메뉴 건너뛰기




Volumn 163, Issue 12, 1999, Pages 6732-6740

NADPH oxidase activation and assembly during phagocytosis

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE (CYTOCHROME); REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 0032741371     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (246)

References (63)
  • 1
    • 0025998962 scopus 로고
    • Binding of IgG containing immune complexes to human neutrophil Fc-γ-RII and Fc-γ-RIII induces actin polymerization by a pertussis toxin-insensitive transduction pathway
    • Brennan, P. J., S. H. Zigmond, A. D. Schreiber, E. R. Smith, and F. S. Southwick. 1991. Binding of IgG containing immune complexes to human neutrophil Fc-γ-RII and Fc-γ-RIII induces actin polymerization by a pertussis toxin-insensitive transduction pathway. J. Immunol. 146:4282.
    • (1991) J. Immunol. , vol.146 , pp. 4282
    • Brennan, P.J.1    Zigmond, S.H.2    Schreiber, A.D.3    Smith, E.R.4    Southwick, F.S.5
  • 2
    • 0017806823 scopus 로고
    • Phagocytosis of bacteria by polymorphonuclear leukocytes: A freeze-fracture, scanning electron microscope, and thin-section investigation of membrane structure
    • Moore, P. L., H. L. Bank, N. T. Brissie, and S. S. Spicer. 1978. Phagocytosis of bacteria by polymorphonuclear leukocytes: a freeze-fracture, scanning electron microscope, and thin-section investigation of membrane structure. J. Cell Biol. 76:158.
    • (1978) J. Cell Biol. , vol.76 , pp. 158
    • Moore, P.L.1    Bank, H.L.2    Brissie, N.T.3    Spicer, S.S.4
  • 3
    • 70449140148 scopus 로고
    • A fatal granulomatous of childhood: The study of a new syndrome
    • Berendes, H., R. A. Bridges, and R. A. Good. 1957. A fatal granulomatous of childhood: the study of a new syndrome. Minnesota Med. 309.
    • (1957) Minnesota Med. , pp. 309
    • Berendes, H.1    Bridges, R.A.2    Good, R.A.3
  • 4
    • 0023251352 scopus 로고
    • The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex
    • Dinauer, M. C., S. H. Orkin, R. Brown, A. J. Jesaitis, and C. A. Parkos. 1987. The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex. Nature 327:717.
    • (1987) Nature , vol.327 , pp. 717
    • Dinauer, M.C.1    Orkin, S.H.2    Brown, R.3    Jesaitis, A.J.4    Parkos, C.A.5
  • 6
    • 0018174745 scopus 로고
    • Absence of a newly described cytochrome b from neutrophils of patients with chronic granulomatous disease
    • Segal, W. W., O. T. G. Jones, D. Webster, and A. C. Allison. 1978. Absence of a newly described cytochrome b from neutrophils of patients with chronic granulomatous disease. Lancet 2:446.
    • (1978) Lancet , vol.2 , pp. 446
    • Segal, W.W.1    Jones, O.T.G.2    Webster, D.3    Allison, A.C.4
  • 7
    • 0023175462 scopus 로고
    • 245 subunits from neutrophils in X-linked chronic granulomatous disease
    • 245 subunits from neutrophils in X-linked chronic granulomatous disease. Nature 326:88.
    • (1987) Nature , vol.326 , pp. 88
    • Segal, A.W.1
  • 9
    • 0023870433 scopus 로고
    • Evidence of direct toxic effects of free radicals on the myocardium
    • Burton, K. P. 1988. Evidence of direct toxic effects of free radicals on the myocardium. Free Radic. Biol. Med. 4:15.
    • (1988) Free Radic. Biol. Med. , vol.4 , pp. 15
    • Burton, K.P.1
  • 11
    • 0027404703 scopus 로고
    • Reactive oxygen metabolites, neutrophils, and the pathogenesis of ischemic-tissue/reperfusion
    • Korthuis, R. J., and D. N. Granger. 1993. Reactive oxygen metabolites, neutrophils, and the pathogenesis of ischemic-tissue/reperfusion. Clin. Cardiol. 16:119.
    • (1993) Clin. Cardiol. , vol.16 , pp. 119
    • Korthuis, R.J.1    Granger, D.N.2
  • 12
    • 0030453086 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins
    • DeLeo, F. R., and M. T. Quinn. 1996. Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins. J. Leukocyte Biol. 60:677.
    • (1996) J. Leukocyte Biol. , vol.60 , pp. 677
    • DeLeo, F.R.1    Quinn, M.T.2
  • 13
    • 0024215472 scopus 로고
    • Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease
    • Volpp, B. D., W. M. Nauseef, and R. A. Clark. 1988. Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease. Science 242:1295.
    • (1988) Science , vol.242 , pp. 1295
    • Volpp, B.D.1    Nauseef, W.M.2    Clark, R.A.3
  • 14
    • 0342266916 scopus 로고
    • Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase
    • Volpp, B. D., W. M. Nauseef, J. E. Donelson, D. R. Moser, and R. A. Clark. 1989. Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase. Proc. Natl. Acad. Sci. USA 86:7195.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7195
    • Volpp, B.D.1    Nauseef, W.M.2    Donelson, J.E.3    Moser, D.R.4    Clark, R.A.5
  • 15
    • 0024376120 scopus 로고
    • Recombinant 47-kilodallon cytosolic factor restores NADPH oxidase in chronic granulomatous disease
    • Lomax, K. J., T. L. Leto, H. Nunoi, J. I. Gallin, and H. L. Malech. 1989. Recombinant 47-kilodallon cytosolic factor restores NADPH oxidase in chronic granulomatous disease. Science 245:409.
    • (1989) Science , vol.245 , pp. 409
    • Lomax, K.J.1    Leto, T.L.2    Nunoi, H.3    Gallin, J.I.4    Malech, H.L.5
  • 17
    • 0027787417 scopus 로고
    • phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains
    • phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem. J. 296:557.
    • (1993) Biochem. J. , vol.296 , pp. 557
    • Wientjes, F.B.1    Hsuan, J.J.2    Totty, N.F.3    Segal, A.W.4
  • 18
    • 0025259712 scopus 로고
    • Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation
    • Clark, R. A., B. D. Volpp, K. G. Leidal, and W. M. Nauseef. 1990. Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation. J. Clin. Invest. 85:714.
    • (1990) J. Clin. Invest. , vol.85 , pp. 714
    • Clark, R.A.1    Volpp, B.D.2    Leidal, K.G.3    Nauseef, W.M.4
  • 19
    • 0026787468 scopus 로고
    • r similar to 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system
    • r similar to 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system. J. Biol. Chem. 267:17327.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17327
    • Park, J.W.1    Ma, M.C.2    Ruedi, J.M.3    Smith, R.M.4    Babior, B.M.5
  • 20
    • 0018123055 scopus 로고
    • Novel cytochrome b system in phagocytic vacuoles of human granulocytes
    • Segal, A. W., and O. T. G. Jones. 1978. Novel cytochrome b system in phagocytic vacuoles of human granulocytes. Nature 276:515.
    • (1978) Nature , vol.276 , pp. 515
    • Segal, A.W.1    Jones, O.T.G.2
  • 21
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2
    • Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and G. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2. Science 254:1512.
    • (1991) Science , vol.254 , pp. 1512
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 24
    • 0022340824 scopus 로고
    • Activation of NADPH-dependent superoxide production in a cell free system by sodium dodecyl sulfate
    • Bromberg, Y., and E. Pick. 1985. Activation of NADPH-dependent superoxide production in a cell free system by sodium dodecyl sulfate. J. Biol. Chem. 260: 13539.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13539
    • Bromberg, Y.1    Pick, E.2
  • 25
    • 0029825302 scopus 로고    scopus 로고
    • Pathophysiology, treatment and outcome of meningococcemia: A review and recent experience
    • Kirsch, E. A., R. P. Barton, L. Kitchen, and B. P. Giroir. 1996. Pathophysiology, treatment and outcome of meningococcemia: a review and recent experience. Pediatr. Infect. Dis. J. 15:967.
    • (1996) Pediatr. Infect. Dis. J. , vol.15 , pp. 967
    • Kirsch, E.A.1    Barton, R.P.2    Kitchen, L.3    Giroir, B.P.4
  • 26
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood
    • Boyum, A. 1968. Isolation of mononuclear cells and granulocytes from human blood. J. Clin. Lab. Invest. 21:77.
    • (1968) J. Clin. Lab. Invest. , vol.21 , pp. 77
    • Boyum, A.1
  • 27
    • 0029961380 scopus 로고    scopus 로고
    • Characterization of peptide diffusion into electropermeabilized neutrophils
    • DeLeo, F. R., M. A. Jutila, and M. T. Quinn. 1996. Characterization of peptide diffusion into electropermeabilized neutrophils. J. Immunol. Methods 198:35.
    • (1996) J. Immunol. Methods , vol.198 , pp. 35
    • DeLeo, F.R.1    Jutila, M.A.2    Quinn, M.T.3
  • 28
    • 0032526264 scopus 로고    scopus 로고
    • A novel form of myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation
    • DeLeo, F. R., M. Goedken, S. J. McCormick, and W. M. Nauseef. 1998. A novel form of myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J. Clin. Invest. 101:2900.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2900
    • DeLeo, F.R.1    Goedken, M.2    McCormick, S.J.3    Nauseef, W.M.4
  • 30
    • 0020540731 scopus 로고
    • Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: Translocation during activation
    • Borregaard, N., J. M. Heiple, E. R. Simons, and R. A. Clark. 1983. Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: translocation during activation. J. Cell Biol. 97:52.
    • (1983) J. Cell Biol. , vol.97 , pp. 52
    • Borregaard, N.1    Heiple, J.M.2    Simons, E.R.3    Clark, R.A.4
  • 31
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin in zymosan phagocytosis by macrophages
    • Allen, L.-A. H., and A. Aderem. 1995. A role for MARCKS, the α isozyme of protein kinase C and myosin in zymosan phagocytosis by macrophages. J. Exp. Med. 182:829.
    • (1995) J. Exp. Med. , vol.182 , pp. 829
    • Allen, L.-A.H.1    Aderem, A.2
  • 34
    • 0026062962 scopus 로고
    • Assembly of the neutrophil respiratory burst oxidase: Protein kinase-C promotes cytoskeletal and membrane association of cytosolic oxidase components
    • Nauseef, W. M., B. D. Volpp, S. J. McCormick, K. G. Leidal, and R. A. Clark. 1991. Assembly of the neutrophil respiratory burst oxidase: protein kinase-C promotes cytoskeletal and membrane association of cytosolic oxidase components. J. Biol. Chem. 266:5911.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5911
    • Nauseef, W.M.1    Volpp, B.D.2    McCormick, S.J.3    Leidal, K.G.4    Clark, R.A.5
  • 36
    • 25944474015 scopus 로고
    • The respiratory burst oxidase and certain members of the 48K phosphoprotein family are associated with the neutrophil cytoskeleton
    • Babior, B. M., J. T. Curnutte, and N. Okamura. 1988. The respiratory burst oxidase and certain members of the 48K phosphoprotein family are associated with the neutrophil cytoskeleton. Blood 72:141a.
    • (1988) Blood , vol.72
    • Babior, B.M.1    Curnutte, J.T.2    Okamura, N.3
  • 37
    • 0024334744 scopus 로고
    • Localization of the 47 kDa phosphoprotein involved in the respiratory burst NADPH oxidase of phagocytic cells
    • Heyworth, P. G., C. F. Shrimpton, and A. W. Segal. 1989. Localization of the 47 kDa phosphoprotein involved in the respiratory burst NADPH oxidase of phagocytic cells. Biochem. J. 260:243.
    • (1989) Biochem. J. , vol.260 , pp. 243
    • Heyworth, P.G.1    Shrimpton, C.F.2    Segal, A.W.3
  • 38
    • 0025264449 scopus 로고
    • Continuous phosphorylation of both the 47 and the 49 kDa proteins during superoxide production by neutrophils
    • Heyworth, P. G., and J. A. Badwey. 1990. Continuous phosphorylation of both the 47 and the 49 kDa proteins during superoxide production by neutrophils. Biochim. Biophys. Acta 1052:299.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 299
    • Heyworth, P.G.1    Badwey, J.A.2
  • 39
    • 0027520431 scopus 로고
    • Translocation of rac correlates with NADPH oxidase activation: Evidence for equimolar translocation of oxidase components
    • Quinn, M. T., T. Evans, L. R. Loetterle, A. J. Jesaitis, and G. M. Bokoch. 1993. Translocation of Rac correlates with NADPH oxidase activation: evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268:20983.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20983
    • Quinn, M.T.1    Evans, T.2    Loetterle, L.R.3    Jesaitis, A.J.4    Bokoch, G.M.5
  • 43
    • 0027326416 scopus 로고
    • Functions of polymorphonuclear leukocytes in early rheumatoid arthritis
    • Leirisalo-Repo, M., L. Paimela, S. Koskimies, and H. Repo. 1993. Functions of polymorphonuclear leukocytes in early rheumatoid arthritis. Inflammation 17: 427.
    • (1993) Inflammation , vol.17 , pp. 427
    • Leirisalo-Repo, M.1    Paimela, L.2    Koskimies, S.3    Repo, H.4
  • 44
    • 0025203499 scopus 로고
    • Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor: Translocation to membrane is associated with distinct phosphorylation events
    • Rotrosen, D., and T. L. Leto. 1990. Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor: translocation to membrane is associated with distinct phosphorylation events. J. Biol. Chem. 265:19910.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19910
    • Rotrosen, D.1    Leto, T.L.2
  • 45
    • 0023677609 scopus 로고
    • Phosphorylation of the oxidase-related 48K phosphoprotein family in the unusual autosomal cytochrome-negative and X-linked cytochrome-positive types of chronic granulomatous disease
    • Okamura, N., S. E. Malawista, R. L. Roberts, H. Rosen, H. D. Ochs, B. M. Babior, and J. T. Curnutte. 1988. Phosphorylation of the oxidase-related 48K phosphoprotein family in the unusual autosomal cytochrome-negative and X-linked cytochrome-positive types of chronic granulomatous disease. Blood 72:811.
    • (1988) Blood , vol.72 , pp. 811
    • Okamura, N.1    Malawista, S.E.2    Roberts, R.L.3    Rosen, H.4    Ochs, H.D.5    Babior, B.M.6    Curnutte, J.T.7
  • 47
    • 0028978633 scopus 로고
    • phox, a subunit of the respiratory burst oxidase: Functions of the individual target serines as evaluated by site-directed mutagenesis
    • phox, a subunit of the respiratory burst oxidase: functions of the individual target serines as evaluated by site-directed mutagenesis. J. Clin. Invest. 96:1499.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1499
    • Faust, L.P.1    El Benna, J.2    Babior, B.M.3    Chanock, S.J.4
  • 48
    • 0020554772 scopus 로고
    • Activation of the respiratory burst enzyme in human polymorphonuclear leukocytes by chemoattractants and other soluble stimuli evidence that the same oxidase is activated by different transductional mechanisms
    • McPhail, L. C., and R. Snyderman. 1983. Activation of the respiratory burst enzyme in human polymorphonuclear leukocytes by chemoattractants and other soluble stimuli evidence that the same oxidase is activated by different transductional mechanisms. J. Clin. Invest. 72:192.
    • (1983) J. Clin. Invest. , vol.72 , pp. 192
    • McPhail, L.C.1    Snyderman, R.2
  • 49
    • 0021869042 scopus 로고
    • Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system
    • Curnutte, J. T. 1985. Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system. J. Clin. Invest. 75:1740.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1740
    • Curnutte, J.T.1
  • 50
    • 0023664087 scopus 로고
    • NADPH oxidase of human neutrophils: Subcellular localization and characterization of an arachidonate-activatable superoxide-generating system
    • Clark, R. A., K. G. Leidel, D. W. Pearson, and W. M. Nauseef. 1987. NADPH oxidase of human neutrophils: subcellular localization and characterization of an arachidonate-activatable superoxide-generating system. J. Biol. Chem. 262:4065.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4065
    • Clark, R.A.1    Leidel, K.G.2    Pearson, D.W.3    Nauseef, W.M.4
  • 51
    • 0021804086 scopus 로고
    • Activation of the respiratory burst enzyme from human neutrophils in a cell-free system: Evidence for a soluble cofactor
    • McPhail, L. C., P. S. Shirley, C. C. Clayton, and R. Snyderman. 1985. Activation of the respiratory burst enzyme from human neutrophils in a cell-free system: evidence for a soluble cofactor. J. Clin. Invest. 75:1735.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1735
    • McPhail, L.C.1    Shirley, P.S.2    Clayton, C.C.3    Snyderman, R.4
  • 52
    • 0029555377 scopus 로고
    • Cell-free activation of the respiratory burst oxidase by protein kinase C
    • El Benna, J., J.-W. Park, J. M. Ruedi, and B. M. Babior. 1995. Cell-free activation of the respiratory burst oxidase by protein kinase C. Blood Cells Mol. Dis. 21:201.
    • (1995) Blood Cells Mol. Dis. , vol.21 , pp. 201
    • El Benna, J.1    Park, J.-W.2    Ruedi, J.M.3    Babior, B.M.4
  • 56
    • 0029096185 scopus 로고
    • Cell-free activation of neutrophil NADPH oxidase by a phosphatidic acid-regulated protein kinase
    • McPhail, L. C., D. Qualliotine-Mann, and K. A. Waite. 1995. Cell-free activation of neutrophil NADPH oxidase by a phosphatidic acid-regulated protein kinase. Proc. Natl. Acad. Sci. USA 92:7931.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7931
    • McPhail, L.C.1    Qualliotine-Mann, D.2    Waite, K.A.3
  • 57
    • 0028281049 scopus 로고
    • Regulatory interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton in human neutrophils
    • Klotz, K.-N., K. L. Krotec, J. Gripentrog, and A. J. Jesaitis. 1994. Regulatory interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton in human neutrophils. J. Immunol. 152:801.
    • (1994) J. Immunol. , vol.152 , pp. 801
    • Klotz, K.-N.1    Krotec, K.L.2    Gripentrog, J.3    Jesaitis, A.J.4
  • 58
    • 0027722215 scopus 로고
    • Cytoskeletal regulation of chemotactic receptors: Molecular complexation of N-formyl peptide receptors with G proteins and actin
    • Jesaitis, A. J., and K.-N. Klotz. 1993. Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin. Eur. J. Haematol. 51:288.
    • (1993) Eur. J. Haematol. , vol.51 , pp. 288
    • Jesaitis, A.J.1    Klotz, K.-N.2
  • 59
    • 0028142461 scopus 로고
    • phox during neutrophil activation: Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • phox during neutrophil activation: phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J. Biol. Chem. 269:23431.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23431
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 61
    • 0029983262 scopus 로고    scopus 로고
    • phox as determined by two-dimensional phosphopeptide mapping: Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase
    • phox as determined by two-dimensional phosphopeptide mapping: phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase. J. Biol. Chem. 271:6374.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6374
    • El Benna, J.1    Faust, L.P.2    Johnson, J.L.3    Babior, B.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.