity in mice. J. Clin. Invest. 93:2616.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2616
    • Tiegs, G.1    Barsig, J.2    Matiba, B.3    Uhlig, S.4    Wendel, A.5
  • 41
    • 0028243786 scopus 로고
    • Endogenous haemopoietic growth factors in neutropenia and infection
    • Cebon, J., J. E. Layton, D. Maher, and G. Morstyn. 1994. Endogenous haemopoietic growth factors in neutropenia and infection. Br. J. Haematol. 86:265.
    • (1994) Br. J. Haematol. , vol.86 , pp. 265
    • Cebon, J.1    Layton, J.E.2    Maher, D.3    Morstyn, G.4
  • 42
    • 0015386406 scopus 로고
    • Studies on the bone marrow colony stimulating factor (CSF): Relation of tissue CSF to serum CSF
    • Sheridan, J. W., and D. Metcalf. 1972. Studies on the bone marrow colony stimulating factor (CSF): relation of tissue CSF to serum CSF. J. Cell Physiol. 80:129.
    • (1972) J. Cell Physiol. , vol.80 , pp. 129
    • Sheridan, J.W.1    Metcalf, D.2
  • 43
    • 0036679853 scopus 로고    scopus 로고
    • GM-CSF in inflammation and autoimmunity
    • Hamilton, J. A. 2002. GM-CSF in inflammation and autoimmunity. Trends Immunol. 23:403.
    • (2002) Trends Immunol. , vol.23 , pp. 403
    • Hamilton, J.A.1
  • 46
    • 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., B. Agerberth, G. Ahangari, M. Stahle-Backdahl, S. Liden, H. Wigzell, and G. H. Gudmundsson. 1997. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272:15258.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 47
    • 43949174950 scopus 로고
    • Colony stimulating factors, cytokines and monocyte-macrophages: Some controversies
    • Hamilton, J. A. 1993. Colony stimulating factors, cytokines and monocyte-macrophages: some controversies. Immunol. Today 14:18.
    • (1993) Immunol. Today , vol.14 , pp. 18
    • Hamilton, J.A.1
  • 48
  • 49
    • 0034488452 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides and their multifunctional role in the immune system
    • Scott, M. G., and R. E. W. Hancock. 2000. Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit. Rev. Immunol. 20:407.
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 407
    • Scott, M.G.1    Hancock, R.E.W.2
  • 50
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson, D. J., A. J. Currie, G. S. Reid, D. M, Bowdish, K. L. MacDonald, R. C. Ma, R. E. Hancock, and D. P. Speert. 2004. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J. Immunol. 172:1146.
    • (2004) J. Immunol. , vol.172 , pp. 1146
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.3    Bowdish, D.M.4    MacDonald, K.L.5    Ma, R.C.6    Hancock, R.E.7    Speert, D.P.8


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