메뉴 건너뛰기




Volumn 62, Issue 19-20, 2005, Pages 2173-2193

Regulation and termination of NADPH oxidase activity

Author keywords

G proteins; Leukocytes; Neutrophil; Phagocytes; Phosphatase; Rac; Reactive oxygen species; Respiratory burst

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHEMOATTRACTANT; CHEMOKINE; GUANOSINE TRIPHOSPHATE; INTEGRIN; IONOPHORE; MYELOPEROXIDASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN P40; RAC PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; ZYMOSAN;

EID: 27144535425     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5177-1     Document Type: Review
Times cited : (219)

References (227)
  • 1
    • 0017834531 scopus 로고
    • Oxygen-dependent microbial killing by phagocytes
    • Babior B. M. (1978) Oxygen-dependent microbial killing by phagocytes. N. Engl. J. Med. 298: 659-668
    • (1978) N. Engl. J. Med. , vol.298 , pp. 659-668
    • Babior, B.M.1
  • 2
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton M. B., Kettle A. J. and 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
  • 3
    • 0037177615 scopus 로고    scopus 로고
    • Lethal weapons
    • Roos D. and Winterbourn C. C. (2002) Lethal weapons. Science 296: 669-671
    • (2002) Science , vol.296 , pp. 669-671
    • Roos, D.1    Winterbourn, C.C.2
  • 4
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • Chapman A. L., Hampton M. B., Senthilmohan R., Winterbourn C. C. and Kettle A. J. (2002) Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. J. Biol. Chem. 277: 9757-9762
    • (2002) J. Biol. Chem. , vol.277 , pp. 9757-9762
    • Chapman, A.L.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 5
    • 7244253000 scopus 로고    scopus 로고
    • Dual role of phagocytic NADPH oxidase in bacterial killing
    • Rada B. K., Geiszt M., Káldi K., Tímár C. and Ligeti E. (2004) Dual role of phagocytic NADPH oxidase in bacterial killing. Blood 104: 2947-2953
    • (2004) Blood , vol.104 , pp. 2947-2953
    • Rada, B.K.1    Geiszt, M.2    Káldi, K.3    Tímár, C.4    Ligeti, E.5
  • 6
    • 0014124339 scopus 로고
    • Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function
    • Holmes B., Page A. R. and Good R. A. (1967) Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function. J. Clin. Invest. 46: 1422-1432
    • (1967) J. Clin. Invest. , vol.46 , pp. 1422-1432
    • Holmes, B.1    Page, A.R.2    Good, R.A.3
  • 7
    • 0025976579 scopus 로고
    • Molecular basis of chronic granulomatous disease
    • Smith R. M. and Curnutte J. T. (1991) Molecular basis of chronic granulomatous disease. Blood 77: 673-686
    • (1991) Blood , vol.77 , pp. 673-686
    • Smith, R.M.1    Curnutte, J.T.2
  • 8
    • 0014005822 scopus 로고
    • Fatal granulomatous disease of childhood: An inborn abnormality of phagocytic function
    • Holmes B., Quie P. G., Windhorst D. B. and Good R. A. (1966) Fatal granulomatous disease of childhood: an inborn abnormality of phagocytic function. Lancet i: 1225-1228
    • (1966) Lancet , vol.1 , pp. 1225-1228
    • Holmes, B.1    Quie, P.G.2    Windhorst, D.B.3    Good, R.A.4
  • 10
    • 0001854459 scopus 로고    scopus 로고
    • Inherited Disorders of phagocyte killing
    • Scriver C. R., Beaudet A. L., Valle D., Sly W. S., Childs B., Kinzler K. W. et al. (Eds), McGraw-Hill, New York
    • Dinauer M. C., Nauseef W. M. and Newburger P. E. (2001) Inherited Disorders of phagocyte killing. In: The Metabolic and Molecular Bases of Inherited Disease, 8th edn., pp. 4857-4887, vol. 3, Scriver C. R., Beaudet A. L., Valle D., Sly W. S., Childs B., Kinzler K. W. et al. (Eds), McGraw-Hill, New York.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease, 8th Edn. , vol.3 , pp. 4857-4887
    • Dinauer, M.C.1    Nauseef, W.M.2    Newburger, P.E.3
  • 12
    • 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., Volpp B. D., McCormick S., Leidal K. G. and Clark R. A. (1991) Assembly of the neutrophil respiratory burst oxidase: protein kinase C promotes cytoskeletal and membrane association of cytosolic oxidase components. J. Biol. Chem. 266: 5911-5917
    • (1991) J. Biol. Chem. , vol.266 , pp. 5911-5917
    • Nauseef, W.M.1    Volpp, B.D.2    McCormick, S.3    Leidal, K.G.4    Clark, R.A.5
  • 14
    • 0019436436 scopus 로고
    • Characteristics of the cofactor requirements for the superoxide- generating NADPH oxidase of human polymorphonuclear leukocytes
    • Light D. R., Walsh C., O'Callaghan A. M., Goetzl E. J. and Tauber A. I. (1981) Characteristics of the cofactor requirements for the superoxide- generating NADPH oxidase of human polymorphonuclear leukocytes. Biochemistry 20: 1468-1476
    • (1981) Biochemistry , vol.20 , pp. 1468-1476
    • Light, D.R.1    Walsh, C.2    O'Callaghan, A.M.3    Goetzl, E.J.4    Tauber, A.I.5
  • 15
    • 0000792494 scopus 로고
    • The extra respiration of phagocytosis
    • Baldridge C. W. and Gerard R. W. (1933) The extra respiration of phagocytosis. Am. J. Physiol. 103: 235-236
    • (1933) Am. J. Physiol. , vol.103 , pp. 235-236
    • Baldridge, C.W.1    Gerard, R.W.2
  • 16
    • 0000054142 scopus 로고
    • The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes
    • Sbarra A. J. and Karnovsky M. L. (1959) The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J. Biol. Chem. 234: 1355-1362
    • (1959) J. Biol. Chem. , vol.234 , pp. 1355-1362
    • Sbarra, A.J.1    Karnovsky, M.L.2
  • 17
    • 0000725406 scopus 로고
    • Biochemical aspects of phagocytosis
    • Iyer G. Y. N., Islam M. F. and Quastel J. H. (1961) Biochemical aspects of phagocytosis. Nature 192: 535-541
    • (1961) Nature , vol.192 , pp. 535-541
    • Iyer, G.Y.N.1    Islam, M.F.2    Quastel, J.H.3
  • 18
    • 0017622613 scopus 로고
    • 2 - Studies with normal and cytochalasin B-treated cells
    • 2 - studies with normal and cytochalasin B-treated cells. J. Clin. Invest. 60: 1266-1279
    • (1977) J. Clin. Invest. , vol.60 , pp. 1266-1279
    • Root, R.K.1    Metcalf, J.A.2
  • 19
    • 0018183487 scopus 로고
    • Superoxide production by digitonin-stimulated guinea pig granulocytes: The effects of N-ethyl maleimide, divalent cations, and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system
    • Cohen H. J. and Chovaniec M. E. (1978) Superoxide production by digitonin-stimulated guinea pig granulocytes: the effects of N-ethyl maleimide, divalent cations, and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system. J. Clin. Invest. 61: 1088-1096
    • (1978) J. Clin. Invest. , vol.61 , pp. 1088-1096
    • Cohen, H.J.1    Chovaniec, M.E.2
  • 20
    • 0002501831 scopus 로고    scopus 로고
    • Interactions between the components of the human NADPH oxidase: A review about the intrigues in the phox family
    • Leusen J. H. W., Verhoeven A. J. and Roos D. (1996) Interactions between the components of the human NADPH oxidase: a review about the intrigues in the phox family. Front. Biosci. 1: d72-d90
    • (1996) Front. Biosci. , vol.1
    • Leusen, J.H.W.1    Verhoeven, A.J.2    Roos, D.3
  • 21
    • 0030453086 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase components
    • DeLeo F. R. and Quinn M. T. (1996) Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase components. J. Leukoc. Biol. 60: 677-691
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 677-691
    • DeLeo, F.R.1    Quinn, M.T.2
  • 22
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior B. M. (1999) NADPH oxidase: an update. Blood 93: 1464-1476
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 23
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais P. V. (2002) The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol. Life Sci. 59: 1428-1459
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 24
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef W. M. (2004) Assembly of the phagocyte NADPH oxidase. Histochem. Cell Biol. 122: 277-291
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 25
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn M. T. and Gauss K. A. (2004) Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukoc. Biol. 76: 760-781
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 26
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes - Prototype of the NOX electron transport chain systems
    • Cross A. R. and Segal A. W. (2004) The NADPH oxidase of professional phagocytes - prototype of the NOX electron transport chain systems. Biochim. Biophys. Acta 1657: 1-22
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 28
    • 0023774165 scopus 로고
    • Rapid deactivation of NADPH oxidase in neutrophils: Continuous replacement by newly activated enzyme sustains the respiratory burst
    • Akard L. P., English D. and Gabig T. G. (1988) Rapid deactivation of NADPH oxidase in neutrophils: continuous replacement by newly activated enzyme sustains the respiratory burst. Blood 72: 322-327
    • (1988) Blood , vol.72 , pp. 322-327
    • Akard, L.P.1    English, D.2    Gabig, T.G.3
  • 29
    • 0026757393 scopus 로고
    • Effects of antagonists of protein phosphatases on superoxide release by neutrophils
    • Ding J. and Badwey J. A. (1992) Effects of antagonists of protein phosphatases on superoxide release by neutrophils. J. Biol. Chem. 267: 6442-6448
    • (1992) J. Biol. Chem. , vol.267 , pp. 6442-6448
    • Ding, J.1    Badwey, J.A.2
  • 31
    • 0027520431 scopus 로고
    • Translocation of Rac correlates with NADPH oxidase activation: Evidence for equimolar translocation of oxidase components
    • Quinn M. T., Evans T., Loetterle L. R., Jesaitis A. J. and Bokoch G. M. (1993) Translocation of Rac correlates with NADPH oxidase activation: evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268: 20983-20987
    • (1993) J. Biol. Chem. , vol.268 , pp. 20983-20987
    • Quinn, M.T.1    Evans, T.2    Loetterle, L.R.3    Jesaitis, A.J.4    Bokoch, G.M.5
  • 32
    • 0030756377 scopus 로고    scopus 로고
    • Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex: Evidence for a novel cycle of phosphorylation and dephosphorylation
    • Heyworth P. G., Robinson J. M., Ding J., Ellis B. A. and Badwey J. A. (1997) Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex: evidence for a novel cycle of phosphorylation and dephosphorylation. Histochem. Cell Biol. 108: 221-233
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 221-233
    • Heyworth, P.G.1    Robinson, J.M.2    Ding, J.3    Ellis, B.A.4    Badwey, J.A.5
  • 35
    • 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
  • 36
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • Stocker R. and Keaney J. F. Jr (2004) Role of oxidative modifications in atherosclerosis. Physiol. Rev. 84: 1381-1478
    • (2004) Physiol. Rev. , vol.84 , pp. 1381-1478
    • Stocker, R.1    Keaney Jr., J.F.2
  • 37
    • 0030663253 scopus 로고    scopus 로고
    • Ischemic stroke injury is reduced in mice lacking a functional NADPH oxidase
    • Walder C. E., Green S. P., Darbonne W. C., Mathias J., Rae J., Dinauer M. C. et al. (1997) Ischemic stroke injury is reduced in mice lacking a functional NADPH oxidase. Stroke 28: 2252-2258
    • (1997) Stroke , vol.28 , pp. 2252-2258
    • Walder, C.E.1    Green, S.P.2    Darbonne, W.C.3    Mathias, J.4    Rae, J.5    Dinauer, M.C.6
  • 38
    • 0033960425 scopus 로고    scopus 로고
    • Inhibition of the Rac1 GTPase protects against nonlethal ischemia/reperfusion-induced necrosis and apoptosis in vivo
    • Ozaki M., Deshpande S. S., Angkeow P., Bellan J., Lowenstein C. J., Dinauer M. C. et al. (2000) Inhibition of the Rac1 GTPase protects against nonlethal ischemia/reperfusion-induced necrosis and apoptosis in vivo. FASEB J. 14: 418-429
    • (2000) FASEB J. , vol.14 , pp. 418-429
    • Ozaki, M.1    Deshpande, S.S.2    Angkeow, P.3    Bellan, J.4    Lowenstein, C.J.5    Dinauer, M.C.6
  • 39
    • 0033802236 scopus 로고    scopus 로고
    • NADPH oxidase-derived free radicals are key oxidants in alcohol-induced liver disease
    • Kono H., Rusyn I., Yin M., Gäbele E., Yamashina S., Dikalova A. et al. (2000) NADPH oxidase-derived free radicals are key oxidants in alcohol-induced liver disease. J. Clin. Invest. 106: 867-872
    • (2000) J. Clin. Invest. , vol.106 , pp. 867-872
    • Kono, H.1    Rusyn, I.2    Yin, M.3    Gäbele, E.4    Yamashina, S.5    Dikalova, A.6
  • 40
    • 0037947448 scopus 로고    scopus 로고
    • NADPH oxidase mediates oxidative stress in the 1-methyl-4-phenyl-1,2.3,6- tetrahydropyridine model of Parkinson's disease
    • USA
    • Wu D. C., Teismann P., Tieu K., Vila M., Jackson-Lewis V., Ischiropoulos H. et al. (2003) NADPH oxidase mediates oxidative stress in the 1-methyl-4-phenyl-1,2.3,6-tetrahydropyridine model of Parkinson's disease. Proc. Natl. Acad. Sci. USA 100: 6145-6150
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 6145-6150
    • Wu, D.C.1    Teismann, P.2    Tieu, K.3    Vila, M.4    Jackson-Lewis, V.5    Ischiropoulos, H.6
  • 41
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R. S., Nemoto S. and Finkel T. (2005) Mitochondria, oxidants, and aging. Cell 120: 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 42
    • 0018136591 scopus 로고
    • Differences in oxygen metabolism of phagocytosing monocytes and neutrophils
    • Reiss M. and Roos D. (1978) Differences in oxygen metabolism of phagocytosing monocytes and neutrophils. J. Clin. Invest. 61: 480-488
    • (1978) J. Clin. Invest. , vol.61 , pp. 480-488
    • Reiss, M.1    Roos, D.2
  • 43
    • 0017876650 scopus 로고
    • Permeation of the erythrocyte stroma by superoxide radical
    • Lynch R. E. and Fridovich I. (1978) Permeation of the erythrocyte stroma by superoxide radical. J. Biol. Chem. 253: 4697-4699
    • (1978) J. Biol. Chem. , vol.253 , pp. 4697-4699
    • Lynch, R.E.1    Fridovich, I.2
  • 44
    • 0018749934 scopus 로고
    • The release of superoxide anion from granulocytes: Effect of inhibitors of anion permeability
    • Gennaro R. and Romeo D. (1979) The release of superoxide anion from granulocytes: effect of inhibitors of anion permeability. Biochem. Biophys. Res. Commun. 88: 44-49
    • (1979) Biochem. Biophys. Res. Commun. , vol.88 , pp. 44-49
    • Gennaro, R.1    Romeo, D.2
  • 45
    • 0020045904 scopus 로고
    • Neutrophil-mediated methemoglobin formation in the erythrocyte: The role of superoxide and hydrogen peroxide
    • Weiss S. J. (1982) Neutrophil-mediated methemoglobin formation in the erythrocyte: the role of superoxide and hydrogen peroxide. J. Biol. Chem. 257: 2947-2953
    • (1982) J. Biol. Chem. , vol.257 , pp. 2947-2953
    • Weiss, S.J.1
  • 46
    • 0021368186 scopus 로고
    • Excretion of superoxide by phagocytes measured with cytochrome c entrapped in resealed erythrocyte ghosts
    • Roos D., Eckmann C. M., Yazdanbakhsh M., Hamers M. N. and Boer M. de (1984) Excretion of superoxide by phagocytes measured with cytochrome c entrapped in resealed erythrocyte ghosts. J. Biol. Chem. 259: 1770-1775
    • (1984) J. Biol. Chem. , vol.259 , pp. 1770-1775
    • Roos, D.1    Eckmann, C.M.2    Yazdanbakhsh, M.3    Hamers, M.N.4    De Boer, M.5
  • 48
    • 0344304496 scopus 로고    scopus 로고
    • Interactions between electron and proton currents in excised patches from human eosinophils
    • Petheö G. L., Maturana A., Spät A. and Demaurex N. (2003) Interactions between electron and proton currents in excised patches from human eosinophils. J. Gen. Physiol. 122:713-726
    • (2003) J. Gen. Physiol. , vol.122 , pp. 713-726
    • Petheö, G.L.1    Maturana, A.2    Spät, A.3    Demaurex, N.4
  • 49
    • 0034612381 scopus 로고    scopus 로고
    • Simultaneous activation of NADPH oxidase-related proton and electron currents in human neutrophils
    • USA
    • DeCoursey T. E., Cherny V. V., Zhou W. and Thomas L. L. (2000) Simultaneous activation of NADPH oxidase-related proton and electron currents in human neutrophils. Proc. Natl. Acad. Sci. USA 97: 6885-6889
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 6885-6889
    • DeCoursey, T.E.1    Cherny, V.V.2    Zhou, W.3    Thomas, L.L.4
  • 50
    • 0016591134 scopus 로고
    • 2 release from human granulocytes during phagocytosis. I. Documentation, quantitation, and some regulating factors
    • 2 release from human granulocytes during phagocytosis. I. Documentation, quantitation, and some regulating factors. J. Clin. Invest. 55: 945-955
    • (1975) J. Clin. Invest. , vol.55 , pp. 945-955
    • Root, R.K.1    Metcalf, J.2    Oshino, N.3    Chance, B.4
  • 51
    • 0018181346 scopus 로고
    • Superoxide generation by digitonin-stimulated guinea pig granulocytes: A basis for a continuous assay for monitoring superoxide production and for the study of the activation of the generating system
    • Cohen H. J. and Chovaniec M. E. (1978) Superoxide generation by digitonin-stimulated guinea pig granulocytes: a basis for a continuous assay for monitoring superoxide production and for the study of the activation of the generating system. J. Clin. Invest. 61: 1081-1087
    • (1978) J. Clin. Invest. , vol.61 , pp. 1081-1087
    • Cohen, H.J.1    Chovaniec, M.E.2
  • 53
    • 0025203499 scopus 로고
    • Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor: Translocation to membrane is associated with distinct phosphorylation events
    • Rotrosen D. and Leto T. L. (1990) Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor: translocation to membrane is associated with distinct phosphorylation events. J. Biol. Chem. 265: 19910-19915
    • (1990) J. Biol. Chem. , vol.265 , pp. 19910-19915
    • Rotrosen, D.1    Leto, T.L.2
  • 55
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y. Lapouge K., Smerdon S. J. and Rittinger K. (2003) Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113: 343-355
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 58
    • 0027395762 scopus 로고
    • The immediate activator of the NADPH oxidase is arachidonate not phosphorylation
    • Henderson L. M., Moule S. K. and Chappell J. B. (1993) The immediate activator of the NADPH oxidase is arachidonate not phosphorylation. Eur. J. Biochem. 211: 157-162
    • (1993) Eur. J. Biochem. , vol.211 , pp. 157-162
    • Henderson, L.M.1    Moule, S.K.2    Chappell, J.B.3
  • 59
    • 0026787468 scopus 로고
    • r approximately 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system
    • r approximately 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system. J. Biol. Chem. 267: 17327-19332
    • (1992) J. Biol. Chem. , vol.267 , pp. 17327-19332
    • Park, J.W.1    Ma, M.2    Ruedi, J.M.3    Smith, R.M.4    Babior, B.M.5
  • 60
    • 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: 557-561
    • (1993) Biochem. J. , vol.296 , pp. 557-561
    • Wientjes, F.B.1    Hsuan, J.J.2    Totty, N.F.3    Segal, A.W.4
  • 63
    • 0037248553 scopus 로고    scopus 로고
    • 2, PtdIns(3)P. and PKC in intracellular production of reactive oxygen species by the NADPH oxidase
    • 2, PtdIns(3)P. and PKC in intracellular production of reactive oxygen species by the NADPH oxidase. Mol. Cell. 11: 35-47
    • (2003) Mol. Cell. , vol.11 , pp. 35-47
    • Brown, G.E.1    Stewart, M.Q.2    Liu, H.3    Ha, V.L.4    Yaffe, M.B.5
  • 64
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2
    • Knaus U. G., Heyworth P. G., Evans T., Curnutte J. T. and Bokoch G. M. (1991) Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254: 1512-1515
    • (1991) Science , vol.254 , pp. 1512-1515
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 67
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey T. E. (2003) Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83: 475-579
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 69
    • 0027375484 scopus 로고
    • Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils
    • DeCoursey T. E. and Cherny V. V. (1993) Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils. Biophys. J. 65: 1590-1598
    • (1993) Biophys. J. , vol.65 , pp. 1590-1598
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 72
    • 0033618397 scopus 로고    scopus 로고
    • + channel in phagocyte-like cells
    • + channel in phagocyte-like cells. J. Biol. Chem. 274: 21603-21608
    • (1999) J. Biol. Chem. , vol.274 , pp. 21603-21608
    • Lowenthal, A.1    Levy, R.2
  • 73
    • 0035884148 scopus 로고    scopus 로고
    • Activation of NADPH oxidase-related proton and electron currents in human eosinophils by arachidonic acid
    • Cherny V. V., Henderson L. M., Xu W., Thomas L. L. and DeCoursey T. E. (2001) Activation of NADPH oxidase-related proton and electron currents in human eosinophils by arachidonic acid. J. Physiol. 535: 783-794
    • (2001) J. Physiol. , vol.535 , pp. 783-794
    • Cherny, V.V.1    Henderson, L.M.2    Xu, W.3    Thomas, L.L.4    DeCoursey, T.E.5
  • 74
    • 0025720460 scopus 로고
    • + (equivalent) conductance in the plasma membrane of human neutrophils
    • USA
    • + (equivalent) conductance in the plasma membrane of human neutrophils. Proc. Natl. Acad. Sci. USA 88: 10816-10820
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 10816-10820
    • Nanda, A.1    Grinstein, S.2
  • 75
    • 0026567207 scopus 로고
    • +-conducting pathway in the membrane of neutrophils
    • +-conducting pathway in the membrane of neutrophils. Biochem. J. 281: 697-701
    • (1992) Biochem. J. , vol.281 , pp. 697-701
    • Kapus, A.1    Szászi, K.2    Ligeti, E.3
  • 76
    • 0027930257 scopus 로고
    • Activation of multiple pH-regulatory pathways in granulocytes by a phosphotyrosine phosphatase antagonist
    • Bianchini L., Nanda A., Wasan S. and Grinstein S. (1994) Activation of multiple pH-regulatory pathways in granulocytes by a phosphotyrosine phosphatase antagonist. Biochem. J. 301: 539-544
    • (1994) Biochem. J. , vol.301 , pp. 539-544
    • Bianchini, L.1    Nanda, A.2    Wasan, S.3    Grinstein, S.4
  • 78
    • 0037417274 scopus 로고    scopus 로고
    • The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels
    • DeCoursey T. E., Morgan D. and Cherny V. V. (2003) The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels. Nature 422: 531-534
    • (2003) Nature , vol.422 , pp. 531-534
    • DeCoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 79
    • 0242573134 scopus 로고    scopus 로고
    • Interactions between NADPH oxidase and voltage-gated proton channels: Why electron transport depends on proton transport
    • DeCoursey T. E. (2003) Interactions between NADPH oxidase and voltage-gated proton channels: why electron transport depends on proton transport. FEBS Lett. 555: 57-61
    • (2003) FEBS Lett. , vol.555 , pp. 57-61
    • DeCoursey, T.E.1
  • 81
    • 20544437867 scopus 로고    scopus 로고
    • Voltage- and NADPH-dependence of electron currents generated by the phagocytic NADPH oxidase
    • Petheo G. L. and Demaurex N. (2005) Voltage- and NADPH-dependence of electron currents generated by the phagocytic NADPH oxidase. Biochem. J. 388: 485-491
    • (2005) Biochem. J. , vol.388 , pp. 485-491
    • Petheo, G.L.1    Demaurex, N.2
  • 82
    • 0033016470 scopus 로고    scopus 로고
    • -245 are required for the activation of NADPH oxidase by anionic amphiphiles: Evidence for an intermediate state of oxidase activation
    • -245 are required for the activation of NADPH oxidase by anionic amphiphiles: evidence for an intermediate state of oxidase activation. J. Biol. Chem. 274: 15519-15525
    • (1999) J. Biol. Chem. , vol.274 , pp. 15519-15525
    • Cross, A.R.1    Erickson, R.W.2    Curnutte, J.T.3
  • 84
    • 0018712161 scopus 로고
    • Effects of oxygen tension and pH on the respiratory burst of human neutrophils
    • Gabig T. G., Bearman S. I. and Babior B. M. (1979) Effects of oxygen tension and pH on the respiratory burst of human neutrophils. Blood 53: 1133-1139
    • (1979) Blood , vol.53 , pp. 1133-1139
    • Gabig, T.G.1    Bearman, S.I.2    Babior, B.M.3
  • 85
    • 0015380565 scopus 로고
    • Comparative study of the metabolic and bactericidal characteristics of severely glucose-6-phosphate dehydrogenase-deficient polymorphonuclear leukocytes and leukocytes from children with chronic granulomatous disease
    • Baehner R. L., Johnston R. B. Jr and Nathan D. G. (1972) Comparative study of the metabolic and bactericidal characteristics of severely glucose-6-phosphate dehydrogenase-deficient polymorphonuclear leukocytes and leukocytes from children with chronic granulomatous disease. J. Reticuloendothel. Soc. 12: 150-169
    • (1972) J. Reticuloendothel. Soc. , vol.12 , pp. 150-169
    • Baehner, R.L.1    Johnston Jr., R.B.2    Nathan, D.G.3
  • 86
    • 0019226842 scopus 로고
    • NAD(P)H oxidase activity in human neutrophils stimulated by phorbol myristate acetate
    • Suzuki Y. and Lehrer R. I. (1980) NAD(P)H oxidase activity in human neutrophils stimulated by phorbol myristate acetate. J. Clin. Invest. 66: 1409-1418
    • (1980) J. Clin. Invest. , vol.66 , pp. 1409-1418
    • Suzuki, Y.1    Lehrer, R.I.2
  • 87
    • 0016288969 scopus 로고
    • Reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate diaphorase activity in human polymorphonuclear leukocytes
    • DeChatelet L. R., McPhail L. C., Mullikin D. and McCall C. E. (1974) Reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate diaphorase activity in human polymorphonuclear leukocytes. Infect. Immun. 10: 528-534
    • (1974) Infect. Immun. , vol.10 , pp. 528-534
    • DeChatelet, L.R.1    McPhail, L.C.2    Mullikin, D.3    McCall, C.E.4
  • 88
    • 0020518299 scopus 로고
    • Activation of mouse peritoneal macrophages by lipopolysaccharide alters the kinetic parameters of the superoxide-producing NADPH oxidase
    • Sasada M., Pabst M. J. and Johnston R. B. Jr (1983) Activation of mouse peritoneal macrophages by lipopolysaccharide alters the kinetic parameters of the superoxide-producing NADPH oxidase. J. Biol. Chem. 258: 9631-9635
    • (1983) J. Biol. Chem. , vol.258 , pp. 9631-9635
    • Sasada, M.1    Pabst, M.J.2    Johnston Jr., R.B.3
  • 89
    • 0018877341 scopus 로고
    • Activation of the guinea pig granulocyte NAD(P)H-dependent superoxide generating enzyme: Localization in a plasma membrane enriched particle and kinetics of activation
    • Cohen H. J., Chovaniec M. E. and Davies W. A. (1980) Activation of the guinea pig granulocyte NAD(P)H-dependent superoxide generating enzyme: localization in a plasma membrane enriched particle and kinetics of activation. Blood 55: 355-363
    • (1980) Blood , vol.55 , pp. 355-363
    • Cohen, H.J.1    Chovaniec, M.E.2    Davies, W.A.3
  • 90
    • 0020490563 scopus 로고
    • Functional relationship of the cytochrome b to the superoxide-generating oxidase of human neutrophils
    • Gabig T. G., Schervish E. W. and Santinga J. T. (1982) Functional relationship of the cytochrome b to the superoxide-generating oxidase of human neutrophils. J. Biol. Chem. 257: 4114-4119
    • (1982) J. Biol. Chem. , vol.257 , pp. 4114-4119
    • Gabig, T.G.1    Schervish, E.W.2    Santinga, J.T.3
  • 91
    • 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 Snyderman R. (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: 192-200
    • (1983) J. Clin. Invest. , vol.72 , pp. 192-200
    • McPhail, L.C.1    Snyderman, R.2
  • 94
    • 0019815612 scopus 로고
    • A variant of chronic granulomatous disease: Deficient oxidative metabolism due to a low-affinity NADPH oxidase
    • Lew P. D., Southwick F. S., Stossel T. P., Whitin J. C., Simons E. and Cohen H. J. (1981) A variant of chronic granulomatous disease: deficient oxidative metabolism due to a low-affinity NADPH oxidase. N. Engl. J. Med. 305: 1329-1333
    • (1981) N. Engl. J. Med. , vol.305 , pp. 1329-1333
    • Lew, P.D.1    Southwick, F.S.2    Stossel, T.P.3    Whitin, J.C.4    Simons, E.5    Cohen, H.J.6
  • 95
    • 0020618499 scopus 로고
    • Impaired granulocyte superoxide production and prolongation of the respiratory burst due to a low-affinity NADPH-dependent oxidase
    • Shurin S. B., Cohen H. J., Whitin J. C. and Newburger P. E. (1983) Impaired granulocyte superoxide production and prolongation of the respiratory burst due to a low-affinity NADPH-dependent oxidase. Blood 62: 564-571
    • (1983) Blood , vol.62 , pp. 564-571
    • Shurin, S.B.1    Cohen, H.J.2    Whitin, J.C.3    Newburger, P.E.4
  • 97
    • 0013852539 scopus 로고
    • Early changes of hexose monophosphate pathway activity and of NADPH oxidation in phagocytizing leucocytes
    • Zatti M. and Rossi F. (1965) Early changes of hexose monophosphate pathway activity and of NADPH oxidation in phagocytizing leucocytes. Biochim. Biophys. Acta 99: 557-561
    • (1965) Biochim. Biophys. Acta , vol.99 , pp. 557-561
    • Zatti, M.1    Rossi, F.2
  • 98
    • 0015181975 scopus 로고
    • Intraleukocytic microbicidal defects
    • Klebanoff S. J. (1971) Intraleukocytic microbicidal defects. Annu. Rev. Med. 22: 39-62
    • (1971) Annu. Rev. Med. , vol.22 , pp. 39-62
    • Klebanoff, S.J.1
  • 99
    • 0015397080 scopus 로고
    • Hexose monophosphate shunt activity and oxygen consumption during phagocytosis: Temporal sequence
    • DeChatelet L. R., Wang P. and McCall C.E. (1972) Hexose monophosphate shunt activity and oxygen consumption during phagocytosis: temporal sequence. Proc. Soc. Exp. Biol. Med. 140: 1434-1436
    • (1972) Proc. Soc. Exp. Biol. Med. , vol.140 , pp. 1434-1436
    • DeChatelet, L.R.1    Wang, P.2    McCall, C.E.3
  • 100
    • 0020730441 scopus 로고
    • Evidence that NADPH is the actual substrate of the oxidase responsible for the "respiratory burst" of phagocytosing polymorphonuclear leukocytes
    • Tokyo
    • Suzuki H. and Kakinuma K. (1983) Evidence that NADPH is the actual substrate of the oxidase responsible for the "respiratory burst" of phagocytosing polymorphonuclear leukocytes. J. Biochem. (Tokyo) 93: 709-715
    • (1983) J. Biochem. , vol.93 , pp. 709-715
    • Suzuki, H.1    Kakinuma, K.2
  • 101
    • 0021203722 scopus 로고
    • Proton secretion by stimulated neutrophils: Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst
    • Borregaard N., Schwartz J. H. and Tauber A. I. (1984) Proton secretion by stimulated neutrophils: significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst. J. Clin. Invest. 74: 455-459
    • (1984) J. Clin. Invest. , vol.74 , pp. 455-459
    • Borregaard, N.1    Schwartz, J.H.2    Tauber, A.I.3
  • 102
    • 0015910925 scopus 로고
    • Neutrophil dysfunction, chronic granulomatous disease, and non-spherocytic haemolytic anaemia caused by complete deficiency of glucose-6-phosphate dehydrogenase
    • Gray G. R., Stamatoyannopoulos G., Naiman S. C., Kliman M. R., Klebanoff S. J., Austin T. et al. (1973) Neutrophil dysfunction, chronic granulomatous disease, and non-spherocytic haemolytic anaemia caused by complete deficiency of glucose-6-phosphate dehydrogenase. Lancet ii: 530-534
    • (1973) Lancet , vol.2 , pp. 530-534
    • Gray, G.R.1    Stamatoyannopoulos, G.2    Naiman, S.C.3    Kliman, M.R.4    Klebanoff, S.J.5    Austin, T.6
  • 103
    • 0010241840 scopus 로고
    • Studies on the physiology of the white blood cell: The glycogen content of leukocytes in leukemia and polycythemia
    • Wagner R. (1947) Studies on the physiology of the white blood cell: the glycogen content of leukocytes in leukemia and polycythemia. Blood 2: 235-243
    • (1947) Blood , vol.2 , pp. 235-243
    • Wagner, R.1
  • 104
    • 0014912238 scopus 로고
    • Carbohydrate metabolism in leukocytes. XIV. Regulation of pentose cycle activity and glycogen metabolism during phagocytosis
    • Stjernholm R. L. and Manak R. C. (1970) Carbohydrate metabolism in leukocytes. XIV. Regulation of pentose cycle activity and glycogen metabolism during phagocytosis. J. Reticuloendothel. Soc. 8: 550-560
    • (1970) J. Reticuloendothel. Soc. , vol.8 , pp. 550-560
    • Stjernholm, R.L.1    Manak, R.C.2
  • 105
    • 0014962917 scopus 로고
    • Regulation of glycogen metabolism in polymorphonuclear leukocytes
    • Stossel T. P., Murad F., Mason R. J. and Vaughan M. (1970) Regulation of glycogen metabolism in polymorphonuclear leukocytes. J. Biol. Chem. 245: 6228-6234
    • (1970) J. Biol. Chem. , vol.245 , pp. 6228-6234
    • Stossel, T.P.1    Murad, F.2    Mason, R.J.3    Vaughan, M.4
  • 106
    • 0018137795 scopus 로고
    • Kinetics of oxygen consumption by phagocytosing human neutrophils
    • Segal A. W. and Coade S. B. (1978) Kinetics of oxygen consumption by phagocytosing human neutrophils. Biochem. Biophys. Res. Commun. 84: 611-617
    • (1978) Biochem. Biophys. Res. Commun. , vol.84 , pp. 611-617
    • Segal, A.W.1    Coade, S.B.2
  • 107
    • 0032741371 scopus 로고    scopus 로고
    • NADPH oxidase activation and assembly during phagocytosis
    • DeLeo F. R., Allen L. A., Apicella M. and Nauseef W. M. (1999) NADPH oxidase activation and assembly during phagocytosis. J. Immunol. 163: 6732-6740
    • (1999) J. Immunol. , vol.163 , pp. 6732-6740
    • DeLeo, F.R.1    Allen, L.A.2    Apicella, M.3    Nauseef, W.M.4
  • 108
    • 0030581632 scopus 로고    scopus 로고
    • Superoxide release and NADPH oxidase components in mature human phagocytes: Correlation between functional capacity and amount of functional proteins
    • Yagisawa M., Yuo A., Yonemaru M., Imajoh-Ohmi S., Kanegasaki S., Yazaki Y. et al. (1996) Superoxide release and NADPH oxidase components in mature human phagocytes: correlation between functional capacity and amount of functional proteins. Biochem. Biophys. Res. Commun. 228: 510-516
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 510-516
    • Yagisawa, M.1    Yuo, A.2    Yonemaru, M.3    Imajoh-Ohmi, S.4    Kanegasaki, S.5    Yazaki, Y.6
  • 109
    • 0023807754 scopus 로고
    • A time-course study on superoxide generation and protein kinase C activation in human neutrophils
    • Christiansen N. O. (1988) A time-course study on superoxide generation and protein kinase C activation in human neutrophils. FEBS Lett. 239: 195-198
    • (1988) FEBS Lett. , vol.239 , pp. 195-198
    • Christiansen, N.O.1
  • 110
    • 0021360476 scopus 로고
    • The NADPH oxidase of human polymorphonuclear leukocytes: Evidence for regulation by multiple signals
    • McPhail L. C., Clayton C. C. and Snyderman R. (1984) The NADPH oxidase of human polymorphonuclear leukocytes: evidence for regulation by multiple signals. J. Biol. Chem. 259: 5768-5775
    • (1984) J. Biol. Chem. , vol.259 , pp. 5768-5775
    • McPhail, L.C.1    Clayton, C.C.2    Snyderman, R.3
  • 111
    • 0026145193 scopus 로고
    • The effects of N-ethyl-maleimide on extracellularly and intracellularly generated chemiluminescence in neutrophils indicate that the rate of deactivation of NADPH-oxidase is higher when the oxidase system is localized on the plasma membrane than when it is localized on the phagosomal membrane
    • Dahlgren C. and Sundqvist T. (1991) The effects of N-ethyl-maleimide on extracellularly and intracellularly generated chemiluminescence in neutrophils indicate that the rate of deactivation of NADPH-oxidase is higher when the oxidase system is localized on the plasma membrane than when it is localized on the phagosomal membrane. J. Biolumin. Chemilumin. 6: 81-86
    • (1991) J. Biolumin. Chemilumin. , vol.6 , pp. 81-86
    • Dahlgren, C.1    Sundqvist, T.2
  • 112
    • 0036554122 scopus 로고    scopus 로고
    • Contribution of phospholipase D and a brefeldin A-sensitive ARF to chemoattractant-induced superoxide production and secretion of human neutrophils
    • Káldi K., Szeberényi J., Rada B. K., Kovács P., Geiszt M., Mócsai A. et al. (2002) Contribution of phospholipase D and a brefeldin A-sensitive ARF to chemoattractant-induced superoxide production and secretion of human neutrophils. J. Leukoc. Biol. 71: 695-700
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 695-700
    • Káldi, K.1    Szeberényi, J.2    Rada, B.K.3    Kovács, P.4    Geiszt, M.5    Mócsai, A.6
  • 113
    • 0020594212 scopus 로고
    • Role of cell surface contact in the kinetics of superoxide production by granulocytes
    • Dahinden C. A., Fehr J. and Hugli T. E. (1983) Role of cell surface contact in the kinetics of superoxide production by granulocytes. J. Clin. Invest. 72: 113-121
    • (1983) J. Clin. Invest. , vol.72 , pp. 113-121
    • Dahinden, C.A.1    Fehr, J.2    Hugli, T.E.3
  • 114
    • 0346690398 scopus 로고    scopus 로고
    • The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils
    • Zhao, T., Benard V., Bohl B. P. and Bokoch G. M. (2003) The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils. J. Clin. Invest. 112: 1732-1740
    • (2003) J. Clin. Invest. , vol.112 , pp. 1732-1740
    • Zhao, T.1    Benard, V.2    Bohl, B.P.3    Bokoch, G.M.4
  • 115
    • 3242775256 scopus 로고    scopus 로고
    • Responses of neutrophils to anti-integrin antibodies depends on costimulation through low affinity FcγRs: Full activation requires both integrin and nonintegrin signals
    • Jakus Z., Berton G., Ligeti E., Lowell C. A. and Mócsai A. (2004) Responses of neutrophils to anti-integrin antibodies depends on costimulation through low affinity FcγRs: full activation requires both integrin and nonintegrin signals. J. Immunol. 173: 2068-2077
    • (2004) J. Immunol. , vol.173 , pp. 2068-2077
    • Jakus, Z.1    Berton, G.2    Ligeti, E.3    Lowell, C.A.4    Mócsai, A.5
  • 116
    • 0018777296 scopus 로고
    • Fluoride-mediated activation of the respiratory burst in human neutrophils: A reversible process
    • Curnutte J. T., Babior B. M. and Karnovsky M. L. (1979) Fluoride-mediated activation of the respiratory burst in human neutrophils: a reversible process. J. Clin. Invest. 63: 637-647
    • (1979) J. Clin. Invest. , vol.63 , pp. 637-647
    • Curnutte, J.T.1    Babior, B.M.2    Karnovsky, M.L.3
  • 118
    • 0035884563 scopus 로고    scopus 로고
    • Interactions between NADPH oxidase-related proton and electron currents in human eosinophils
    • DeCoursey T. E., Cherny V. V., DeCoursey A. G., Xu W. and Thomas L. L. (2001) Interactions between NADPH oxidase-related proton and electron currents in human eosinophils. J. Physiol. 535: 767-781
    • (2001) J. Physiol. , vol.535 , pp. 767-781
    • DeCoursey, T.E.1    Cherny, V.V.2    DeCoursey, A.G.3    Xu, W.4    Thomas, L.L.5
  • 119
    • 0026744167 scopus 로고
    • Stabilization of human neutrophil NADPH oxidase activated in a cell-free system by cytosolic proteins and by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
    • Tamura M., Takeshita M., Curnutte J. T., Uhlinger D. J. and Lambeth J. D. (1992) Stabilization of human neutrophil NADPH oxidase activated in a cell-free system by cytosolic proteins and by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. J. Biol. Chem. 267: 7529-7538
    • (1992) J. Biol. Chem. , vol.267 , pp. 7529-7538
    • Tamura, M.1    Takeshita, M.2    Curnutte, J.T.3    Uhlinger, D.J.4    Lambeth, J.D.5
  • 120
    • 0033566040 scopus 로고    scopus 로고
    • The mechanism of activation of NADPH oxidase in the cell-free system: The activation process is primarily catalytic and not through the formation of a stoichiometric complex
    • Cross A. R., Erickson R. W. and Curnutte J. T. (1999) The mechanism of activation of NADPH oxidase in the cell-free system: the activation process is primarily catalytic and not through the formation of a stoichiometric complex. Biochem. J. 341: 251-255
    • (1999) Biochem. J. , vol.341 , pp. 251-255
    • Cross, A.R.1    Erickson, R.W.2    Curnutte, J.T.3
  • 121
    • 0028181632 scopus 로고
    • 2 for activation of the assembled NADPH oxidase in human neutrophils
    • 2 for activation of the assembled NADPH oxidase in human neutrophils. Biochem. J. 297: 217-223
    • (1994) Biochem. J. , vol.297 , pp. 217-223
    • Dana, R.1    Malech, H.L.2    Levy, R.3
  • 123
    • 0027918427 scopus 로고
    • Aminoacyl chloromethanes as tools to study the requirements of NADPH oxidase activation in human neutrophils
    • Chollet-Przednowed E. and Lederer F. (1993) Aminoacyl chloromethanes as tools to study the requirements of NADPH oxidase activation in human neutrophils. Eur. J. Biochem. 218: 89-93
    • (1993) Eur. J. Biochem. , vol.218 , pp. 89-93
    • Chollet-Przednowed, E.1    Lederer, F.2
  • 124
    • 0015383043 scopus 로고
    • Role of myeloperoxidase-mediated antimicrobial systems in intact leukocytes
    • Klebanoff S. J. and Hamon C. B. (1972) Role of myeloperoxidase-mediated antimicrobial systems in intact leukocytes. J. Reticuloendothel. Soc. 12: 170-196
    • (1972) J. Reticuloendothel. Soc. , vol.12 , pp. 170-196
    • Klebanoff, S.J.1    Hamon, C.B.2
  • 125
    • 0017121834 scopus 로고
    • Chemiluminescence and superoxide production by myeloperoxidase-deficient leukocytes
    • Rosen H. and Klebanoff S. J. (1976) Chemiluminescence and superoxide production by myeloperoxidase-deficient leukocytes. J. Clin. Invest. 58: 50-60
    • (1976) J. Clin. Invest. , vol.58 , pp. 50-60
    • Rosen, H.1    Klebanoff, S.J.2
  • 126
    • 0020662879 scopus 로고
    • Role of myeloperoxidase in the respiratory burst of human neutrophils
    • Nauseef W. M., Metcalf J. A. and Root R. K. (1983) Role of myeloperoxidase in the respiratory burst of human neutrophils. Blood 61: 483-492
    • (1983) Blood , vol.61 , pp. 483-492
    • Nauseef, W.M.1    Metcalf, J.A.2    Root, R.K.3
  • 127
    • 0021329788 scopus 로고
    • Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient
    • Stendahl O., Coble B. I., Dahlgren C., Hed J. and Molin L. (1984) Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient. J. Clin. Invest. 73: 366-373
    • (1984) J. Clin. Invest. , vol.73 , pp. 366-373
    • Stendahl, O.1    Coble, B.I.2    Dahlgren, C.3    Hed, J.4    Molin, L.5
  • 128
    • 0022000165 scopus 로고
    • Role of myeloperoxidase in respiratory burst of human polymorphonuclear leukocytes: Studies with myeloperoxidase-deficient subjects
    • Dri P., Soranzo M. R, Cramer R., Menegazzi R., Miotti V. and Patriarca P. (1985) Role of myeloperoxidase in respiratory burst of human polymorphonuclear leukocytes: studies with myeloperoxidase-deficient subjects. Inflammation 9: 21-31
    • (1985) Inflammation , vol.9 , pp. 21-31
    • Dri, P.1    Soranzo, M.R.2    Cramer, R.3    Menegazzi, R.4    Miotti, V.5    Patriarca, P.6
  • 129
    • 0033562347 scopus 로고    scopus 로고
    • Transient association of the nicotinamide adenine dinucleotide phosphate oxidase subunits p47phox and p67phox with phagosomes in neutrophils from patients with X-linked chronic granulomatous disease
    • Allen L. A., DeLeo F. R., Gallois A., Toyoshima S., Suzuki K. and Nauseef W. M. (1999) Transient association of the nicotinamide adenine dinucleotide phosphate oxidase subunits p47phox and p67phox with phagosomes in neutrophils from patients with X-linked chronic granulomatous disease. Blood 93: 3521-3530
    • (1999) Blood , vol.93 , pp. 3521-3530
    • Allen, L.A.1    DeLeo, F.R.2    Gallois, A.3    Toyoshima, S.4    Suzuki, K.5    Nauseef, W.M.6
  • 130
    • 0021966301 scopus 로고
    • Membrane-cytoskeleton interactions and the regulation of chemotactic peptide-induced activation of human granulocytes: The effects of dihydrocytochalasin B
    • Jesaitis A. J., Tolley J. O., Painter R. G., Sklar L. A. and Cochrane C. G. (1985) Membrane-cytoskeleton interactions and the regulation of chemotactic peptide-induced activation of human granulocytes: the effects of dihydrocytochalasin B. J. Cell. Biochem. 27: 241-253
    • (1985) J. Cell. Biochem. , vol.27 , pp. 241-253
    • Jesaitis, A.J.1    Tolley, J.O.2    Painter, R.G.3    Sklar, L.A.4    Cochrane, C.G.5
  • 131
    • 0028961115 scopus 로고
    • Chemoattractant-induced NADPH oxidase activity in human monocytes is terminated without any association of receptor-ligand complex to cytoskeleton
    • Johansson A., Särndahl E., Andersson T., Bengtsson T., Lundqvist H. and Dahlgren C. (1995) Chemoattractant-induced NADPH oxidase activity in human monocytes is terminated without any association of receptor-ligand complex to cytoskeleton. Inflammation 19: 179-191
    • (1995) Inflammation , vol.19 , pp. 179-191
    • Johansson, A.1    Särndahl, E.2    Andersson, T.3    Bengtsson, T.4    Lundqvist, H.5    Dahlgren, C.6
  • 132
    • 0030922016 scopus 로고    scopus 로고
    • Desensitization of the fMLP-induced NADPH-oxidase response in human neutrophils is lacking in okadaic acid-treated cells
    • Harbecke O., Liu L., Karlsson A. and Dahlgren C. (1997) Desensitization of the fMLP-induced NADPH-oxidase response in human neutrophils is lacking in okadaic acid-treated cells. J. Leukoc. Biol. 61: 753-758
    • (1997) J. Leukoc. Biol. , vol.61 , pp. 753-758
    • Harbecke, O.1    Liu, L.2    Karlsson, A.3    Dahlgren, C.4
  • 133
    • 0022519273 scopus 로고
    • Aberrant activation and regulation of the oxidative burst in neutrophils with Mol glycoprotein deficiency
    • Nauseef W. M., De Alarcon P., Bale J. F. and Clark R. A. (1986) Aberrant activation and regulation of the oxidative burst in neutrophils with Mol glycoprotein deficiency. J. Immunol. 137: 636-642
    • (1986) J. Immunol. , vol.137 , pp. 636-642
    • Nauseef, W.M.1    De Alarcon, P.2    Bale, J.F.3    Clark, R.A.4
  • 134
    • 0032032205 scopus 로고    scopus 로고
    • Desensitization of formyl peptide receptors is abolished in calcium ionophore-primed neutrophils: An association of the ligand-receptor complex to the cytoskeleton is not required for a rapid termination of the NADPH-oxidase response
    • Liu, L. Harbecke O., Elwing H., Follin P., Karlsson A. and Dahlgren C. (1998) Desensitization of formyl peptide receptors is abolished in calcium ionophore-primed neutrophils: an association of the ligand-receptor complex to the cytoskeleton is not required for a rapid termination of the NADPH-oxidase response. J. Immunol. 160: 2463-2468
    • (1998) J. Immunol. , vol.160 , pp. 2463-2468
    • Liu, L.1    Harbecke, O.2    Elwing, H.3    Follin, P.4    Karlsson, A.5    Dahlgren, C.6
  • 135
    • 0026577529 scopus 로고
    • Modulation of neutrophil activation by okadaic acid, a protein phosphatase inhibitor
    • Lu D. J., Takai A., Leto T. L. and Grinstein S. (1992) Modulation of neutrophil activation by okadaic acid, a protein phosphatase inhibitor. Am. J. Physiol. 262: C39-C49
    • (1992) Am. J. Physiol. , vol.262
    • Lu, D.J.1    Takai, A.2    Leto, T.L.3    Grinstein, S.4
  • 136
    • 0034235366 scopus 로고    scopus 로고
    • Deactivation of neutrophil NADPH oxidase by actin-depolymerizing agents in a cell-free system
    • Tamura M., Kanno M. and Endo Y. (2000) Deactivation of neutrophil NADPH oxidase by actin-depolymerizing agents in a cell-free system. Biochem. J. 349: 369-375
    • (2000) Biochem. J. , vol.349 , pp. 369-375
    • Tamura, M.1    Kanno, M.2    Endo, Y.3
  • 137
    • 0035017408 scopus 로고    scopus 로고
    • An intact cytoskeleton is required for prolonged respiratory burst activity during neutrophil phagocytosis
    • Granfeldt D. and Dahlgren C. (2001) An intact cytoskeleton is required for prolonged respiratory burst activity during neutrophil phagocytosis. Inflammation 25: 165-169
    • (2001) Inflammation , vol.25 , pp. 165-169
    • Granfeldt, D.1    Dahlgren, C.2
  • 138
    • 0025264449 scopus 로고
    • Continuous phosphorylation of both the 47 and the 49 kDa proteins occurs during superoxide production by neutrophils
    • Heyworth P. G. and Badwey J. A. (1990) Continuous phosphorylation of both the 47 and the 49 kDa proteins occurs during superoxide production by neutrophils. Biochim. Biophys. Acta 1052: 299-305
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 299-305
    • Heyworth, P.G.1    Badwey, J.A.2
  • 139
    • 0028321912 scopus 로고
    • Reciprocal interactions between protein kinase C and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester
    • Curnutte J. T., Erickson R. W., Ding J. and Badwey J. A. (1994) Reciprocal interactions between protein kinase C and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester. J. Biol. Chem. 269: 10813-10819
    • (1994) J. Biol. Chem. , vol.269 , pp. 10813-10819
    • Curnutte, J.T.1    Erickson, R.W.2    Ding, J.3    Badwey, J.A.4
  • 140
    • 0026774864 scopus 로고
    • Okadaic acid produces changes in phosphorylation and translocation of proteins and in intracellular calcium in human neutrophils: Relationship with the activation of the NADPH oxidase by different stimuli
    • Garcia R. C., Whitaker M., Heyworth P. G. and Segal A. W. (1992) Okadaic acid produces changes in phosphorylation and translocation of proteins and in intracellular calcium in human neutrophils: relationship with the activation of the NADPH oxidase by different stimuli. Biochem. J. 286: 687-692
    • (1992) Biochem. J. , vol.286 , pp. 687-692
    • Garcia, R.C.1    Whitaker, M.2    Heyworth, P.G.3    Segal, A.W.4
  • 141
    • 0029994065 scopus 로고    scopus 로고
    • Okadaic acid inhibits the signal responsible for activation of the NADPH-oxidase in neutrophils stimulated with serum-opsonized yeast
    • Harbecke O., Lundqvist H. and Dahlgren C. (1996) Okadaic acid inhibits the signal responsible for activation of the NADPH-oxidase in neutrophils stimulated with serum-opsonized yeast. J. Leukoc. Biol. 59: 754-762
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 754-762
    • Harbecke, O.1    Lundqvist, H.2    Dahlgren, C.3
  • 142
    • 0027957673 scopus 로고
    • Modulation of superoxide generation in in vivo lipopolysaccharide-primed Kupffer cells by staurosporine, okadaic acid, manoalide, arachidonic acid, genistein and sodium orthovanadate
    • Mayer A. M. and Spitzer J. A. (1994) Modulation of superoxide generation in in vivo lipopolysaccharide-primed Kupffer cells by staurosporine, okadaic acid, manoalide, arachidonic acid, genistein and sodium orthovanadate. J. Pharmacol. Exp. Ther. 268: 238-247
    • (1994) J. Pharmacol. Exp. Ther. , vol.268 , pp. 238-247
    • Mayer, A.M.1    Spitzer, J.A.2
  • 143
    • 0030789975 scopus 로고    scopus 로고
    • Phosphatase activity regulates superoxide anion generation and intracellular signaling in human neutrophils
    • Gay J. C., Raddassi K., Truett 3rd A. P. and Murray J. J. (1997) Phosphatase activity regulates superoxide anion generation and intracellular signaling in human neutrophils. Biochim. Biophys. Acta 1336: 243-253
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 243-253
    • Gay, J.C.1    Raddassi, K.2    Truett III, A.P.3    Murray, J.J.4
  • 144
    • 0025166531 scopus 로고
    • Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electro permeabilized human neutrophils
    • Grinstein S., Furuya W., Lu D. J. and Mills G. B. (1990) Vanadate stimulates oxygen consumption and tyrosine phosphorylation in electro permeabilized human neutrophils. J. Biol. Chem. 265: 318-327
    • (1990) J. Biol. Chem. , vol.265 , pp. 318-327
    • Grinstein, S.1    Furuya, W.2    Lu, D.J.3    Mills, G.B.4
  • 145
    • 0029018974 scopus 로고
    • Tyrosine phosphatase antagonist-induced activation of the neutrophil NADPH oxidase: A possible role for protein kinase C
    • Bennett P. A., Finan P. M., Dixon R. J. and Kellie S. (1995) Tyrosine phosphatase antagonist-induced activation of the neutrophil NADPH oxidase: a possible role for protein kinase C. Immunology 85: 304-310
    • (1995) Immunology , vol.85 , pp. 304-310
    • Bennett, P.A.1    Finan, P.M.2    Dixon, R.J.3    Kellie, S.4
  • 147
    • 0025944684 scopus 로고
    • Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1
    • Abo A., Pick E., Hall A., Totty N., Teahan C. G. and Segal A. W. (1991) Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 353: 668-670
    • (1991) Nature , vol.353 , pp. 668-670
    • Abo, A.1    Pick, E.2    Hall, A.3    Totty, N.4    Teahan, C.G.5    Segal, A.W.6
  • 148
    • 0033082165 scopus 로고    scopus 로고
    • Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense
    • Roberts A. W., Kim C., Zhen L., Lowe J. B., Kapur R., Petryniak B. et al. (1999) Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense. Immunity 10: 183-196
    • (1999) Immunity , vol.10 , pp. 183-196
    • Roberts, A.W.1    Kim, C.2    Zhen, L.3    Lowe, J.B.4    Kapur, R.5    Petryniak, B.6
  • 153
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch G. M. and Diebold B. A. (2002) Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 100: 2692-2696
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 154
    • 0035293023 scopus 로고    scopus 로고
    • Molecular basis for Rac2 regulation of phagocyte NADPH oxidase
    • Diebold B. A. and Bokoch G. M. (2001) Molecular basis for Rac2 regulation of phagocyte NADPH oxidase. Nat. Immunol. 2: 211-215
    • (2001) Nat. Immunol. , vol.2 , pp. 211-215
    • Diebold, B.A.1    Bokoch, G.M.2
  • 155
    • 0345062252 scopus 로고    scopus 로고
    • Possible role of Rac-GTPase-activating protein in the termination of superoxide production in phagocytic cells
    • Szászi K., Korda A., Wölfl J., Paclet M. H., Morel F. and Ligeti E. (1999) Possible role of Rac-GTPase-activating protein in the termination of superoxide production in phagocytic cells. Free Radic. Biol. Med. 27: 764-772
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 764-772
    • Szászi, K.1    Korda, A.2    Wölfl, J.3    Paclet, M.H.4    Morel, F.5    Ligeti, E.6
  • 156
    • 0037183494 scopus 로고    scopus 로고
    • Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase
    • Moskwa P., Dagher M. C., Paclet M. H., Morel F. and Ligeti E. (2002) Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase. Biochemistry 41: 10710-10716
    • (2002) Biochemistry , vol.41 , pp. 10710-10716
    • Moskwa, P.1    Dagher, M.C.2    Paclet, M.H.3    Morel, F.4    Ligeti, E.5
  • 157
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek K., Ahmadian M. R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F. et al. (1997) The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277: 333-338
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5    Schmitz, F.6
  • 158
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter I. R. and Wittinghofer A. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 159
    • 0037451803 scopus 로고    scopus 로고
    • GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila
    • Bernards A. (2003) GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim. Biophys. Acta 1603: 47-82
    • (2003) Biochim. Biophys. Acta , vol.1603 , pp. 47-82
    • Bernards, A.1
  • 160
    • 0035339971 scopus 로고    scopus 로고
    • Characterization of membrane-localized and cytosolic Rac-GTPase- activating proteins in human neutrophil granulocytes: Contribution to the regulation of NADPH oxidase
    • Geiszt M., Dagher M. C., Molnar G., Havasi A., Faure J., Paclet M. H. et al. (2001) Characterization of membrane-localized and cytosolic Rac-GTPase-activating proteins in human neutrophil granulocytes: contribution to the regulation of NADPH oxidase. Biochem. J. 355: 851-858
    • (2001) Biochem. J. , vol.355 , pp. 851-858
    • Geiszt, M.1    Dagher, M.C.2    Molnar, G.3    Havasi, A.4    Faure, J.5    Paclet, M.H.6
  • 162
    • 0030037238 scopus 로고    scopus 로고
    • In vitro activation of the NADPH oxidase by fluoride: Possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP)
    • Wölfl J., Dagher M. C., Fuchs A., Geiszt M. and Ligeti E. (1996) In vitro activation of the NADPH oxidase by fluoride: possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP). Eur. J. Biochem. 239: 369-375
    • (1996) Eur. J. Biochem. , vol.239 , pp. 369-375
    • Wölfl, J.1    Dagher, M.C.2    Fuchs, A.3    Geiszt, M.4    Ligeti, E.5
  • 163
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins
    • Mittal R., Ahmadian M. R., Goody R. S. and Wittinghofer A. (1996) Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science 273: 115-117
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wittinghofer, A.4
  • 164
    • 0035806898 scopus 로고    scopus 로고
    • Role of prenylation in the interaction of Rho-family small GTPases with GTPase activating proteins
    • Molnar G., Dagher M. C., Geiszt M., Settleman J. and Ligeti E. (2001) Role of prenylation in the interaction of Rho-family small GTPases with GTPase activating proteins. Biochemistry 40: 10542-10549
    • (2001) Biochemistry , vol.40 , pp. 10542-10549
    • Molnar, G.1    Dagher, M.C.2    Geiszt, M.3    Settleman, J.4    Ligeti, E.5
  • 166
    • 0030759770 scopus 로고    scopus 로고
    • Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
    • Rittinger K., Walker P. A., Eccleston J. F., Nurmahomed K., Owen D., Laue E. et al. (1997) Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature 388: 693-697
    • (1997) Nature , vol.388 , pp. 693-697
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Nurmahomed, K.4    Owen, D.5    Laue, E.6
  • 167
    • 3042796979 scopus 로고    scopus 로고
    • GAP control: Regulating the regulators of small GTPases
    • Bernards A. and Settleman J. (2004) GAP control: regulating the regulators of small GTPases. Trends Cell Biol. 14: 377-385
    • (2004) Trends Cell Biol. , vol.14 , pp. 377-385
    • Bernards, A.1    Settleman, J.2
  • 168
    • 1242272132 scopus 로고    scopus 로고
    • Phospholipids can switch the GTPase substrate preference of a GTPase-activating protein
    • Ligeti E., Dagher M. C., Hernandez S. E., Koleske A. J. and Settleman J. (2004) Phospholipids can switch the GTPase substrate preference of a GTPase-activating protein. J. Biol. Chem. 279: 5055-5058
    • (2004) J. Biol. Chem. , vol.279 , pp. 5055-5058
    • Ligeti, E.1    Dagher, M.C.2    Hernandez, S.E.3    Koleske, A.J.4    Settleman, J.5
  • 169
    • 14844325701 scopus 로고    scopus 로고
    • Autoinhibition of p50 Rho GTPase-activating protein (GAP) is released by prenylated small GTPases
    • Moskwa P., Paclet M. H., Dagher M. C. and Ligeti E. (2005) Autoinhibition of p50 Rho GTPase-activating protein (GAP) is released by prenylated small GTPases. J. Biol. Chem. 280: 6716-6720
    • (2005) J. Biol. Chem. , vol.280 , pp. 6716-6720
    • Moskwa, P.1    Paclet, M.H.2    Dagher, M.C.3    Ligeti, E.4
  • 170
    • 0035873774 scopus 로고    scopus 로고
    • 2 integrin regulation of RhoA in human neutrophils
    • 2 integrin regulation of RhoA in human neutrophils. J. Immunol. 166: 6311-6322
    • (2001) J. Immunol. , vol.166 , pp. 6311-6322
    • Dib, K.1    Melander, F.2    Andersson, T.3
  • 172
    • 5344232045 scopus 로고    scopus 로고
    • Inactivation of neutrophil NADPH oxidase upon dilution and its prevention by cross-link and fusion of phox proteins
    • Miyano K., Kitahara H., Ohmi S., Kakinuma K. and Tamura M. (2004) Inactivation of neutrophil NADPH oxidase upon dilution and its prevention by cross-link and fusion of phox proteins. Arch. Biochem. Biophys. 431: 129-137
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 129-137
    • Miyano, K.1    Kitahara, H.2    Ohmi, S.3    Kakinuma, K.4    Tamura, M.5
  • 173
    • 0035816575 scopus 로고    scopus 로고
    • phox truncations efficiently reconstitute NADPH oxidase with higher activity and stability than the individual components
    • phox truncations efficiently reconstitute NADPH oxidase with higher activity and stability than the individual components. J. Biol. Chem. 276: 24498-244505
    • (2001) J. Biol. Chem. , vol.276 , pp. 24498-244505
    • Ebisu, K.1    Nagasawa, T.2    Watanabe, K.3    Kakinuma, K.4    Miyano, K.5    Tamura, M.6
  • 175
    • 3142654859 scopus 로고    scopus 로고
    • Antagonistic cross-talk between Rac and Cdc42 GTPases regulates generation of reactive oxygen species
    • Diebold B. A., Fowler B., Lu J., Dinauer M. C. and Bokoch G. M. (2004) Antagonistic cross-talk between Rac and Cdc42 GTPases regulates generation of reactive oxygen species. J. Biol. Chem. 279: 28136-28142
    • (2004) J. Biol. Chem. , vol.279 , pp. 28136-28142
    • Diebold, B.A.1    Fowler, B.2    Lu, J.3    Dinauer, M.C.4    Bokoch, G.M.5
  • 176
    • 0035823487 scopus 로고    scopus 로고
    • 2 for stimulation of NADPH oxidase-associated diaphorase activity in granulocyte-like cells
    • 2 for stimulation of NADPH oxidase-associated diaphorase activity in granulocyte-like cells. J. Biol. Chem. 276: 33495-33503
    • (2001) J. Biol. Chem. , vol.276 , pp. 33495-33503
    • Pessach, I.1    Leto, T.L.2    Malech, H.L.3    Levy, R.4
  • 179
    • 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., Shirley P. S., Clayton C. C. and Snyderman R. (1985) Activation of the respiratory burst enzyme from human neutrophils in a cell-free system: evidence for a soluble cofactor. J. Clin. Invest. 75: 1735-1739
    • (1985) J. Clin. Invest. , vol.75 , pp. 1735-1739
    • McPhail, L.C.1    Shirley, P.S.2    Clayton, C.C.3    Snyderman, R.4
  • 180
    • 0022340824 scopus 로고
    • Activation of NADPH-dependent superoxide production in a cell-free system by sodium dodecyl sulfate
    • Bromberg Y. and Pick E. (1985) Activation of NADPH-dependent superoxide production in a cell-free system by sodium dodecyl sulfate. J. Biol. Chem. 260: 13539-13545
    • (1985) J. Biol. Chem. , vol.260 , pp. 13539-13545
    • Bromberg, Y.1    Pick, E.2
  • 183
    • 0034607649 scopus 로고    scopus 로고
    • phox to activate the phagocyte NADPH oxidase
    • phox to activate the phagocyte NADPH oxidase. J. Biol. Chem. 275: 13793-13801
    • (2000) J. Biol. Chem. , vol.275 , pp. 13793-13801
    • Shiose, A.1    Sumimoto, H.2
  • 184
    • 0029822371 scopus 로고    scopus 로고
    • - generating flavocytochrome b of neutrophils: Evidence for a transition from a low-spin state to a high-spin state of the heme iron component
    • - generating flavocytochrome b of neutrophils: evidence for a transition from a low-spin state to a high-spin state of the heme iron component. Biochemistry 35: 13400-13410
    • (1996) Biochemistry , vol.35 , pp. 13400-13410
    • Doussière, J.1    Gaillard, J.2    Vignais, P.V.3
  • 186
    • 0029842074 scopus 로고    scopus 로고
    • Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex
    • Zhan S., Vazquez N., Zhan S., Wientjes F. B., Budarf M. L., Schrock E. et al. (1996) Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex. Blood 88: 2714-2721
    • (1996) Blood , vol.88 , pp. 2714-2721
    • Zhan, S.1    Vazquez, N.2    Zhan, S.3    Wientjes, F.B.4    Budarf, M.L.5    Schrock, E.6
  • 187
    • 0037089309 scopus 로고    scopus 로고
    • Creation of a genetic system for analysis of the phagocyte respiratory burst: High-level reconstitution of the NADPH oxidase in a nonhematopoietic system
    • Price M. O., McPhail L. C., Lambeth J. D., Han C. -H., Knaus U. G. and Dinauer M. C. (2002) Creation of a genetic system for analysis of the phagocyte respiratory burst: high-level reconstitution of the NADPH oxidase in a nonhematopoietic system. Blood 99: 2653-2661
    • (2002) Blood , vol.99 , pp. 2653-2661
    • Price, M.O.1    McPhail, L.C.2    Lambeth, J.D.3    Han, C.H.4    Knaus, U.G.5    Dinauer, M.C.6
  • 189
    • 0027262939 scopus 로고
    • 558 allows reconstitution of the phagocyte NADPH oxidase solely from recombinant proteins
    • 558 allows reconstitution of the phagocyte NADPH oxidase solely from recombinant proteins. J. Biol. Chem. 268: 14256-14260
    • (1993) J. Biol. Chem. , vol.268 , pp. 14256-14260
    • Rotrosen, D.1    Yeung, C.L.2    Katkin, J.P.3
  • 190
    • 0033966545 scopus 로고    scopus 로고
    • Complementation of NADPH oxidase in p67-phox-deficient CGD patients. p67-phox/p40-phox interaction
    • Vergnaud S., Paclet M. H., Benna J. El, Pocidalo M. A. and Morel F. (2000) Complementation of NADPH oxidase in p67-phox-deficient CGD patients. p67-phox/p40-phox interaction. Eur. J. Biochem. 267: 1059-1067
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1059-1067
    • Vergnaud, S.1    Paclet, M.H.2    Benna, J.El.3    Pocidalo, M.A.4    Morel, F.5
  • 197
    • 10344246590 scopus 로고    scopus 로고
    • Reconstitution of chemotactic peptide-induced nicotinamide adenine dinucleotide phosphate (reduced) oxidase activation in transgenic COS-phox cells
    • He R., Nanamori M., Sang H., Yin H., Dinauer M. C. and Ye R. D. (2004) Reconstitution of chemotactic peptide-induced nicotinamide adenine dinucleotide phosphate (reduced) oxidase activation in transgenic COS-phox cells. J. Immunol. 173: 7462-7470
    • (2004) J. Immunol. , vol.173 , pp. 7462-7470
    • He, R.1    Nanamori, M.2    Sang, H.3    Yin, H.4    Dinauer, M.C.5    Ye, R.D.6
  • 198
    • 0015230979 scopus 로고
    • Mode of activation of granule-bound NADPH oxidase in leucocytes during phagocytosis
    • Patriarca P., Cramer R., Marussi M., Rossi F. and Romeo D. (1971) Mode of activation of granule-bound NADPH oxidase in leucocytes during phagocytosis. Biochim. Biophys. Acta 237: 335-338
    • (1971) Biochim. Biophys. Acta , vol.237 , pp. 335-338
    • Patriarca, P.1    Cramer, R.2    Marussi, M.3    Rossi, F.4    Romeo, D.5
  • 199
    • 0017249347 scopus 로고
    • Manganese-dependent NADPH oxidation by granulocyte particles: The role of superoxide and the nonphysiological nature of the manganese requirement
    • Curnutte J. T., Karnovsky M. L. and Babior B. M. (1976) Manganese-dependent NADPH oxidation by granulocyte particles: the role of superoxide and the nonphysiological nature of the manganese requirement. J. Clin. Invest. 57: 1059-1067
    • (1976) J. Clin. Invest. , vol.57 , pp. 1059-1067
    • Curnutte, J.T.1    Karnovsky, M.L.2    Babior, B.M.3
  • 200
    • 0021739838 scopus 로고
    • Oxidants from phagocytes: Agents of defense and destruction
    • Babior B. M. (1984) Oxidants from phagocytes: agents of defense and destruction. Blood 64: 959-966
    • (1984) Blood , vol.64 , pp. 959-966
    • Babior, B.M.1
  • 201
    • 0023930551 scopus 로고
    • Kinetics of activation of the respiratory burst oxidase in a fully soluble system from human neutrophils
    • Babior B. M., Kuver R. and Curnutte J. T. (1988) Kinetics of activation of the respiratory burst oxidase in a fully soluble system from human neutrophils. J. Biol. Chem. 263: 1713-1718
    • (1988) J. Biol. Chem. , vol.263 , pp. 1713-1718
    • Babior, B.M.1    Kuver, R.2    Curnutte, J.T.3
  • 202
    • 0027459487 scopus 로고
    • Arachidonic acid increases the activity of the assembled NADPH oxidase in cytoplasmic membranes and endosomes
    • Rubinek T. and Levy R. (1993) Arachidonic acid increases the activity of the assembled NADPH oxidase in cytoplasmic membranes and endosomes. Biochim. Biophys. Acta 1176: 51-58
    • (1993) Biochim. Biophys. Acta , vol.1176 , pp. 51-58
    • Rubinek, T.1    Levy, R.2
  • 203
    • 0027518061 scopus 로고
    • 558 in particulate NADPH oxidase from activated human neutrophils
    • 558 in particulate NADPH oxidase from activated human neutrophils. Biochem. Biophys. Res. Commun. 196: 543-552
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 543-552
    • Ravel, P.1    Lederer, F.2
  • 204
    • 0026033558 scopus 로고
    • Deactivation of the subcellular NADPH oxidase and its relationship to termination of the respiratory burst
    • Eklund E. A. and Gabig T. G. (1991) Deactivation of the subcellular NADPH oxidase and its relationship to termination of the respiratory burst. Biochem. Soc. Trans. 19: 51-54
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 51-54
    • Eklund, E.A.1    Gabig, T.G.2
  • 206
    • 0030688041 scopus 로고    scopus 로고
    • Polyisoprenyl phosphates in intracellular signalling
    • Levy B. D., Petasis N. A. and Serhan C. N. (1997) Polyisoprenyl phosphates in intracellular signalling. Nature 389: 985-990
    • (1997) Nature , vol.389 , pp. 985-990
    • Levy, B.D.1    Petasis, N.A.2    Serhan, C.N.3
  • 209
    • 0019394542 scopus 로고
    • --producing enzyme of human neutrophils: Further properties
    • --producing enzyme of human neutrophils: further properties. J. Biol. Chem. 256: 2321-2323
    • (1981) J. Biol. Chem. , vol.256 , pp. 2321-2323
    • Babior, B.M.1    Peters, W.A.2
  • 211
    • 13544261760 scopus 로고    scopus 로고
    • Activation of the phagocyte NADPH oxidase by Rac guanine nucleotide exchange factors in conjunction with ATP and nucleoside diphosphate kinase
    • Mizrahi A., Molshanski-Mor S., Weinbaum C., Zheng Y., Hirshberg M. and Pick E. (2005) Activation of the phagocyte NADPH oxidase by Rac guanine nucleotide exchange factors in conjunction with ATP and nucleoside diphosphate kinase. J. Biol. Chem. 280: 3802-3811
    • (2005) J. Biol. Chem. , vol.280 , pp. 3802-3811
    • Mizrahi, A.1    Molshanski-Mor, S.2    Weinbaum, C.3    Zheng, Y.4    Hirshberg, M.5    Pick, E.6
  • 214
    • 0036016543 scopus 로고    scopus 로고
    • Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components
    • Morgan D., Cherny V. V., Price M. O., Dinauer M. C. and DeCoursey T. E. (2002) Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components. J. Gen. Physiol. 119: 571-580
    • (2002) J. Gen. Physiol. , vol.119 , pp. 571-580
    • Morgan, D.1    Cherny, V.V.2    Price, M.O.3    Dinauer, M.C.4    DeCoursey, T.E.5
  • 215
    • 0019495038 scopus 로고
    • Arrangement of the respiratory burst oxidase in the plasma membrane of the neutrophil
    • Babior G. L., Rosin R. E., McMurrich B. J., Peters W. A. and Babior B. M. (1981) Arrangement of the respiratory burst oxidase in the plasma membrane of the neutrophil. J. Clin. Invest. 67: 1724-1728
    • (1981) J. Clin. Invest. , vol.67 , pp. 1724-1728
    • Babior, G.L.1    Rosin, R.E.2    McMurrich, B.J.3    Peters, W.A.4    Babior, B.M.5
  • 217
    • 0029969718 scopus 로고    scopus 로고
    • Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase
    • Finegold A. A., Shatwell K. P., Segal A. W., Klausner R. D. and Dancis A. (1996) Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase. J. Biol. Chem. 271: 31021-31024
    • (1996) J. Biol. Chem. , vol.271 , pp. 31021-31024
    • Finegold, A.A.1    Shatwell, K.P.2    Segal, A.W.3    Klausner, R.D.4    Dancis, A.5
  • 218
    • 0025913125 scopus 로고
    • 1 complex from Rhodobacter sphaeroides by site-directed mutagenesis
    • 1 complex from Rhodobacter sphaeroides by site-directed mutagenesis. Biochemistry 30: 6747-6754
    • (1991) Biochemistry , vol.30 , pp. 6747-6754
    • Yun, C.H.1    Crofts, A.R.2    Gennis, R.B.3
  • 222
    • 0021920513 scopus 로고
    • 2 is necessary for the fast reduction of cytochrome b-245 by NADPH
    • 2 is necessary for the fast reduction of cytochrome b-245 by NADPH. Biochem. J. 226: 881-884
    • (1985) Biochem. J. , vol.226 , pp. 881-884
    • Cross, A.R.1    Parkinson, J.F.2    Jones, O.T.G.3
  • 223
    • 0030947231 scopus 로고    scopus 로고
    • Electron transfer in the superoxide-generating NADPH oxidase complex reconstituted in vitro
    • Koshkin V., Lotan O. and Pick E. (1997) Electron transfer in the superoxide-generating NADPH oxidase complex reconstituted in vitro. Biochim. Biophys. Acta 1319: 139-146
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 139-146
    • Koshkin, V.1    Lotan, O.2    Pick, E.3
  • 225
    • 0019802590 scopus 로고
    • Cis-polyunsaturated fatty acids induce high levels of superoxide production by human neutrophils
    • Badwey J. A., Curnutte J. T. and Karnovsky M. L. (1981) cis-polyunsaturated fatty acids induce high levels of superoxide production by human neutrophils. J. Biol. Chem. 256: 12640-12643
    • (1981) J. Biol. Chem. , vol.256 , pp. 12640-12643
    • Badwey, J.A.1    Curnutte, J.T.2    Karnovsky, M.L.3
  • 226
    • 0025085584 scopus 로고
    • Noncytotoxic activation of neutrophils by eosinophil granule major basic protein: Effect on superoxide anion generation and lysosomal enzyme release
    • Moy J. N., Gleich G. J. and Thomas L. L. (1990) Noncytotoxic activation of neutrophils by eosinophil granule major basic protein: effect on superoxide anion generation and lysosomal enzyme release. J. Immunol. 145: 2626-2632
    • (1990) J. Immunol. , vol.145 , pp. 2626-2632
    • Moy, J.N.1    Gleich, G.J.2    Thomas, L.L.3
  • 227
    • 0019844782 scopus 로고
    • Opsonized zymosan-stimulated granulocytes-activation and activity of the superoxide-generating system and membrane potential changes
    • Cohen H. J., Newburger P. E., Chovaniec M. E., Whitin J. C. and Simons E. R. (1981) Opsonized zymosan-stimulated granulocytes-activation and activity of the superoxide-generating system and membrane potential changes. Blood 58: 975-982
    • (1981) Blood , vol.58 , pp. 975-982
    • Cohen, H.J.1    Newburger, P.E.2    Chovaniec, M.E.3    Whitin, J.C.4    Simons, E.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.