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Volumn 2016, Issue , 2016, Pages

Neutrophil-mediated regulation of innate and adaptive immunity: The role of myeloperoxidase

Author keywords

[No Author keywords available]

Indexed keywords

MYELOPEROXIDASE; PEROXIDASE;

EID: 84958787507     PISSN: 23148861     EISSN: 23147156     Source Type: Journal    
DOI: 10.1155/2016/2349817     Document Type: Review
Times cited : (159)

References (128)
  • 2
    • 84884851530 scopus 로고    scopus 로고
    • The neutrophil in antineutrophil cytoplasmic autoantibody-associated vasculitis
    • A. Schreiber and R. Kettritz, "The neutrophil in antineutrophil cytoplasmic autoantibody-associated vasculitis, " Journal of Leukocyte Biology, vol. 94, no. 4, pp. 623-631, 2013.
    • (2013) Journal of Leukocyte Biology , vol.94 , Issue.4 , pp. 623-631
    • Schreiber, A.1    Kettritz, R.2
  • 3
    • 78049413094 scopus 로고    scopus 로고
    • Neutrophils influence the level of antigen presentation during the immune response to protein antigens in adjuvants
    • C.-W. Yang, B. S. I. Strong, M. J. Miller, and E. R. Unanue, "Neutrophils influence the level of antigen presentation during the immune response to protein antigens in adjuvants, " Journal of Immunology, vol. 185, no. 5, pp. 2927-2934, 2010.
    • (2010) Journal of Immunology , vol.185 , Issue.5 , pp. 2927-2934
    • Yang, C.-W.1    Strong, B.S.I.2    Miller, M.J.3    Unanue, E.R.4
  • 4
    • 0002902079 scopus 로고
    • Verdoperoxidase. A ferment isolated from leukocytes
    • K. Agner, "Verdoperoxidase. A ferment isolated from leukocytes, " Acta Chemica Scandinavica, vol. 2, supplement 8, pp. 1-62, 1941.
    • (1941) Acta Chemica Scandinavica , vol.2 , pp. 1-62
    • Agner, K.1
  • 5
    • 0000807647 scopus 로고
    • Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization
    • J. Schultz and K. Kaminker, "Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization, " Archives of Biochemistry and Biophysics, vol. 96, no. 3, pp. 465-467, 1962.
    • (1962) Archives of Biochemistry and Biophysics , vol.96 , Issue.3 , pp. 465-467
    • Schultz, J.1    Kaminker, K.2
  • 6
    • 0016595791 scopus 로고
    • Granule enzymes of polymorphonuclear neutrophils: A phylogenetic comparison
    • P. G. Rausch and T. G. Moore, "Granule enzymes of polymorphonuclear neutrophils: a phylogenetic comparison, " Blood, vol. 46, no. 6, pp. 913-919, 1975.
    • (1975) Blood , vol.46 , Issue.6 , pp. 913-919
    • Rausch, P.G.1    Moore, T.G.2
  • 7
    • 0018144790 scopus 로고
    • Characterization and quantification of the peroxidase in human monocytes
    • A. Bos, R. Wever, and D. Roos, "Characterization and quantification of the peroxidase in human monocytes, " Biochimica et Biophysica Acta, vol. 525, no. 1, pp. 37-44, 1978.
    • (1978) Biochimica et Biophysica Acta , vol.525 , Issue.1 , pp. 37-44
    • Bos, A.1    Wever, R.2    Roos, D.3
  • 8
    • 73449143528 scopus 로고    scopus 로고
    • Myeloperoxidase: Molecular mechanisms of action and their relevance to human health and disease
    • B. S. van derVeen, M. P. deWinther, and P. Heeringa, "Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease, " Antioxidants & Redox Signaling, vol. 11, no. 11, pp. 2899-2937, 2009.
    • (2009) Antioxidants & Redox Signaling , vol.11 , Issue.11 , pp. 2899-2937
    • Van Derveen, B.S.1    DeWinther, M.P.2    Heeringa, P.3
  • 9
    • 0035190154 scopus 로고    scopus 로고
    • Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver
    • K. E. Brown, E. M. Brunt, and J. W. Heinecke, "Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver, " American Journal of Pathology, vol. 159, no. 6, pp. 2081-2088, 2001.
    • (2001) American Journal of Pathology , vol.159 , Issue.6 , pp. 2081-2088
    • Brown, K.E.1    Brunt, E.M.2    Heinecke, J.W.3
  • 11
    • 0030764896 scopus 로고    scopus 로고
    • Immunohistochemical and genetic evidence ofmyeloperoxidase involvement in multiple sclerosis
    • R. M. Nagra, B. Becher, W. W. Tourtellotte et al., "Immunohistochemical and genetic evidence ofmyeloperoxidase involvement in multiple sclerosis, " Journal of Neuroimmunology, vol. 78, no. 1-2, pp. 97-107, 1997.
    • (1997) Journal of Neuroimmunology , vol.78 , Issue.1-2 , pp. 97-107
    • Nagra, R.M.1    Becher, B.2    Tourtellotte, W.W.3
  • 12
    • 0001059250 scopus 로고    scopus 로고
    • Immunohistochemical evidence for the myeloperoxidase/H2O2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochloritemodified proteins
    • E. Malle, G. Waeg, R. Schreiber, E. F. Gröne, W. Sattler, and H.-J. Gröne, "Immunohistochemical evidence for the myeloperoxidase/H2O2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochloritemodified proteins, " European Journal of Biochemistry, vol. 267, no. 14, pp. 4495-4503, 2000.
    • (2000) European Journal of Biochemistry , vol.267 , Issue.14 , pp. 4495-4503
    • Malle, E.1    Waeg, G.2    Schreiber, R.3    Gröne, E.F.4    Sattler, W.5    Gröne, H.-J.6
  • 13
    • 0035205632 scopus 로고    scopus 로고
    • Mice lacking myeloperoxidase are more susceptible to experimental autoimmune encephalomyelitis
    • M.-L. Brennan, A. Gaur, A. Pahuja, A. J. Lusis, and W. F. Reynolds, "Mice lacking myeloperoxidase are more susceptible to experimental autoimmune encephalomyelitis, " Journal of Neuroimmunology, vol. 112, no. 1-2, pp. 97-105, 2001.
    • (2001) Journal of Neuroimmunology , vol.112 , Issue.1-2 , pp. 97-105
    • Brennan, M.-L.1    Gaur, A.2    Pahuja, A.3    Lusis, A.J.4    Reynolds, W.F.5
  • 14
    • 84947602409 scopus 로고    scopus 로고
    • Renal participation ofmyeloperoxidase in antineutrophil cytoplasmic antibody (ANCA)-associated glomerulonephritis
    • K. M. OSullivan, C. Y. Lo, S. A. Summers et al., "Renal participation ofmyeloperoxidase in antineutrophil cytoplasmic antibody (ANCA)-associated glomerulonephritis, " Kidney International, vol. 88, no. 5, pp. 1030-1046, 2015.
    • (2015) Kidney International , vol.88 , Issue.5 , pp. 1030-1046
    • O'Sullivan, K.M.1    Lo, C.Y.2    Summers, S.A.3
  • 15
    • 0025407762 scopus 로고
    • Clearance of neutrophilderived myeloperoxidase by the macrophage mannose receptor
    • V. L. Shepherd and J. R. Hoidal, "Clearance of neutrophilderived myeloperoxidase by the macrophage mannose receptor," American Journal of Respiratory Cell and Molecular Biology, vol. 2, no. 4, pp. 335-340, 1990.
    • (1990) American Journal of Respiratory Cell and Molecular Biology , vol.2 , Issue.4 , pp. 335-340
    • Shepherd, V.L.1    Hoidal, J.R.2
  • 16
    • 0035108136 scopus 로고    scopus 로고
    • Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes
    • S. Sugiyama, Y. Okada, G. K. Sukhova, R. Virmani, J. W. Heinecke, and P. Libby, "Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes, " The American Journal of Pathology, vol. 158, no. 3, pp. 879-891, 2001.
    • (2001) The American Journal of Pathology , vol.158 , Issue.3 , pp. 879-891
    • Sugiyama, S.1    Okada, Y.2    Sukhova, G.K.3    Virmani, R.4    Heinecke, J.W.5    Libby, P.6
  • 17
    • 30544452175 scopus 로고    scopus 로고
    • Biosynthesis, processing, and sorting of humanmyeloperoxidase
    • M. Hansson, I. Olsson, and W. M. Nauseef, "Biosynthesis, processing, and sorting of humanmyeloperoxidase, " Archives of Biochemistry and Biophysics, vol. 445, no. 2, pp. 214-224, 2006.
    • (2006) Archives of Biochemistry and Biophysics , vol.445 , Issue.2 , pp. 214-224
    • Hansson, M.1    Olsson, I.2    Nauseef, W.M.3
  • 19
    • 0032549522 scopus 로고    scopus 로고
    • Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase
    • W. M. Nauseef, S. J. McCormick, and M. Goedken, "Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase, " The Journal of Biological Chemistry, vol. 273, no. 12, pp. 7107-7111, 1998.
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 7107-7111
    • Nauseef, W.M.1    McCormick, S.J.2    Goedken, M.3
  • 20
    • 0016758657 scopus 로고
    • Purification and properties of myeloperoxidase from mice leukocytes
    • M. Shafran and S. Lyslova, "Purification and properties of myeloperoxidase from mice leukocytes, " Voprosy MeditsinskoѤ Khimii, vol. 21, pp. 629-633, 1975.
    • (1975) Voprosy MeditsinskoѤ Khimii , vol.21 , pp. 629-633
    • Shafran, M.1    Lyslova, S.2
  • 21
    • 84881047281 scopus 로고    scopus 로고
    • Neutrophil myeloperoxidase regulates T-cell-driven tissue inflammation in mice by inhibiting dendritic cell function
    • D. Odobasic, A. R. Kitching, Y. Yang et al., "Neutrophil myeloperoxidase regulates T-cell-driven tissue inflammation in mice by inhibiting dendritic cell function, " Blood, vol. 121, no. 20, pp. 4195-4204, 2013.
    • (2013) Blood , vol.121 , Issue.20 , pp. 4195-4204
    • Odobasic, D.1    Kitching, A.R.2    Yang, Y.3
  • 22
    • 0027438307 scopus 로고
    • The effects of GM-CSF on myeloperoxidase release in normal and myelodysplastic neutrophils
    • Y. Dang, G. M. Lowe, S. W. Edwards, and D. W. Galvani, "The effects of GM-CSF on myeloperoxidase release in normal and myelodysplastic neutrophils, " Leukemia Research, vol. 17, no. 12, pp. 1037-1044, 1993.
    • (1993) Leukemia Research , vol.17 , Issue.12 , pp. 1037-1044
    • Dang, Y.1    Lowe, G.M.2    Edwards, S.W.3    Galvani, D.W.4
  • 23
    • 84879833759 scopus 로고    scopus 로고
    • Toll-like receptor TLR2 and TLR9 ligation triggers neutrophil activation in granulomatosis with polyangiitis
    • J. U. Holle, M. Windmöller, C. Lange, W. L. Gross, K. Herlyn, and E. Csernok, "Toll-like receptor TLR2 and TLR9 ligation triggers neutrophil activation in granulomatosis with polyangiitis, " Rheumatology, vol. 52, no. 7, pp. 1183-1189, 2013.
    • (2013) Rheumatology , vol.52 , Issue.7 , pp. 1183-1189
    • Holle, J.U.1    Windmöller, M.2    Lange, C.3    Gross, W.L.4    Herlyn, K.5    Csernok, E.6
  • 24
    • 0027944315 scopus 로고
    • Determinants of neutrophil HOCl generation: Ligand-dependent responses and the role of surface adhesion
    • W. W. Chatham, A. Turkiewicz, and W. D. Blackburn Jr. , "Determinants of neutrophil HOCl generation: ligand-dependent responses and the role of surface adhesion, " Journal of Leukocyte Biology, vol. 56, no. 5, pp. 654-660, 1994.
    • (1994) Journal of Leukocyte Biology , vol.56 , Issue.5 , pp. 654-660
    • Chatham, W.W.1    Turkiewicz, A.2    Blackburn, W.D.3
  • 25
    • 0018850590 scopus 로고
    • The sequential release of granule constituents from human neutrophils
    • B. J. Bentwood and P. M. Henson, "The sequential release of granule constituents from human neutrophils, " Journal of Immunology, vol. 124, no. 2, pp. 855-862, 1980.
    • (1980) Journal of Immunology , vol.124 , Issue.2 , pp. 855-862
    • Bentwood, B.J.1    Henson, P.M.2
  • 26
    • 67349279881 scopus 로고    scopus 로고
    • Netting neutrophils in autoimmune small-vessel vasculitis
    • K. Kessenbrock, M. Krumbholz, U. Schönermarck et al., "Netting neutrophils in autoimmune small-vessel vasculitis, " Nature Medicine, vol. 15, no. 6, pp. 623-625, 2009.
    • (2009) Nature Medicine , vol.15 , Issue.6 , pp. 623-625
    • Kessenbrock, K.1    Krumbholz, M.2    Schönermarck, U.3
  • 27
    • 0024232736 scopus 로고
    • Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants
    • H. Fliss, "Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants, " Molecular and Cellular Biochemistry, vol. 84, no. 2, pp. 177-188, 1988.
    • (1988) Molecular and Cellular Biochemistry , vol.84 , Issue.2 , pp. 177-188
    • Fliss, H.1
  • 28
    • 0037184780 scopus 로고    scopus 로고
    • Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid
    • C. C. Winterbourn, "Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid, " Toxicology, vol. 181-182, pp. 223-227, 2002.
    • (2002) Toxicology , vol.181-182 , pp. 223-227
    • Winterbourn, C.C.1
  • 29
    • 70249098135 scopus 로고    scopus 로고
    • Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatographytandem mass spectrometry
    • D. T. Harwood, A. J. Kettle, S. Brennan, and C. C. Winterbourn, "Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatographytandem mass spectrometry, " Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, vol. 877, no. 28, pp. 3393-3399, 2009.
    • (2009) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.877 , Issue.28 , pp. 3393-3399
    • Harwood, D.T.1    Kettle, A.J.2    Brennan, S.3    Winterbourn, C.C.4
  • 30
    • 33749422853 scopus 로고    scopus 로고
    • Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method
    • D. T. Harwood, A. J. Kettle, and C. C. Winterbourn, "Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method, " Biochemical Journal, vol. 399, no. 1, pp. 161-168, 2006.
    • (2006) Biochemical Journal , vol.399 , Issue.1 , pp. 161-168
    • Harwood, D.T.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 31
    • 0025339493 scopus 로고
    • Taurine and hypotaurine content of human leukocytes
    • D. B. Learn, V. A. Fried, and E. L. Thomas, "Taurine and hypotaurine content of human leukocytes, " Journal of Leukocyte Biology, vol. 48, no. 2, pp. 174-182, 1990.
    • (1990) Journal of Leukocyte Biology , vol.48 , Issue.2 , pp. 174-182
    • Learn, D.B.1    Fried, V.A.2    Thomas, E.L.3
  • 33
    • 0033041907 scopus 로고    scopus 로고
    • Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase
    • Y. Aratani, H. Koyama, S.-I. Nyui, K. Suzuki, F. Kura, and N. Maeda, "Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase, " Infection and Immunity, vol. 67, no. 4, pp. 1828-1836, 1999.
    • (1999) Infection and Immunity , vol.67 , Issue.4 , pp. 1828-1836
    • Aratani, Y.1    Koyama, H.2    Nyui, S.-I.3    Suzuki, K.4    Kura, F.5    Maeda, N.6
  • 34
    • 0033800733 scopus 로고    scopus 로고
    • Differential host susceptibility to pulmonary infections with bacteria and fungi in mice deficient inmyeloperoxidase
    • Y. Aratani, F. Kura, H. Watanabe et al., "Differential host susceptibility to pulmonary infections with bacteria and fungi in mice deficient inmyeloperoxidase, " Journal of Infectious Diseases, vol. 182, no. 4, pp. 1276-1279, 2000.
    • (2000) Journal of Infectious Diseases , vol.182 , Issue.4 , pp. 1276-1279
    • Aratani, Y.1    Kura, F.2    Watanabe, H.3
  • 35
    • 49049100515 scopus 로고    scopus 로고
    • Augmented inducible nitric oxide synthase expression and increased NO production reduce sepsis-induced lung injury and mortality in myeloperoxidase-null mice
    • V. Brovkovych, X.-P. Gao, E. Ong et al., "Augmented inducible nitric oxide synthase expression and increased NO production reduce sepsis-induced lung injury and mortality in myeloperoxidase-null mice, " American Journal of Physiology-Lung Cellular and Molecular Physiology, vol. 295, no. 1, pp. L96-L103, 2008.
    • (2008) American Journal of Physiology-Lung Cellular and Molecular Physiology , vol.295 , Issue.1 , pp. L96-L103
    • Brovkovych, V.1    Gao, X.-P.2    Ong, E.3
  • 36
    • 77954161132 scopus 로고    scopus 로고
    • Production of extracellular traps against aspergillus fumigatus in vitro and in infected lung tissue is dependent on invading neutrophils and influenced by hydrophobin roda
    • Article ID e1000873
    • S. Bruns, O. Kniemeyer, M. Hasenberg et al., "Production of extracellular traps against aspergillus fumigatus in vitro and in infected lung tissue is dependent on invading neutrophils and influenced by hydrophobin roda, " PLoS Pathogens, vol. 6, no. 4, Article ID e1000873, 2010.
    • (2010) PLoS Pathogens , vol.6 , Issue.4
    • Bruns, S.1    Kniemeyer, O.2    Hasenberg, M.3
  • 37
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • V. Brinkmann, U. Reichard, C. Goosmann et al., "Neutrophil extracellular traps kill bacteria, " Science, vol. 303, no. 5663, pp. 1532-1535, 2004.
    • (2004) Science , vol.303 , Issue.5663 , pp. 1532-1535
    • Brinkmann, V.1    Reichard, U.2    Goosmann, C.3
  • 38
    • 78751693139 scopus 로고    scopus 로고
    • Myeloperoxidase is required for neutrophil extracellular trap formation: Implications for innate immunity
    • K. D. Metzler, T. A. Fuchs, W. M. Nauseef et al., "Myeloperoxidase is required for neutrophil extracellular trap formation: implications for innate immunity, " Blood, vol. 117, no. 3, pp. 953-959, 2011.
    • (2011) Blood , vol.117 , Issue.3 , pp. 953-959
    • Metzler, K.D.1    Fuchs, T.A.2    Nauseef, W.M.3
  • 39
    • 84857862903 scopus 로고    scopus 로고
    • Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide
    • H. Parker, A. M. Albrett, A. J. Kettle, and C. C. Winterbourn, "Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide, " Journal of Leukocyte Biology, vol. 91, no. 3, pp. 369-376, 2012.
    • (2012) Journal of Leukocyte Biology , vol.91 , Issue.3 , pp. 369-376
    • Parker, H.1    Albrett, A.M.2    Kettle, A.J.3    Winterbourn, C.C.4
  • 40
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • V. Papayannopoulos, K. D. Metzler, A. Hakkim, and A. Zychlinsky, "Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps, " Journal of Cell Biology, vol. 191, no. 3, pp. 677-691, 2010.
    • (2010) Journal of Cell Biology , vol.191 , Issue.3 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 41
    • 84868113151 scopus 로고    scopus 로고
    • Cytokines induced neutrophil extracellular traps formation: Implication for the inflammatory disease condition
    • Article ID e48111
    • R. S. Keshari, A. Jyoti, M. Dubey et al., "Cytokines induced neutrophil extracellular traps formation: implication for the inflammatory disease condition, " PLoS ONE, vol. 7, no. 10, Article ID e48111, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Keshari, R.S.1    Jyoti, A.2    Dubey, M.3
  • 42
    • 84908201445 scopus 로고    scopus 로고
    • A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis
    • K. D. Metzler, C. Goosmann, A. Lubojemska, A. Zychlinsky, and V. Papayannopoulos, "A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis, " Cell Reports, vol. 8, no. 3, pp. 883-896, 2014.
    • (2014) Cell Reports , vol.8 , Issue.3 , pp. 883-896
    • Metzler, K.D.1    Goosmann, C.2    Lubojemska, A.3    Zychlinsky, A.4    Papayannopoulos, V.5
  • 43
    • 84866177387 scopus 로고    scopus 로고
    • Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus
    • H. Parker, M. Dragunow, M. B. Hampton, A. J. Kettle, and C. C. Winterbourn, "Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus, " Journal of Leukocyte Biology, vol. 92, no. 4, pp. 841-849, 2012.
    • (2012) Journal of Leukocyte Biology , vol.92 , Issue.4 , pp. 841-849
    • Parker, H.1    Dragunow, M.2    Hampton, M.B.3    Kettle, A.J.4    Winterbourn, C.C.5
  • 44
    • 84865049455 scopus 로고    scopus 로고
    • Influences of chloride and hypochlorite on neutrophil extracellular trap formation
    • Article ID e42984
    • K. Akong-Moore, O. A. Chow, M. von Köckritz-Blickwede, and V. Nizet, "Influences of chloride and hypochlorite on neutrophil extracellular trap formation, " PLoS ONE, vol. 7, no. 8, Article ID e42984, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Akong-Moore, K.1    Chow, O.A.2    Von Köckritz-Blickwede, M.3    Nizet, V.4
  • 45
    • 84866423248 scopus 로고    scopus 로고
    • Fibrosis in atrial fibrillation-role of reactive species and MPO
    • article 214
    • K. Friedrichs, S. Baldus, and A. Klinke, "Fibrosis in atrial fibrillation-role of reactive species and MPO, " Frontiers in Physiology, vol. 3, article 214, 2012.
    • (2012) Frontiers in Physiology , vol.3
    • Friedrichs, K.1    Baldus, S.2    Klinke, A.3
  • 46
    • 0019997889 scopus 로고
    • Cellular and extracellular myeloperoxidase in pyogenic inflammation
    • P. P. Bradley, R. D. Christensen, and G. Rothstein, "Cellular and extracellular myeloperoxidase in pyogenic inflammation, " Blood, vol. 60, no. 3, pp. 618-622, 1982.
    • (1982) Blood , vol.60 , Issue.3 , pp. 618-622
    • Bradley, P.P.1    Christensen, R.D.2    Rothstein, G.3
  • 47
    • 10644263047 scopus 로고    scopus 로고
    • Myeloperoxidase and protein oxidation in the airways of young children with cystic fibrosis
    • A. J. Kettle, T. Chan, I. Osberg et al., "Myeloperoxidase and protein oxidation in the airways of young children with cystic fibrosis, " American Journal of Respiratory and Critical Care Medicine, vol. 170, no. 12, pp. 1317-1323, 2004.
    • (2004) American Journal of Respiratory and Critical Care Medicine , vol.170 , Issue.12 , pp. 1317-1323
    • Kettle, A.J.1    Chan, T.2    Osberg, I.3
  • 49
    • 84867132934 scopus 로고    scopus 로고
    • Myeloperoxidase and oxidative stress in rheumatoid arthritis
    • Article ID kes193
    • L. K. Stamp, I. Khalilova, J. M. Tarr et al., "Myeloperoxidase and oxidative stress in rheumatoid arthritis, " Rheumatology, vol. 51, no. 10, Article ID kes193, pp. 1796-1803, 2012.
    • (2012) Rheumatology , vol.51 , Issue.10 , pp. 1796-1803
    • Stamp, L.K.1    Khalilova, I.2    Tarr, J.M.3
  • 51
    • 0023162140 scopus 로고
    • Participation of the myeloperoxidase-H2O2-halide system in immune complex nephritis
    • R. J. Johnson, S. J. Klebanoff, R. F. Ochi et al., "Participation of the myeloperoxidase-H2O2-halide system in immune complex nephritis, " Kidney International, vol. 32, no. 3, pp. 342-349, 1987.
    • (1987) Kidney International , vol.32 , Issue.3 , pp. 342-349
    • Johnson, R.J.1    Klebanoff, S.J.2    Ochi, R.F.3
  • 52
    • 0032908178 scopus 로고    scopus 로고
    • Neutrophilicmyeloperoxidase-macrophage interactions perpetuate chronic inflammation associated with experimental arthritis
    • D. L. Lefkowitz, M. P. Gelderman, S. R. Fuhrmann et al., "Neutrophilicmyeloperoxidase-macrophage interactions perpetuate chronic inflammation associated with experimental arthritis, " Clinical Immunology, vol. 91, no. 2, pp. 145-155, 1999.
    • (1999) Clinical Immunology , vol.91 , Issue.2 , pp. 145-155
    • Lefkowitz, D.L.1    Gelderman, M.P.2    Fuhrmann, S.R.3
  • 53
    • 84906062814 scopus 로고    scopus 로고
    • Myeloperoxidase deficiency ameliorates progression of chronic kidney disease in mice
    • A. Lehners, S. Lange, G. Niemann et al., "Myeloperoxidase deficiency ameliorates progression of chronic kidney disease in mice, " American Journal of Physiology-Renal Physiology, vol. 307, no. 4, pp. F407-F417, 2014.
    • (2014) American Journal of Physiology-Renal Physiology , vol.307 , Issue.4 , pp. F407-F417
    • Lehners, A.1    Lange, S.2    Niemann, G.3
  • 54
    • 38349000796 scopus 로고    scopus 로고
    • Myeloperoxidase is critically involved in the induction of organ damage after renal ischemia reperfusion
    • R. A. Matthijsen, D. Huugen, N. T. Hoebers et al., "Myeloperoxidase is critically involved in the induction of organ damage after renal ischemia reperfusion, " The American Journal of Pathology, vol. 171, no. 6, pp. 1743-1752, 2007.
    • (2007) The American Journal of Pathology , vol.171 , Issue.6 , pp. 1743-1752
    • Matthijsen, R.A.1    Huugen, D.2    Hoebers, N.T.3
  • 55
    • 20344391164 scopus 로고    scopus 로고
    • Expression of human myeloperoxidase by macrophages promotes atherosclerosis in mice
    • T. S. McMillen, J. W. Heinecke, and R. C. LeBoeuf, "Expression of human myeloperoxidase by macrophages promotes atherosclerosis in mice, " Circulation, vol. 111, no. 21, pp. 2798-2804, 2005.
    • (2005) Circulation , vol.111 , Issue.21 , pp. 2798-2804
    • McMillen, T.S.1    Heinecke, J.W.2    LeBoeuf, R.C.3
  • 56
    • 33947244860 scopus 로고    scopus 로고
    • Endogenous myeloperoxidase promotes neutrophil-mediated renal injury, but attenuates T cell immunity inducing crescentic glomerulonephritis
    • D. Odobasic, A. R. Kitching, T. J. Semple, and S. R. Holdsworth, "Endogenous myeloperoxidase promotes neutrophil-mediated renal injury, but attenuates T cell immunity inducing crescentic glomerulonephritis, " Journal of the AmericanSociety of Nephrology, vol. 18, no. 3, pp. 760-770, 2007.
    • (2007) Journal of the AmericanSociety of Nephrology , vol.18 , Issue.3 , pp. 760-770
    • Odobasic, D.1    Kitching, A.R.2    Semple, T.J.3    Holdsworth, S.R.4
  • 57
    • 84898658937 scopus 로고    scopus 로고
    • Endogenousmyeloperoxidase is a mediator of joint inflammation and damage in experimental arthritis
    • D. Odobasic, Y. Yang, R. C. M. Muljadi et al., "Endogenousmyeloperoxidase is a mediator of joint inflammation and damage in experimental arthritis, " Arthritis and Rheumatology, vol. 66, no. 4, pp. 907-917, 2014.
    • (2014) Arthritis and Rheumatology , vol.66 , Issue.4 , pp. 907-917
    • Odobasic, D.1    Yang, Y.2    Muljadi, R.C.M.3
  • 58
    • 77950547453 scopus 로고    scopus 로고
    • Myeloperoxidase acts as a profibrotic mediator of atrial fibrillation
    • V. Rudolph, R. P. Andrié, T. K. Rudolph et al., "Myeloperoxidase acts as a profibrotic mediator of atrial fibrillation, " Nature Medicine, vol. 16, no. 4, pp. 470-474, 2010.
    • (2010) Nature Medicine , vol.16 , Issue.4 , pp. 470-474
    • Rudolph, V.1    Andrié, R.P.2    Rudolph, T.K.3
  • 59
    • 79960392810 scopus 로고    scopus 로고
    • Netting neutrophils induce endothelial damage, infiltrate tissues, and expose immunostimulatory molecules in systemic lupus erythematosus
    • E. Villanueva, S. Yalavarthi, C. C. Berthier et al., "Netting neutrophils induce endothelial damage, infiltrate tissues, and expose immunostimulatory molecules in systemic lupus erythematosus, " Journal of Immunology, vol. 187, no. 1, pp. 538-552, 2011.
    • (2011) Journal of Immunology , vol.187 , Issue.1 , pp. 538-552
    • Villanueva, E.1    Yalavarthi, S.2    Berthier, C.C.3
  • 60
    • 84937719061 scopus 로고    scopus 로고
    • Inflammation. Neutrophil extracellular traps license macrophages for cytokine production in atherosclerosis
    • A. Warnatsch, M. Ioannou, Q. Wang, and V. Papayannopoulos, "Inflammation. Neutrophil extracellular traps license macrophages for cytokine production in atherosclerosis, " Science, vol. 349, no. 6245, pp. 316-320, 2015.
    • (2015) Science , vol.349 , Issue.6245 , pp. 316-320
    • Warnatsch, A.1    Ioannou, M.2    Wang, Q.3    Papayannopoulos, V.4
  • 61
    • 84901637810 scopus 로고    scopus 로고
    • Humans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced highdensity lipoprotein oxidation by myeloperoxidase
    • B. Shao, C. Tang, A. Sinha et al., "Humans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced highdensity lipoprotein oxidation by myeloperoxidase, " Circulation Research, vol. 114, no. 11, pp. 1733-1742, 2014.
    • (2014) Circulation Research , vol.114 , Issue.11 , pp. 1733-1742
    • Shao, B.1    Tang, C.2    Sinha, A.3
  • 62
    • 84907410099 scopus 로고    scopus 로고
    • Neutrophil extracellular trap-derived enzymes oxidize high-density lipoprotein: An additional proatherogenic mechanism in systemic lupus erythematosus
    • C. K. Smith, A. Vivekanandan-Giri, C. Tang et al., "Neutrophil extracellular trap-derived enzymes oxidize high-density lipoprotein: an additional proatherogenic mechanism in systemic lupus erythematosus, " Arthritis and Rheumatology, vol. 66, no. 9, pp. 2532-2544, 2014.
    • (2014) Arthritis and Rheumatology , vol.66 , Issue.9 , pp. 2532-2544
    • Smith, C.K.1    Vivekanandan-Giri, A.2    Tang, C.3
  • 63
    • 84876104421 scopus 로고    scopus 로고
    • NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis
    • Article ID 178ra40
    • R. Khandpur, C. Carmona-Rivera, A. Vivekanandan-Giri et al., "NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis, " Science Translational Medicine, vol. 5, no. 178, Article ID 178ra40, 2013.
    • (2013) Science Translational Medicine , vol.5 , Issue.178
    • Khandpur, R.1    Carmona-Rivera, C.2    Vivekanandan-Giri, A.3
  • 64
    • 84922322204 scopus 로고    scopus 로고
    • Emerging concepts in the pathogenesis of antineutrophil cytoplasmic antibody-associated vasculitis
    • S. M. Flint, E. F. McKinney, and K. G. C. Smith, "Emerging concepts in the pathogenesis of antineutrophil cytoplasmic antibody-associated vasculitis, " Current Opinion in Rheumatology, vol. 27, no. 2, pp. 197-203, 2015.
    • (2015) Current Opinion in Rheumatology , vol.27 , Issue.2 , pp. 197-203
    • Flint, S.M.1    McKinney, E.F.2    Smith, K.G.C.3
  • 66
    • 84864772500 scopus 로고    scopus 로고
    • Animal models of anti-neutrophil cytoplasmic antibody-associated vasculitis
    • A. M. Coughlan, S. J. Freeley, and M. G. Robson, "Animal models of anti-neutrophil cytoplasmic antibody-associated vasculitis, " Clinical and Experimental Immunology, vol. 169, no. 3, pp. 229-237, 2012.
    • (2012) Clinical and Experimental Immunology , vol.169 , Issue.3 , pp. 229-237
    • Coughlan, A.M.1    Freeley, S.J.2    Robson, M.G.3
  • 67
    • 84877323023 scopus 로고    scopus 로고
    • Myeloperoxidase (MPO)-specific CD4+ T cells contribute to MPO-anti-neutrophil cytoplasmic antibody (ANCA) associated glomerulonephritis
    • P.-Y. Gan, S. R. Holdsworth, A. R. Kitching, and J. D. Ooi, "Myeloperoxidase (MPO)-specific CD4+ T cells contribute to MPO-anti-neutrophil cytoplasmic antibody (ANCA) associated glomerulonephritis, " Cellular Immunology, vol. 282, no. 1, pp. 21-27, 2013.
    • (2013) Cellular Immunology , vol.282 , Issue.1 , pp. 21-27
    • Gan, P.-Y.1    Holdsworth, S.R.2    Kitching, A.R.3    Ooi, J.D.4
  • 68
    • 84864748957 scopus 로고    scopus 로고
    • How anti-neutrophil cytoplasmic autoantibodies activate neutrophils
    • R. Kettritz, "How anti-neutrophil cytoplasmic autoantibodies activate neutrophils, " Clinical and Experimental Immunology, vol. 169, no. 3, pp. 220-228, 2012.
    • (2012) Clinical and Experimental Immunology , vol.169 , Issue.3 , pp. 220-228
    • Kettritz, R.1
  • 69
    • 33745844851 scopus 로고    scopus 로고
    • Anti-neutrophil cytoplasmic antibodies and effector CD4+ cells play nonredundant roles in anti-myeloperoxidase crescentic glomerulonephritis
    • A.-J. Ruth, A. R. Kitching, R. Y. Q. Kwan et al., "Anti-neutrophil cytoplasmic antibodies and effector CD4+ cells play nonredundant roles in anti-myeloperoxidase crescentic glomerulonephritis, " Journal of the American Society of Nephrology, vol. 17, no. 7, pp. 1940-1949, 2006.
    • (2006) Journal of the American Society of Nephrology , vol.17 , Issue.7 , pp. 1940-1949
    • Ruth, A.-J.1    Kitching, A.R.2    Kwan, R.Y.Q.3
  • 70
    • 0036790387 scopus 로고    scopus 로고
    • Antineutrophil cytoplasmic autoantibodies specific for myeloperoxidase cause glomerulonephritis and vasculitis in mice
    • H. Xiao, P. Heeringa, P. Hu et al., "Antineutrophil cytoplasmic autoantibodies specific for myeloperoxidase cause glomerulonephritis and vasculitis in mice, " Journal of Clinical Investigation, vol. 110, no. 7, pp. 955-963, 2002.
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.7 , pp. 955-963
    • Xiao, H.1    Heeringa, P.2    Hu, P.3
  • 71
    • 0035046590 scopus 로고    scopus 로고
    • IgG from myeloperoxidase-antineutrophil cytoplasmic antibody-positive patients stimulates greater activation of primed neutrophils than IgG from proteinase 3-antineutrophil cytosplasmic antibody-positive patients
    • L. Harper, D. Radford, T. Plant, M. Drayson, D. Adu, and C. O. S. Savage, "IgG from myeloperoxidase-antineutrophil cytoplasmic antibody-positive patients stimulates greater activation of primed neutrophils than IgG from proteinase 3-antineutrophil cytosplasmic antibody-positive patients, " Arthritis & Rheumatism, vol. 44, no. 4, pp. 921-930, 2001.
    • (2001) Arthritis & Rheumatism , vol.44 , Issue.4 , pp. 921-930
    • Harper, L.1    Radford, D.2    Plant, T.3    Drayson, M.4    Adu, D.5    Savage, C.O.S.6
  • 72
    • 84866880246 scopus 로고    scopus 로고
    • The immunodominant myeloperoxidase T-cell epitope induces local cell-mediated injury in antimyeloperoxidase glomerulonephritis
    • J. D. Ooi, J. Chang, M. J. Hickey et al., "The immunodominant myeloperoxidase T-cell epitope induces local cell-mediated injury in antimyeloperoxidase glomerulonephritis, " Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 39, pp. E2615-E2624, 2012.
    • (2012) Proceedings of the National Academy of Sciences of the United States of America , vol.109 , Issue.39 , pp. E2615-E2624
    • Ooi, J.D.1    Chang, J.2    Hickey, M.J.3
  • 73
    • 84867836102 scopus 로고    scopus 로고
    • Neutrophil extracellular traps mediate transfer of cytoplasmic neutrophil antigens tomyeloid dendritic cells toward ANCA induction and associated autoimmunity
    • S. Sangaletti, C. Tripodo, C. Chiodoni et al., "Neutrophil extracellular traps mediate transfer of cytoplasmic neutrophil antigens tomyeloid dendritic cells toward ANCA induction and associated autoimmunity, " Blood, vol. 120, no. 15, pp. 3007-3018, 2012.
    • (2012) Blood , vol.120 , Issue.15 , pp. 3007-3018
    • Sangaletti, S.1    Tripodo, C.2    Chiodoni, C.3
  • 74
    • 84875827100 scopus 로고    scopus 로고
    • Epitope specificity determines pathogenicity and detectability in anca-associated vasculitis
    • A. J. Roth, J. D. Ooi, J. J. Hess et al., "Epitope specificity determines pathogenicity and detectability in anca-associated vasculitis, " Journal of Clinical Investigation, vol. 123, no. 4, pp. 1773-1783, 2013.
    • (2013) Journal of Clinical Investigation , vol.123 , Issue.4 , pp. 1773-1783
    • Roth, A.J.1    Ooi, J.D.2    Hess, J.J.3
  • 75
    • 67650578429 scopus 로고    scopus 로고
    • Antimyeloperoxidase antibodies rapidly induce α4-integrin-dependent glomerular neutrophil adhesion
    • M. P. Kuligowski, R. Y. Q. Kwan, C. Lo et al., "Antimyeloperoxidase antibodies rapidly induce α4-integrin-dependent glomerular neutrophil adhesion, " Blood, vol. 113, no. 25, pp. 6485-6494, 2009.
    • (2009) Blood , vol.113 , Issue.25 , pp. 6485-6494
    • Kuligowski, M.P.1    Kwan, R.Y.Q.2    Lo, C.3
  • 76
    • 0036790387 scopus 로고    scopus 로고
    • Antineutrophil cytoplasmic autoantibodies specific for myeloperoxidase cause glomerulonephritis and vasculitis in mice
    • H. Xiao, P. Heeringa, P. Hu et al., "Antineutrophil cytoplasmic autoantibodies specific for myeloperoxidase cause glomerulonephritis and vasculitis in mice, " Journal of Clinical Investigation, vol. 110, no. 7, pp. 955-963, 2002.
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.7 , pp. 955-963
    • Xiao, H.1    Heeringa, P.2    Hu, P.3
  • 77
    • 84878702257 scopus 로고    scopus 로고
    • Podocytes are nonhematopoietic professional antigen-presenting cells
    • A. Goldwich, M. Burkard, M. Ölke et al., "Podocytes are nonhematopoietic professional antigen-presenting cells, " Journal of the American Society of Nephrology, vol. 24, no. 6, pp. 906-916, 2013.
    • (2013) Journal of the American Society of Nephrology , vol.24 , Issue.6 , pp. 906-916
    • Goldwich, A.1    Burkard, M.2    Ölke, M.3
  • 78
    • 0035187247 scopus 로고    scopus 로고
    • Polymorphonuclear neutrophils inWegeners granulomatosis acquire characteristics of antigen presenting cells
    • C. Iking-Konert, S. Vogt, M. Radsak, C. Wagner, G. M. Hänsch, and K. Andrassy, "Polymorphonuclear neutrophils inWegeners granulomatosis acquire characteristics of antigen presenting cells, " Kidney International, vol. 60, no. 6, pp. 2247-2262, 2001.
    • (2001) Kidney International , vol.60 , Issue.6 , pp. 2247-2262
    • Iking-Konert, C.1    Vogt, S.2    Radsak, M.3    Wagner, C.4    Hänsch, G.M.5    Andrassy, K.6
  • 79
    • 0033082475 scopus 로고    scopus 로고
    • Endotoxin downregulates T cell activation by antigen-presenting liver sinusoidal endothelial cells
    • P. A. Knolle, T. Germann, U. Treichel et al., "Endotoxin downregulates T cell activation by antigen-presenting liver sinusoidal endothelial cells, " Journal of Immunology, vol. 162, no. 3, pp. 1401-1407, 1999.
    • (1999) Journal of Immunology , vol.162 , Issue.3 , pp. 1401-1407
    • Knolle, P.A.1    Germann, T.2    Treichel, U.3
  • 80
    • 84856566896 scopus 로고    scopus 로고
    • Acquisition of antigen-presenting functions by neutrophils isolated frommice with chronic colitis
    • D. V. Ostanin, E. Kurmaeva, K. Furr et al., "Acquisition of antigen-presenting functions by neutrophils isolated frommice with chronic colitis, " Journal of Immunology, vol. 188, no. 3, pp. 1491-1502, 2012.
    • (2012) Journal of Immunology , vol.188 , Issue.3 , pp. 1491-1502
    • Ostanin, D.V.1    Kurmaeva, E.2    Furr, K.3
  • 81
    • 80054798514 scopus 로고    scopus 로고
    • 2-Thioxanthines are mechanism-based inactivators of myeloperoxidase that block oxidative stress during inflammation
    • A.-K. Tide, T. Sjögren, M. Svensson et al., "2-Thioxanthines are mechanism-based inactivators of myeloperoxidase that block oxidative stress during inflammation, " The Journal of Biological Chemistry, vol. 286, no. 43, pp. 37578-37589, 2011.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.43 , pp. 37578-37589
    • Tide, A.-K.1    Sjögren, T.2    Svensson, M.3
  • 82
    • 84929941913 scopus 로고    scopus 로고
    • PF-1355, A mechanismbased myeloperoxidase inhibitor, prevents immune complex vasculitis and anti-glomerular basement membrane glomerulonephritis
    • W. Zheng, R. Warner, R. Ruggeri et al., "PF-1355, A mechanismbased myeloperoxidase inhibitor, prevents immune complex vasculitis and anti-glomerular basement membrane glomerulonephritis, " Journal of Pharmacology and Experimental Therapeutics, vol. 353, no. 2, pp. 288-298, 2015.
    • (2015) Journal of Pharmacology and Experimental Therapeutics , vol.353 , Issue.2 , pp. 288-298
    • Zheng, W.1    Warner, R.2    Ruggeri, R.3
  • 83
    • 84870887288 scopus 로고    scopus 로고
    • Effects of a novel pharmacologic inhibitor of myeloperoxidase in a mouse atherosclerosis model
    • Article IDe50767
    • C. Liu, R. Desikan, Z. Ying et al., "Effects of a novel pharmacologic inhibitor of myeloperoxidase in a mouse atherosclerosis model, " PLoS ONE, vol. 7, no. 12, Article IDe50767, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.12
    • Liu, C.1    Desikan, R.2    Ying, Z.3
  • 85
    • 50949130053 scopus 로고    scopus 로고
    • Myeloperoxidase delays neutrophil apoptosis through CD11b/CD18 integrins and prolongs inflammation
    • D. El Kebir, L. József, W. Pan, and J. G. Filep, "Myeloperoxidase delays neutrophil apoptosis through CD11b/CD18 integrins and prolongs inflammation, " Circulation Research, vol. 103, no. 4, pp. 352-359, 2008.
    • (2008) Circulation Research , vol.103 , Issue.4 , pp. 352-359
    • El Kebir, D.1    József, L.2    Pan, W.3    Filep, J.G.4
  • 86
    • 0030920656 scopus 로고    scopus 로고
    • Myeloperoxidase mediates cell adhesion via the alpha Mbeta 2 integrin (Mac-1, CD11b/CD18)
    • M. W. Johansson, M. Patarroyo, F. Oberg, A. Siegbahn, and K. Nilsson, "Myeloperoxidase mediates cell adhesion via the alpha Mbeta 2 integrin (Mac-1, CD11b/CD18), " Journal of Cell Science, vol. 110, part 9, pp. 1133-1139, 1997.
    • (1997) Journal of Cell Science , vol.110 , pp. 1133-1139
    • Johansson, M.W.1    Patarroyo, M.2    Oberg, F.3    Siegbahn, A.4    Nilsson, K.5
  • 87
    • 0036014833 scopus 로고    scopus 로고
    • Alveolar macrophage activation by myeloperoxidase: A model for exacerbation of lung inflammation
    • K. Grattendick, R. Stuart, E. Roberts et al., "Alveolar macrophage activation by myeloperoxidase: a model for exacerbation of lung inflammation, " American Journal of Respiratory Cell and Molecular Biology, vol. 26, no. 6, pp. 716-722, 2002.
    • (2002) American Journal of Respiratory Cell and Molecular Biology , vol.26 , Issue.6 , pp. 716-722
    • Grattendick, K.1    Stuart, R.2    Roberts, E.3
  • 88
    • 0034713175 scopus 로고    scopus 로고
    • The endothelium and cytokine secretion: The role of peroxidases as immunoregulators
    • D. L. Lefkowitz, E. Roberts, K. Grattendick et al., "The endothelium and cytokine secretion: the role of peroxidases as immunoregulators, " Cellular Immunology, vol. 202, no. 1, pp. 23-30, 2000.
    • (2000) Cellular Immunology , vol.202 , Issue.1 , pp. 23-30
    • Lefkowitz, D.L.1    Roberts, E.2    Grattendick, K.3
  • 89
    • 0345690207 scopus 로고    scopus 로고
    • Crosstalk in the innate immune system: Neutrophils instruct recruitment and activation of dendritic cells during microbial infection
    • S. Bennouna, S. K. Bliss, T. J. Curiel, and E. Y. Denkers, "Crosstalk in the innate immune system: neutrophils instruct recruitment and activation of dendritic cells during microbial infection, " The Journal of Immunology, vol. 171, no. 11, pp. 6052-6058, 2003.
    • (2003) The Journal of Immunology , vol.171 , Issue.11 , pp. 6052-6058
    • Bennouna, S.1    Bliss, S.K.2    Curiel, T.J.3    Denkers, E.Y.4
  • 90
    • 17044418149 scopus 로고    scopus 로고
    • Microbial antigen triggers rapid mobilization of TNF-alpha to the surface of mouse neutrophils transforming them into inducers of high-level dendritic cell TNF-alpha production
    • S. Bennouna and E. Y. Denkers, "Microbial antigen triggers rapid mobilization of TNF-alpha to the surface of mouse neutrophils transforming them into inducers of high-level dendritic cell TNF-alpha production, " The Journal of Immunology, vol. 174, no. 8, pp. 4845-4851, 2005.
    • (2005) The Journal of Immunology , vol.174 , Issue.8 , pp. 4845-4851
    • Bennouna, S.1    Denkers, E.Y.2
  • 91
    • 84921418943 scopus 로고    scopus 로고
    • Neutrophils are required for both the sensitization and elicitation phase of contact hypersensitivity
    • F. C. Weber, T. Németh, J. Z. Csepregi et al., "Neutrophils are required for both the sensitization and elicitation phase of contact hypersensitivity, " Journal of Experimental Medicine, vol. 212, no. 1, pp. 15-22, 2015.
    • (2015) Journal of Experimental Medicine , vol.212 , Issue.1 , pp. 15-22
    • Weber, F.C.1    Németh, T.2    Csepregi, J.Z.3
  • 92
    • 84929590599 scopus 로고    scopus 로고
    • Microbe-dependent lymphatic migration of neutrophils modulates lymphocyte proliferation in lymph nodes
    • article 7139
    • H. R. Hampton, J. Bailey, M. Tomura, R. Brink, and T. Chtanova, "Microbe-dependent lymphatic migration of neutrophils modulates lymphocyte proliferation in lymph nodes, " Nature Communications, vol. 6, article 7139, 2015.
    • (2015) Nature Communications , vol.6
    • Hampton, H.R.1    Bailey, J.2    Tomura, M.3    Brink, R.4    Chtanova, T.5
  • 93
    • 79251559088 scopus 로고    scopus 로고
    • CCR7 is involved in the migration of neutrophils to lymph nodes
    • C. Beauvillain, P. Cunin, A. Doni et al., "CCR7 is involved in the migration of neutrophils to lymph nodes, " Blood, vol. 117, no. 4, pp. 1196-1204, 2011.
    • (2011) Blood , vol.117 , Issue.4 , pp. 1196-1204
    • Beauvillain, C.1    Cunin, P.2    Doni, A.3
  • 94
    • 84905987693 scopus 로고    scopus 로고
    • Neutrophils exhibit differential requirements for homing molecules in their lymphatic and blood trafficking into draining lymph nodes
    • C. V. Gorlino, R. P. Ranocchia, M. F. Harman et al., "Neutrophils exhibit differential requirements for homing molecules in their lymphatic and blood trafficking into draining lymph nodes, "The Journal of Immunology, vol. 193, no. 4, pp. 1966-1974, 2014.
    • (2014) The Journal of Immunology , vol.193 , Issue.4 , pp. 1966-1974
    • Gorlino, C.V.1    Ranocchia, R.P.2    Harman, M.F.3
  • 95
    • 84855444617 scopus 로고    scopus 로고
    • A subset of neutrophils in human systemic inflammation inhibits T cell responses through Mac-1
    • J. Pillay, V. M. Kamp, E. Van Hoffen et al., "A subset of neutrophils in human systemic inflammation inhibits T cell responses through Mac-1, " Journal of Clinical Investigation, vol. 122, no. 1, pp. 327-336, 2012.
    • (2012) Journal of Clinical Investigation , vol.122 , Issue.1 , pp. 327-336
    • Pillay, J.1    Kamp, V.M.2    Van Hoffen, E.3
  • 96
    • 84933074147 scopus 로고    scopus 로고
    • Suppression of autoimmunity and renal disease in pristane-induced lupus by myeloperoxidase
    • D. Odobasic, R. C. Muljadi, K. M. OSullivan et al., "Suppression of autoimmunity and renal disease in pristane-induced lupus by myeloperoxidase, " Arthritis & Rheumatology, vol. 67, no. 7, pp. 1868-1880, 2015.
    • (2015) Arthritis & Rheumatology , vol.67 , Issue.7 , pp. 1868-1880
    • Odobasic, D.1    Muljadi, R.C.2    O'Sullivan, K.M.3
  • 97
    • 23944508045 scopus 로고    scopus 로고
    • Neutrophils rapidly migrate via lymphatics after Mycobacterium bovis BCG intradermal vaccination and shuttle live bacilli to the draining lymph nodes
    • V. Abadie, E. Badell, P. Douillard et al., "Neutrophils rapidly migrate via lymphatics after Mycobacterium bovis BCG intradermal vaccination and shuttle live bacilli to the draining lymph nodes, " Blood, vol. 106, no. 5, pp. 1843-1850, 2005.
    • (2005) Blood , vol.106 , Issue.5 , pp. 1843-1850
    • Abadie, V.1    Badell, E.2    Douillard, P.3
  • 98
    • 0032743727 scopus 로고    scopus 로고
    • Regulation of murine dendritic cell functions in vitro by taurine chloramine, amajor product of the neutrophil myeloperoxidase-halide system
    • J. Marcinkiewicz, B. Nowak, A. Grabowska, M. Bobek, L. Petrovska, and B. Chain, "Regulation of murine dendritic cell functions in vitro by taurine chloramine, amajor product of the neutrophil myeloperoxidase-halide system, " Immunology, vol. 98, no. 3, pp. 371-378, 1999.
    • (1999) Immunology , vol.98 , Issue.3 , pp. 371-378
    • Marcinkiewicz, J.1    Nowak, B.2    Grabowska, A.3    Bobek, M.4    Petrovska, L.5    Chain, B.6
  • 99
    • 70449679220 scopus 로고    scopus 로고
    • The role of hypothiocyanous acid (HOSCN) in biological systems
    • C. L. Hawkins, "The role of hypothiocyanous acid (HOSCN) in biological systems, " Free Radical Research, vol. 43, no. 12, pp. 1147-1158, 2009.
    • (2009) Free Radical Research , vol.43 , Issue.12 , pp. 1147-1158
    • Hawkins, C.L.1
  • 100
    • 1642304742 scopus 로고    scopus 로고
    • Inhibition of interleukin-12 p40 transcription and NF-κB activation by nitric oxide in murine macrophages and dendritic cells
    • H. Xiong, C. Zhu, F. Li et al., "Inhibition of interleukin-12 p40 transcription and NF-κB activation by nitric oxide in murine macrophages and dendritic cells, " Journal of Biological Chemistry, vol. 279, no. 11, pp. 10776-10783, 2004.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 10776-10783
    • Xiong, H.1    Zhu, C.2    Li, F.3
  • 101
    • 34248174388 scopus 로고    scopus 로고
    • Complement receptor 3 ligation of dendritic cells suppresses their stimulatory capacity
    • E. M. Behrens, U. Sriram, D. K. Shivers et al., "Complement receptor 3 ligation of dendritic cells suppresses their stimulatory capacity, "The Journal of Immunology, vol. 178, no. 10, pp. 6268-6279, 2007.
    • (2007) The Journal of Immunology , vol.178 , Issue.10 , pp. 6268-6279
    • Behrens, E.M.1    Sriram, U.2    Shivers, D.K.3
  • 102
    • 0032589682 scopus 로고    scopus 로고
    • Redox regulation of β2-integrin CD11b/CD18 activation
    • E. Blouin, L. Halbwachs-Mecarelli, and P. Rieu, "Redox regulation of β2-integrin CD11b/CD18 activation, " European Journal of Immunology, vol. 29, no. 11, pp. 3419-3431, 1999.
    • (1999) European Journal of Immunology , vol.29 , Issue.11 , pp. 3419-3431
    • Blouin, E.1    Halbwachs-Mecarelli, L.2    Rieu, P.3
  • 103
    • 84055182927 scopus 로고    scopus 로고
    • Mechanisms of tissue injury in lupus nephritis
    • article 250
    • T. K. Nowling and G. S. Gilkeson, "Mechanisms of tissue injury in lupus nephritis, " Arthritis Research and Therapy, vol. 13, no. 6, article 250, 2011.
    • (2011) Arthritis Research and Therapy , vol.13 , Issue.6
    • Nowling, T.K.1    Gilkeson, G.S.2
  • 104
    • 68949183471 scopus 로고    scopus 로고
    • Induction of autoimmunity by pristane and other naturally occurring hydrocarbons
    • W. H. Reeves, P. Y. Lee, J. S. Weinstein, M. Satoh, and L. Lu, "Induction of autoimmunity by pristane and other naturally occurring hydrocarbons, " Trends in Immunology, vol. 30, no. 9, pp. 455-464, 2009.
    • (2009) Trends in Immunology , vol.30 , Issue.9 , pp. 455-464
    • Reeves, W.H.1    Lee, P.Y.2    Weinstein, J.S.3    Satoh, M.4    Lu, L.5
  • 105
    • 35148852109 scopus 로고    scopus 로고
    • Association of the G-463A myeloperoxidase gene polymorphism with renal disease in African Americans with systemic lupus erythematosus
    • H. Bouali, P. Nietert, T. M. Nowling et al., "Association of the G-463A myeloperoxidase gene polymorphism with renal disease in African Americans with systemic lupus erythematosus, " Journal of Rheumatology, vol. 34, no. 10, pp. 2028-2034, 2007.
    • (2007) Journal of Rheumatology , vol.34 , Issue.10 , pp. 2028-2034
    • Bouali, H.1    Nietert, P.2    Nowling, T.M.3
  • 106
    • 1542329511 scopus 로고    scopus 로고
    • Anti-CD4 monoclonal antibody treatment in acute and early chronic antigen-induced arthritis: Influence on T helper cell activation
    • D. Pohlers, K. Nissler, O. Frey et al., "Anti-CD4 monoclonal antibody treatment in acute and early chronic antigen-induced arthritis: influence on T helper cell activation, " Clinical and Experimental Immunology, vol. 135, no. 3, pp. 409-415, 2004.
    • (2004) Clinical and Experimental Immunology , vol.135 , Issue.3 , pp. 409-415
    • Pohlers, D.1    Nissler, K.2    Frey, O.3
  • 107
  • 108
    • 33646873774 scopus 로고    scopus 로고
    • Leukocyte recruitment to the inflamed glomerulus: A critical role for platelet-derived P-selectin in the absence of rolling
    • M. P. Kuligowski, A. R. Kitching, and M. J. Hickey, "Leukocyte recruitment to the inflamed glomerulus: a critical role for platelet-derived P-selectin in the absence of rolling, " Journal of Immunology, vol. 176, no. 11, pp. 6991-6999, 2006.
    • (2006) Journal of Immunology , vol.176 , Issue.11 , pp. 6991-6999
    • Kuligowski, M.P.1    Kitching, A.R.2    Hickey, M.J.3
  • 109
    • 0028322355 scopus 로고
    • Evidence for delayed-type hypersensitivity mechanisms in glomerular crescent formation
    • X. R. Huang, S. R. Holdsworth, and P. G. Tipping, "Evidence for delayed-type hypersensitivity mechanisms in glomerular crescent formation, " Kidney International, vol. 46, no. 1, pp. 69-78, 1994.
    • (1994) Kidney International , vol.46 , Issue.1 , pp. 69-78
    • Huang, X.R.1    Holdsworth, S.R.2    Tipping, P.G.3
  • 110
    • 2642707490 scopus 로고    scopus 로고
    • Crescentic glomerulonephritis in CD4-and CD8-deficient mice: Requirement for CD4 but not CD8 cells
    • P. G. Tipping, X. R. Huang, M. Qi, G. Y. Van, and W. W. Tang, "Crescentic glomerulonephritis in CD4-and CD8-deficient mice: requirement for CD4 but not CD8 cells, " The American Journal of Pathology, vol. 152, no. 6, pp. 1541-1548, 1998.
    • (1998) The American Journal of Pathology , vol.152 , Issue.6 , pp. 1541-1548
    • Tipping, P.G.1    Huang, X.R.2    Qi, M.3    Van, G.Y.4    Tang, W.W.5
  • 111
    • 58149398613 scopus 로고    scopus 로고
    • A key role for G-CSF-induced neutrophil production and trafficking during inflammatory arthritis
    • J. L. Eyles, M. J. Hickey, M. U. Norman et al., "A key role for G-CSF-induced neutrophil production and trafficking during inflammatory arthritis, " Blood, vol. 112, no. 13, pp. 5193-5201, 2008.
    • (2008) Blood , vol.112 , Issue.13 , pp. 5193-5201
    • Eyles, J.L.1    Hickey, M.J.2    Norman, M.U.3
  • 112
    • 0031573090 scopus 로고    scopus 로고
    • Treatment of a newly established transgenic model of chronic arthritis with nondepleting anti-CD4 monoclonal antibody
    • C. Mauri, C.-Q. Q. Chu, D. Woodrow, L. Mori, and M. Londei, "Treatment of a newly established transgenic model of chronic arthritis with nondepleting anti-CD4 monoclonal antibody, " The Journal of Immunology, vol. 159, no. 10, pp. 5032-5041, 1997.
    • (1997) The Journal of Immunology , vol.159 , Issue.10 , pp. 5032-5041
    • Mauri, C.1    Chu, C.-Q.Q.2    Woodrow, D.3    Mori, L.4    Londei, M.5
  • 113
    • 0031899715 scopus 로고    scopus 로고
    • B celldeficient mice do not develop type II collagen-induced arthritis (CIA)
    • L. Svensson, J. Jirholt, R. Holmdahl, and L. Jansson, "B celldeficient mice do not develop type II collagen-induced arthritis (CIA), " Clinical and Experimental Immunology, vol. 111, no. 3, pp. 521-526, 1998.
    • (1998) Clinical and Experimental Immunology , vol.111 , Issue.3 , pp. 521-526
    • Svensson, L.1    Jirholt, J.2    Holmdahl, R.3    Jansson, L.4
  • 114
    • 0035423403 scopus 로고    scopus 로고
    • Essential role of neutrophils in the initiation and progression of amurine model of rheumatoid arthritis
    • B. T. Wipke and P. M. Allen, "Essential role of neutrophils in the initiation and progression of amurine model of rheumatoid arthritis, " The Journal of Immunology, vol. 167, no. 3, pp. 1601-1608, 2001.
    • (2001) The Journal of Immunology , vol.167 , Issue.3 , pp. 1601-1608
    • Wipke, B.T.1    Allen, P.M.2
  • 115
    • 0020004716 scopus 로고
    • Incidence of myeloperoxidase deficiency in an area of northern Italy: Histochemical, biochemical and functional studies
    • R. Cramer, M. R. Soranzo, and P. Dri, "Incidence of myeloperoxidase deficiency in an area of northern Italy: histochemical, biochemical and functional studies, " British Journal of Haematology, vol. 51, no. 1, pp. 81-87, 1982.
    • (1982) British Journal of Haematology , vol.51 , Issue.1 , pp. 81-87
    • Cramer, R.1    Soranzo, M.R.2    Dri, P.3
  • 119
    • 0014559249 scopus 로고
    • Leukocyte myeloperoxidase deficiency and disseminated candidiasis: The role of myeloperoxidase in resistance to Candida infection
    • R. I. Lehrer and M. J. Cline, "Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infection, " Journal of Clinical Investigation, vol. 48, no. 8, pp. 1478-1488, 1969.
    • (1969) Journal of Clinical Investigation , vol.48 , Issue.8 , pp. 1478-1488
    • Lehrer, R.I.1    Cline, M.J.2
  • 120
    • 0031056469 scopus 로고    scopus 로고
    • Myeloperoxidase deficiency manifesting as pustular candidal dermatitis
    • C. Nguyen and H. P. Katner, "Myeloperoxidase deficiency manifesting as pustular candidal dermatitis, " Clinical Infectious Diseases, vol. 24, no. 2, pp. 258-260, 1997.
    • (1997) Clinical Infectious Diseases , vol.24 , Issue.2 , pp. 258-260
    • Nguyen, C.1    Katner, H.P.2
  • 121
    • 0031681380 scopus 로고    scopus 로고
    • Prevalence of myeloperoxidase deficiency: Population studies using Bayer-Technicon automated hematology
    • D. Kutter, "Prevalence of myeloperoxidase deficiency: population studies using Bayer-Technicon automated hematology, " Journal of Molecular Medicine, vol. 76, no. 10, pp. 669-675, 1998.
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.10 , pp. 669-675
    • Kutter, D.1
  • 122
    • 12444329704 scopus 로고    scopus 로고
    • Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: Effects on host defense
    • T. O. Hirche, J. P. Gaut, J. W. Heinecke, and A. Belaaouaj, "Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: effects on host defense, " The Journal of Immunology, vol. 174, no. 3, pp. 1557-1565, 2005.
    • (2005) The Journal of Immunology , vol.174 , Issue.3 , pp. 1557-1565
    • Hirche, T.O.1    Gaut, J.P.2    Heinecke, J.W.3    Belaaouaj, A.4
  • 123
    • 38849143983 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3 and cathepsin G: Physicochemical properties, activity and physiopathological functions
    • B. Korkmaz, T. Moreau, and F. Gauthier, "Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions, " Biochimie, vol. 90, no. 2, pp. 227-242, 2008.
    • (2008) Biochimie , vol.90 , Issue.2 , pp. 227-242
    • Korkmaz, B.1    Moreau, T.2    Gauthier, F.3
  • 124
    • 23844495082 scopus 로고    scopus 로고
    • Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: An oxidative mechanism for regulation of serine proteinases by myeloperoxidase
    • B. Shao, A. Belaaouaj, C. L. M. J. Verlinde, X. Fu, and J. W. Heinecke, "Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase, " Journal of Biological Chemistry, vol. 280, no. 32, pp. 29311-29321, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.32 , pp. 29311-29321
    • Shao, B.1    Belaaouaj, A.2    Verlinde, C.L.M.J.3    Fu, X.4    Heinecke, J.W.5
  • 125
    • 0021965175 scopus 로고
    • Increased degranulation of human myeloperoxidase-deficient polymorphonuclear leucocytes
    • P. Dri, R. Cramer, R. Menegazzi, and P. Patriarca, "Increased degranulation of human myeloperoxidase-deficient polymorphonuclear leucocytes, " British Journal of Haematology, vol. 59, no. 1, pp. 115-125, 1985.
    • (1985) British Journal of Haematology , vol.59 , Issue.1 , pp. 115-125
    • Dri, P.1    Cramer, R.2    Menegazzi, R.3    Patriarca, P.4
  • 126
    • 0021329788 scopus 로고
    • Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient
    • O. Stendahl, B. I. Coble, C. Dahlgren, J. Hed, and L. Molin, "Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient, " The Journal of Clinical Investigation, vol. 73, no. 2, pp. 366-373, 1984.
    • (1984) The Journal of Clinical Investigation , vol.73 , Issue.2 , pp. 366-373
    • Stendahl, O.1    Coble, B.I.2    Dahlgren, C.3    Hed, J.4    Molin, L.5
  • 128
    • 0033549921 scopus 로고    scopus 로고
    • Changes in superoxide dismutase activities and concentrations and myeloperoxidase activities in leukocytes from patients with diabetes mellitus
    • K. Uchimura, A. Nagasaka, R. Hayashi et al., "Changes in superoxide dismutase activities and concentrations and myeloperoxidase activities in leukocytes from patients with diabetes mellitus, " Journal of Diabetes and its Complications, vol. 13, no. 5-6, pp. 264-270, 1999.
    • (1999) Journal of Diabetes and Its Complications , vol.13 , Issue.5-6 , pp. 264-270
    • Uchimura, K.1    Nagasaka, A.2    Hayashi, R.3


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