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Volumn 92, Issue 4, 2012, Pages 841-849

Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus

Author keywords

Calcium; Escherichia coli; Ionomycin; NETs; Pseudomonas aeruginosa; Staphylococcus aureus

Indexed keywords

IONOMYCIN; MYELOPEROXIDASE; OXIDIZING AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 84866177387     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.1211601     Document Type: Article
Times cited : (334)

References (50)
  • 1
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton, M. B., Kettle, A. J., Winterbourn, C. C. (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
  • 2
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • Nauseef, W. M. (2007) How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 219, 88-102.
    • (2007) Immunol. Rev. , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 6
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • Urban, C. F., Reichard, U., Brinkmann, V., Zychlinsky, A. (2006) Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell. Microbiol. 8, 668-676.
    • (2006) Cell. Microbiol. , vol.8 , pp. 668-676
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3    Zychlinsky, A.4
  • 7
    • 84857862903 scopus 로고    scopus 로고
    • Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide
    • Parker, H., Albrett, A. M., Kettle, A. J., Winterbourn, C. C. (2012) Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide. J. Leukoc. Biol. 91, 369-376.
    • (2012) J. Leukoc. Biol. , vol.91 , pp. 369-376
    • Parker, H.1    Albrett, A.M.2    Kettle, A.J.3    Winterbourn, C.C.4
  • 8
    • 70349263992 scopus 로고    scopus 로고
    • Innate immunity turned inside-out: Antimicrobial defense by phagocyte extracellular traps
    • Von Kockritz-Blickwede, M., Nizet, V. (2009) Innate immunity turned inside-out: antimicrobial defense by phagocyte extracellular traps. J. Mol. Med. (Berl.) 87, 775-783.
    • (2009) J. Mol. Med. (Berl.) , vol.87 , pp. 775-783
    • von Kockritz-Blickwede, M.1    Nizet, V.2
  • 11
    • 80052510176 scopus 로고    scopus 로고
    • Excessive neutrophils and neutrophil extracellular traps contribute to acute lung injury of influenza pneumonitis
    • Narasaraju, T., Yang, E., Samy, R. P., Ng, H. H., Poh, W. P., Liew, A. A., Phoon, M. C., van Rooijen, N., Chow, V. T. (2011) Excessive neutrophils and neutrophil extracellular traps contribute to acute lung injury of influenza pneumonitis. Am. J. Pathol. 179, 199-210.
    • (2011) Am. J. Pathol. , vol.179 , pp. 199-210
    • Narasaraju, T.1    Yang, E.2    Samy, R.P.3    Ng, H.H.4    Poh, W.P.5    Liew, A.A.6    Phoon, M.C.7    van Rooijen, N.8    Chow, V.T.9
  • 13
    • 70350001718 scopus 로고    scopus 로고
    • Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps
    • Yousefi, S., Mihalache, C., Kozlowski, E., Schmid, I., Simon, H. U. (2009) Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps. Cell Death Differ. 16, 1438-1444.
    • (2009) Cell Death Differ. , vol.16 , pp. 1438-1444
    • Yousefi, S.1    Mihalache, C.2    Kozlowski, E.3    Schmid, I.4    Simon, H.U.5
  • 16
    • 34248524638 scopus 로고    scopus 로고
    • Unconventional roles of the NADPH oxidase: Signaling, ion homeostasis, and cell death
    • Steinberg, B. E., Grinstein, S. (2007) Unconventional roles of the NADPH oxidase: signaling, ion homeostasis, and cell death. Sci. STKE 2007, pe11.
    • (2007) Sci. STKE , vol.2007
    • Steinberg, B.E.1    Grinstein, S.2
  • 20
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • Papayannopoulos, V., Metzler, K. D., Hakkim, A., Zychlinsky, A. (2010) Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps. J. Cell Biol. 191, 677-691.
    • (2010) J. Cell Biol. , vol.191 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 23
    • 84861034431 scopus 로고    scopus 로고
    • The impact of various reactive oxygen species on the formation of neutrophil extracellular traps
    • Kirchner, T., Moller, S., Klinger, M., Solbach, W., Laskay, T., Behnen, M. (2012) The impact of various reactive oxygen species on the formation of neutrophil extracellular traps. Mediators Inflamm. 2012, 849136.
    • (2012) Mediators Inflamm. , vol.2012 , pp. 849136
    • Kirchner, T.1    Moller, S.2    Klinger, M.3    Solbach, W.4    Laskay, T.5    Behnen, M.6
  • 24
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle, A. J., Winterbourn, C. C. (1997) Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox. Rep. 3, 3-15.
    • (1997) Redox. Rep. , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 25
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S. J. (2005) Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77, 598-625.
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 27
    • 2542553381 scopus 로고    scopus 로고
    • The mechanism for activation of the neutrophil NADPH-oxidase by the peptides formyl-Met-Leu-Phe and Trp-Lys-Tyr-Met-Val-Met differs from that for interleukin-8
    • Fu, H., Bylund, J., Karlsson, A., Pellme, S., Dahlgren, C. (2004) The mechanism for activation of the neutrophil NADPH-oxidase by the peptides formyl-Met-Leu-Phe and Trp-Lys-Tyr-Met-Val-Met differs from that for interleukin-8. Immunology 112, 201-210.
    • (2004) Immunology , vol.112 , pp. 201-210
    • Fu, H.1    Bylund, J.2    Karlsson, A.3    Pellme, S.4    Dahlgren, C.5
  • 29
    • 77956245423 scopus 로고    scopus 로고
    • PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps
    • Li, P., Li, M., Lindberg, M. R., Kennett, M. J., Xiong, N., Wang, Y. (2010) PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps. J. Exp. Med. 207, 1853-1862.
    • (2010) J. Exp. Med. , vol.207 , pp. 1853-1862
    • Li, P.1    Li, M.2    Lindberg, M.R.3    Kennett, M.J.4    Xiong, N.5    Wang, Y.6
  • 30
    • 55549117812 scopus 로고    scopus 로고
    • Regulation of superoxide production in neutrophils: Role of calcium influx
    • Brechard, S., Tschirhart, E. J. (2008) Regulation of superoxide production in neutrophils: role of calcium influx. J. Leukoc. Biol. 84, 1223-1237.
    • (2008) J. Leukoc. Biol. , vol.84 , pp. 1223-1237
    • Brechard, S.1    Tschirhart, E.J.2
  • 31
    • 77954681058 scopus 로고    scopus 로고
    • The role of calcium signaling in phagocytosis
    • Nunes, P., Demaurex, N. (2010) The role of calcium signaling in phagocytosis. J. Leukoc. Biol. 88, 57-68.
    • (2010) J. Leukoc. Biol. , vol.88 , pp. 57-68
    • Nunes, P.1    Demaurex, N.2
  • 32
    • 0035046590 scopus 로고    scopus 로고
    • IgG from myeloperoxidase-antineutrophil cytoplasmic antibodypositive patients stimulates greater activation of primed neutrophils than IgG from proteinase 3-antineutrophil cytosplasmic antibody-positive patients
    • Harper, L., Radford, D., Plant, T., Drayson, M., Adu, D., Savage, C. O. (2001) IgG from myeloperoxidase-antineutrophil cytoplasmic antibodypositive patients stimulates greater activation of primed neutrophils than IgG from proteinase 3-antineutrophil cytosplasmic antibody-positive patients. Arthritis Rheum. 44, 921-930.
    • (2001) Arthritis Rheum. , vol.44 , pp. 921-930
    • Harper, L.1    Radford, D.2    Plant, T.3    Drayson, M.4    Adu, D.5    Savage, C.O.6
  • 33
    • 70149115487 scopus 로고    scopus 로고
    • The functional significance behind expressing two IL-8 receptor types on PMN
    • Stillie, R., Farooq, S. M., Gordon, J. R., Stadnyk, A. W. (2009) The functional significance behind expressing two IL-8 receptor types on PMN. J. Leukoc. Biol. 86, 529-543.
    • (2009) J. Leukoc. Biol. , vol.86 , pp. 529-543
    • Stillie, R.1    Farooq, S.M.2    Gordon, J.R.3    Stadnyk, A.W.4
  • 35
    • 0028240904 scopus 로고
    • Superoxide-dependent hydroxylation by myeloperoxidase
    • Kettle, A. J., Winterbourn, C. C. (1994) Superoxide-dependent hydroxylation by myeloperoxidase. J. Biol. Chem. 269, 17146-17151.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17146-17151
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 36
    • 80053351733 scopus 로고    scopus 로고
    • Rac2 is required for the formation of neutrophil extracellular traps
    • Lim, M. B., Kuiper, J. W., Katchky, A., Goldberg, H., Glogauer, M. (2011) Rac2 is required for the formation of neutrophil extracellular traps. J. Leukoc. Biol. 90, 771-776.
    • (2011) J. Leukoc. Biol. , vol.90 , pp. 771-776
    • Lim, M.B.1    Kuiper, J.W.2    Katchky, A.3    Goldberg, H.4    Glogauer, M.5
  • 37
    • 0029913108 scopus 로고    scopus 로고
    • Phorbol myristate acetate-induced NADPH oxidase activity in human neutrophils: Only half the story has been told
    • Lundqvist, H., Follin, P., Khalfan, L., Dahlgren, C. (1996) Phorbol myristate acetate-induced NADPH oxidase activity in human neutrophils: only half the story has been told. J. Leukoc. Biol. 59, 270-279.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 270-279
    • Lundqvist, H.1    Follin, P.2    Khalfan, L.3    Dahlgren, C.4
  • 38
    • 0023924814 scopus 로고
    • Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance
    • Beckman, J. S., Minor, R. L., Jr., White, C. W., Repine, J. E., Rosen, G. M., Freeman, B. A. (1988) Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance. J. Biol. Chem. 263, 6884-6892.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6884-6892
    • Beckman, J.S.1    Minor Jr., R.L.2    White, C.W.3    Repine, J.E.4    Rosen, G.M.5    Freeman, B.A.6
  • 39
  • 41
    • 0029846572 scopus 로고    scopus 로고
    • Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils
    • Hampton, M. B., Kettle, A. J., Winterbourn, C. C. (1996) Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils. Infect. Immun. 64, 3512-3517.
    • (1996) Infect. Immun. , vol.64 , pp. 3512-3517
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 43
    • 40749128547 scopus 로고    scopus 로고
    • Histone deimination as a response to inflammatory stimuli in neutrophils
    • Neeli, I., Khan, S. N., Radic, M. (2008) Histone deimination as a response to inflammatory stimuli in neutrophils. J. Immunol. 180, 1895-1902.
    • (2008) J. Immunol. , vol.180 , pp. 1895-1902
    • Neeli, I.1    Khan, S.N.2    Radic, M.3
  • 44
    • 77953435880 scopus 로고    scopus 로고
    • Regulation of extracellular chromatin release from neutrophils
    • Neeli, I., Dwivedi, N., Khan, S., Radic, M. (2009) Regulation of extracellular chromatin release from neutrophils. J. Innate Immun. 1, 194-201.
    • (2009) J. Innate Immun. , vol.1 , pp. 194-201
    • Neeli, I.1    Dwivedi, N.2    Khan, S.3    Radic, M.4
  • 45
    • 0344299171 scopus 로고    scopus 로고
    • NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils
    • Vaissiere, C., Le Cabec, V., Maridonneau-Parini, I. (1999) NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils. J. Leukoc. Biol. 65, 629-634.
    • (1999) J. Leukoc. Biol. , vol.65 , pp. 629-634
    • Vaissiere, C.1    Le Cabec, V.2    Maridonneau-Parini, I.3
  • 46
    • 5344271785 scopus 로고    scopus 로고
    • Chlorine transfer between glycine, taurine, and histamine: Reaction rates and impact on cellular reactivity
    • Peskin, A. V., Midwinter, R. G., Harwood, D. T., Winterbourn, C. C. (2004) Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity. Free Radic. Biol. Med. 37, 1622-1630.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1622-1630
    • Peskin, A.V.1    Midwinter, R.G.2    Harwood, D.T.3    Winterbourn, C.C.4
  • 47
    • 0026782751 scopus 로고
    • Activation of the oxygen-radical-generating system in granules of intact human neutrophils by a calcium ionophore (ionomycin)
    • Dahlgren, C., Johansson, A., Lundqvist, H., Bjerrum, O. W., Borregaard, N. (1992) Activation of the oxygen-radical-generating system in granules of intact human neutrophils by a calcium ionophore (ionomycin). Biochim. Biophys. Acta 1137, 182-188.
    • (1992) Biochim. Biophys. Acta , vol.1137 , pp. 182-188
    • Dahlgren, C.1    Johansson, A.2    Lundqvist, H.3    Bjerrum, O.W.4    Borregaard, N.5
  • 48
    • 0023206032 scopus 로고
    • Priming of neutrophils and macrophages for enhanced release of superoxide anion by the calcium ionophore ionomycin. Implications for regulation of the respiratory burst
    • Finkel, T. H., Pabst, M. J., Suzuki, H., Guthrie, L. A., Forehand, J. R., Phillips, W. A., Johnston R. B., Jr., (1987) Priming of neutrophils and macrophages for enhanced release of superoxide anion by the calcium ionophore ionomycin. Implications for regulation of the respiratory burst. J. Biol. Chem. 262, 12589-12596.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12589-12596
    • Finkel, T.H.1    Pabst, M.J.2    Suzuki, H.3    Guthrie, L.A.4    Forehand, J.R.5    Phillips, W.A.6    Johnston Jr., R.B.7
  • 49
    • 0022979861 scopus 로고
    • Identification of distinct activation pathways of the human neutrophil NADPHoxidase
    • Maridonneau-Parini, I., Tringale, S. M., Tauber, A. I. (1986) Identification of distinct activation pathways of the human neutrophil NADPHoxidase. J. Immunol. 137, 2925-2929.
    • (1986) J. Immunol. , vol.137 , pp. 2925-2929
    • Maridonneau-Parini, I.1    Tringale, S.M.2    Tauber, A.I.3
  • 50
    • 0032621388 scopus 로고    scopus 로고
    • Dependence of superoxide anion production on extracellular and intracellular calcium ions and protein kinase C in PMA-stimulated bovine neutrophils
    • Allard, B., Long, E., Block, E., Zhao, X. (1999) Dependence of superoxide anion production on extracellular and intracellular calcium ions and protein kinase C in PMA-stimulated bovine neutrophils. Can. J. Vet. Res. 63, 13-17.
    • (1999) Can. J. Vet. Res. , vol.63 , pp. 13-17
    • Allard, B.1    Long, E.2    Block, E.3    Zhao, X.4


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