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Volumn 181, Issue 7, 2008, Pages 4945-4954

Neutrophil elastase mediates innate host protection against Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

LEUKOCYTE ELASTASE; OUTER MEMBRANE PROTEIN F; OUTER MEMBRANE PROTEIN;

EID: 58149306382     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.181.7.4945     Document Type: Article
Times cited : (81)

References (55)
  • 1
    • 39049085847 scopus 로고    scopus 로고
    • Acute lower respiratory tract infection
    • Mizgerd, J. P. 2008. Acute lower respiratory tract infection. N. Engl. J. Med. 358: 716-727.
    • (2008) N. Engl. J. Med. , vol.358 , pp. 716-727
    • Mizgerd, J.P.1
  • 2
    • 0030077370 scopus 로고    scopus 로고
    • Leukocyte disorders: Quantitative and qualitative disorders of the neutrophil, part 2
    • Boxer, L. A., and R. A. Blackwood. 1996. Leukocyte disorders: quantitative and qualitative disorders of the neutrophil, part 2. Pediatr. Rev. 17: 47-50.
    • (1996) Pediatr. Rev. , vol.17 , pp. 47-50
    • Boxer, L.A.1    Blackwood, R.A.2
  • 3
    • 0037296467 scopus 로고    scopus 로고
    • Neutrophil abnormalities
    • Boxer, L. A. 2003. Neutrophil abnormalities. Pediatr. Rev. 24: 52-62.
    • (2003) Pediatr. Rev. , vol.24 , pp. 52-62
    • Boxer, L.A.1
  • 5
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton, M. B., A. J. Kettle, and C. C. Winterbourn. 1998. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92: 3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 6
    • 0032880505 scopus 로고    scopus 로고
    • Oxygen-independent microbicidal mechanisms of phagocytes
    • Ganz, T. 1999. Oxygen-independent microbicidal mechanisms of phagocytes. Proc. Assoc. Am. Physicians 111: 390-395.
    • (1999) Proc. Assoc. Am. Physicians , vol.111 , pp. 390-395
    • Ganz, T.1
  • 7
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • DOI 10.1021/bi00431a001
    • Bode, W., E. Meyer, Jr., and J. C. Powers. 1989. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28: 1951-1963. (Pubitemid 19084420)
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 1951-1963
    • Bode, W.1    Meyer Jr., E.2    Powers, J.C.3
  • 8
    • 0028787054 scopus 로고
    • Nonisotropic enzyme-inhibitor interactions: A novel nonoxidative mechanism for quantum proteolysis by human neutrophils
    • Liou, T. G., and E. J. Campbell. 1995. Nonisotropic enzyme-inhibitor interactions: a novel nonoxidative mechanism for quantum proteolysis by human neutrophils. Biochemistry 34: 16171-16177.
    • (1995) Biochemistry , vol.34 , pp. 16171-16177
    • Liou, T.G.1    Campbell, E.J.2
  • 9
    • 0030627476 scopus 로고    scopus 로고
    • Characterization of the mouse neutrophil elastase gene and localization to Chromosome 10
    • DOI 10.1007/s003359900337
    • Belaaouaj, A., B. C. Walsh, N. A. Jenkins, N. G. Copeland, and S. D. Shapiro. 1997. Characterization of the mouse neutrophil elastase gene and localization to chromosome 10. Mamm. Genome 8: 5-8. (Pubitemid 28060735)
    • (1997) Mammalian Genome , vol.8 , Issue.1 , pp. 5-8
    • Belaaouaj, A.1    Walsh, B.C.2    Jenkins, N.A.3    Copeland, N.G.4    Shapiro, S.D.5
  • 10
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • DOI 10.1038/nm0598-615
    • Belaaouaj, A., R. McCarthy, M. Baumann, Z. Gao, T. J. Ley, S. N. Abraham, and S. D. Shapiro. 1998. Mice lacking neutrophil elastase reveal impaired host defense against Gram negative bacterial sepsis. Nat. Med. 4: 615-618. (Pubitemid 28237363)
    • (1998) Nature Medicine , vol.4 , Issue.5 , pp. 615-618
    • Belaaouaj, A.1    Mccarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6    Shapiro, S.D.7
  • 11
    • 0034144636 scopus 로고    scopus 로고
    • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G
    • Tkalcevic, J., M. Novelli, M. Phylactides, J. P. Iredale, A. W. Segal, and J. Roes. 2000. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity 12: 201-210. (Pubitemid 30398634)
    • (2000) Immunity , vol.12 , Issue.2 , pp. 201-210
    • Tkalcevic, J.1    Novelli, M.2    Phylactides, M.3    Iredale, J.P.4    Segal, A.W.5    Roes, J.6
  • 13
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein a in Escherichia coli killing by neutrophil elastase
    • DOI 10.1126/science.289.5482.1185
    • Belaaouaj, A., K. S. Kim, and S. D. Shapiro. 2000. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 289: 1185-1188. (Pubitemid 30650729)
    • (2000) Science , vol.289 , Issue.5482 , pp. 1185-1187
    • Belaaouaj, A.A.1    Kwang Sik, K.2    Shapiro, S.D.3
  • 14
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • DOI 10.1038/417091a
    • Weinrauch, Y., D. Drujan, S. D. Shapiro, J. Weiss, and A. Zychlinsky. 2002. Neutrophil elastase targets virulence factors of enterobacteria. Nature 417: 91-94. (Pubitemid 34498822)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 15
    • 0346734183 scopus 로고    scopus 로고
    • Neutrophil serine proteinases cleave bacterial flagellin, abrogating its host response-inducing activity
    • Lopez-boado, Y. S., M. Espinola, S. Bahr, and A. Belaaouaj. 2004. Neutrophil serine proteinases cleave bacterial flagellin, abrogating its host response-inducing activity. J. Immunol. 172: 509-515.
    • (2004) J. Immunol. , vol.172 , pp. 509-515
    • Lopez-boado, Y.S.1    Espinola, M.2    Bahr, S.3    Belaaouaj, A.4
  • 17
    • 0033847562 scopus 로고    scopus 로고
    • Establishment of Pseudomonas aeruginosa infection: Lessons from a versatile opportunist
    • Lyczak, J. B., C. L. Cannon, and G. B. Pier. 2000. Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microbes Infect. 2: 1051-1060.
    • (2000) Microbes Infect. , vol.2 , pp. 1051-1060
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 21
    • 0037397798 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pneumonia
    • Garau, J., and L. Gomez. 2003. Pseudomonas aeruginosa pneumonia. Curr. Opin. Infect. Dis. 16: 135-143.
    • (2003) Curr. Opin. Infect. Dis. , vol.16 , pp. 135-143
    • Garau, J.1    Gomez, L.2
  • 22
    • 27244449960 scopus 로고    scopus 로고
    • The microbiology of ventilator-associated pneumonia
    • Park, D. R. 2005. The microbiology of ventilator-associated pneumonia. Respir. Care 50: 742-763.
    • (2005) Respir. Care , vol.50 , pp. 742-763
    • Park, D.R.1
  • 23
    • 1842556194 scopus 로고    scopus 로고
    • Deficiency in neutrophil elastase does not impair neutrophil recruitment to inflamed sites
    • Hirche, T. O., J. J. Atkinson, S. Bahr, and A. Belaaouaj. 2004. Deficiency in neutrophil elastase does not impair neutrophil recruitment to inflamed sites. Am. J. Respir. Cell Mol. Biol. 30: 576-584.
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.30 , pp. 576-584
    • Hirche, T.O.1    Atkinson, J.J.2    Bahr, S.3    Belaaouaj, A.4
  • 24
    • 0027174515 scopus 로고
    • Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis
    • Meyer, K. C., and J. Zimmerman. 1993. Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis. J. Lab. Clin. Med. 121: 654-661. (Pubitemid 23148691)
    • (1993) Journal of Laboratory and Clinical Medicine , vol.121 , Issue.5 , pp. 654-661
    • Meyer, K.C.1    Zimmerman, J.2
  • 27
    • 0028962836 scopus 로고
    • Proteases and antiproteases in cystic fibrosis: Pathogenetic considerations and therapeutic strategies
    • Birrer, P. 1995. Proteases and antiproteases in cystic fibrosis: pathogenetic considerations and therapeutic strategies. Respiration 62: 25-28.
    • (1995) Respiration , vol.62 , pp. 25-28
    • Birrer, P.1
  • 29
    • 0023891445 scopus 로고
    • Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene
    • Woodruff, W. A., and R. E. Hancock. 1988. Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene. J. Bacteriol. 170: 2592-2598.
    • (1988) J. Bacteriol. , vol.170 , pp. 2592-2598
    • Woodruff, W.A.1    Hancock, R.E.2
  • 30
    • 0033853378 scopus 로고    scopus 로고
    • Novel receptor-targeted fluorescent contrast agents for in vivo tumor imaging
    • DOI 10.1097/00004424-200008000-00004
    • Achilefu, S., R. B. Dorshow, J. E. Bugaj, and R. Rajagopalan. 2000. Novel receptor-targeted fluorescent contrast agents for in vivo tumor imaging. Invest. Radiol. 35: 479-485. (Pubitemid 30622015)
    • (2000) Investigative Radiology , vol.35 , Issue.8 , pp. 479-485
    • Achilefu, S.1    Dorshow, R.B.2    Bugaj, J.E.3    Rajagopalan, R.4
  • 31
    • 12444329704 scopus 로고    scopus 로고
    • Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: Effects on host defense
    • Hirche, T. O., J. P. Gaut, J. W. Heinecke, and A. Belaaouaj. 2005. Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: effects on host defense. J. Immunol. 174: 1557-1565.
    • (2005) J. Immunol. , vol.174 , pp. 1557-1565
    • Hirche, T.O.1    Gaut, J.P.2    Heinecke, J.W.3    Belaaouaj, A.4
  • 33
    • 0026625774 scopus 로고
    • Analysis of the Pseudomonas aeruginosa major outer membrane protein OprF by use of truncated OprF derivatives and monoclonal antibodies
    • Finnen, R. L., N. L. Martin, R. J. Siehnel, W. A. Woodruff, M. Rosok, and R. E. Hancock. 1992. Analysis of the Pseudomonas aeruginosa major outer membrane protein OprF by use of truncated OprF derivatives and monoclonal antibodies. J. Bacteriol. 174: 4977-4985.
    • (1992) J. Bacteriol. , vol.174 , pp. 4977-4985
    • Finnen, R.L.1    Martin, N.L.2    Siehnel, R.J.3    Woodruff, W.A.4    Rosok, M.5    Hancock, R.E.6
  • 36
    • 0029899658 scopus 로고    scopus 로고
    • Purification of hydrophobic integral membrane proteins from Mycoplasma hyopneumoniae by reversed-phase high-performance liquid chromatography
    • DOI 10.1016/0021-9673(96)00005-2
    • Lee, R. P., S. W. Doughty, K. Ashman, and J. Walker. 1996. Purification of hydrophobic integral membrane proteins from Mycoplasma hyopneumoniae by reversed-phase high-performance liquid chromatography. J. Chromatogr. 737: 273-279. (Pubitemid 26193237)
    • (1996) Journal of Chromatography a , vol.737 , Issue.2 , pp. 273-279
    • Lee, R.P.1    Doughty, S.W.2    Ashman, K.3    Walker, J.4
  • 38
    • 0021170801 scopus 로고
    • Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa
    • Loh, B., C. Grant, and R. E. Hancock. 1984. Use of the fluorescent probe 1-Nphenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 26: 546-551. (Pubitemid 14018094)
    • (1984) Antimicrobial Agents and Chemotherapy , vol.26 , Issue.4 , pp. 546-551
    • Loh, B.1    Grant, C.2    Hancock, R.E.W.3
  • 39
    • 0021282341 scopus 로고
    • Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane
    • Hancock, R. E., and P. G. Wong. 1984. Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane. Antimicrob. Agents Chemother. 26: 48-52. (Pubitemid 14086723)
    • (1984) Antimicrobial Agents and Chemotherapy , vol.26 , Issue.1 , pp. 48-52
    • Hancock, R.E.W.1    Wong, P.G.W.2
  • 40
    • 0036024103 scopus 로고    scopus 로고
    • Molecular mechanisms of neutrophil recruitment elicited by bacteria in the lungs
    • Mizgerd, J. P. 2002. Molecular mechanisms of neutrophil recruitment elicited by bacteria in the lungs. Semin. Immunol. 14: 123-132.
    • (2002) Semin. Immunol. , vol.14 , pp. 123-132
    • Mizgerd, J.P.1
  • 42
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen, C. A., M. A. Campbell, P. L. Sannes, S. S. Boukedes, and E. J. Campbell. 1995. Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131: 775-789.
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 43
    • 0032806926 scopus 로고    scopus 로고
    • PAF-induced elastase-dependent neutrophil transendothelial migration is associated with the mobilization of elastase to the neutrophil surface and localization to the migrating front
    • Cepinskas, G., M. Sandig, and P. R. Kvietys. 1999. PAF-induced elastase-dependent neutrophil transendothelial migration is associated with the mobilization of elastase to the neutrophil surface and localization to the migrating front. J. Cell Sci. 112: 1937-1945. (Pubitemid 29338818)
    • (1999) Journal of Cell Science , vol.112 , Issue.12 , pp. 1937-1945
    • Cepinskas, G.1    Sandig, M.2    Kvietys, P.R.3
  • 44
    • 0031813752 scopus 로고    scopus 로고
    • Role of alveolar macrophages in initiation and regulation of inflammation in Pseudomonas aeruginosa pneumonia
    • Kooguchi, K., S. Hashimoto, A. Kobayashi, Y. Kitamura, I. Kudoh, J. Wiener-Kronish, and T. Sawa. 1998. Role of alveolar macrophages in initiation and regulation of inflammation in Pseudomonas aeruginosa pneumonia. Infect. Immun. 66: 3164-3169. (Pubitemid 28303112)
    • (1998) Infection and Immunity , vol.66 , Issue.7 , pp. 3164-3169
    • Kooguchi, K.1    Hashimoto, S.2    Kobayashi, A.3    Kitamura, Y.4    Kudoh, I.5    Wiener-Kronish, J.6    Sawa, T.7
  • 45
    • 0022546719 scopus 로고
    • Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F
    • Woodruff, W. A., T. R. Parr, Jr., R. E. Hancock, L. F. Hanne, T. I. Nicas, and B. H. Iglewski. 1986. Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F. J. Bacteriol. 167: 473-479.
    • (1986) J. Bacteriol. , vol.167 , pp. 473-479
    • Woodruff, W.A.1    Parr Jr., T.R.2    Hancock, R.E.3    Hanne, L.F.4    Nicas, T.I.5    Iglewski, B.H.6
  • 46
    • 0024501638 scopus 로고
    • Role of protein F in maintaining structural integrity of the Pseudomonas aeruginosa outer membrane
    • Gotoh, N., H. Wakebe, E. Yoshihara, T. Nakae, and T. Nishino. 1989. Role of protein F in maintaining structural integrity of the Pseudomonas aeruginosa outer membrane. J. Bacteriol. 171: 983-990. (Pubitemid 19053487)
    • (1989) Journal of Bacteriology , vol.171 , Issue.2 , pp. 983-990
    • Gotoh, N.1    Wakebe, H.2    Yoshihara, E.3    Nakae, T.4    Nishino, T.5
  • 47
    • 0033816975 scopus 로고    scopus 로고
    • The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: Correlation with a three-dimensional model
    • Brinkman, F. S., M. Bains, and R. E. Hancock. 2000. The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: correlation with a three-dimensional model. J. Bacteriol. 182: 5251-5255.
    • (2000) J. Bacteriol. , vol.182 , pp. 5251-5255
    • Brinkman, F.S.1    Bains, M.2    Hancock, R.E.3
  • 49
    • 33845481599 scopus 로고    scopus 로고
    • Neutrophil elastase, an innate immunity effector molecule, represses flagellin transcription in Pseudomonas aeruginosa
    • DOI 10.1128/IAI.00922-06
    • Sonawane, A., J. Jyot, R. During, and R. Ramphal. 2006. Neutrophil elastase, an innate immunity effector molecule, represses flagellin transcription in Pseudomonas aeruginosa. Infect. Immun. 74: 6682-6689. (Pubitemid 44913142)
    • (2006) Infection and Immunity , vol.74 , Issue.12 , pp. 6682-6689
    • Sonawane, A.1    Jyot, J.2    During, R.3    Ramphal, R.4
  • 50
    • 0028878069 scopus 로고
    • Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF
    • Rawling, E. G., N. L. Martin, and R. E. Hancock. 1995. Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF. Infect. Immun. 63: 38-42.
    • (1995) Infect. Immun. , vol.63 , pp. 38-42
    • Rawling, E.G.1    Martin, N.L.2    Hancock, R.E.3
  • 51
    • 0002016013 scopus 로고
    • Elastases: Catalytic and biological properties
    • R. Mecham, ed. Academic Press, New York
    • Bieth, J. G. 1986. Elastases: catalytic and biological properties. In Regulation of Matrix Accumulation. R. Mecham, ed. Academic Press, New York, pp. 2228-2232.
    • (1986) Regulation of Matrix Accumulation , pp. 2228-2232
    • Bieth, J.G.1
  • 53
    • 33846942667 scopus 로고    scopus 로고
    • Cathepsin-G interferes with clearance of Pseudomonas aeruginosa from mouse lungs
    • DOI 10.1203/01.pdr.0000250043.90468.c2, PII 0000645020070100000007
    • Sedor, J., L. Hogue, K. Akers, S. Boslaugh, J. Schreiber, and T. Ferkol. 2007. Cathepsin-G interferes with clearance of Pseudomonas aeruginosa from mouse lungs. Pediatr. Res. 61: 26-31. (Pubitemid 46352311)
    • (2007) Pediatric Research , vol.61 , Issue.1 , pp. 26-31
    • Sedor, J.1    Hogue, L.2    Akers, K.3    Boslaugh, S.4    Schreiber, J.5    Ferkol, T.6
  • 54
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli omP protein
    • Woodruff, W. A., and R. E. Hancock. 1989. Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J. Bacteriol. 171: 3304-3309. (Pubitemid 19145686)
    • (1989) Journal of Bacteriology , vol.171 , Issue.6 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.W.2
  • 55
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • Pham, C. T. 2006. Neutrophil serine proteases: specific regulators of inflammation. Nat. Rev. Immunol. 6: 541-550.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 541-550
    • Pham, C.T.1


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