The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism

Cellular and Molecular Life Sciences

Volumn 59, Issue 9, 2002, Pages 1428-1459

  Vignais, P V ^a  

^a CEA GRENOBLE   (France)

Author keywords

Neutrophil flavocytochrome b; NOX protein; Phagocyte oxidase; Respiratory burst; Superoxide anion

Indexed keywords

CELL PROTEIN; FLAVINE ADENINE NUCLEOTIDE; GLYCOPROTEIN; GLYCOPROTEIN GP 91; HYDROCHLORIC ACID; HYDROGEN PEROXIDE; LACTATE DEHYDROGENASE (CYTOCHROME); OXIDOREDUCTASE; OXYGEN; PROTEIN DUOX; PROTEIN NOX; PROTEIN P22; PROTEIN P40; PROTEIN P40PHOX; PROTEIN P47; PROTEIN P47PHOX; PROTEIN P67; PROTEIN P67PHOX; PROTEIN SUBUNIT; PROTON; RAC PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; UNCLASSIFIED DRUG;

BINDING SITE; CATALYSIS; CHRONIC GRANULOMATOUS DISEASE; CYTOSOL; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; GENETIC DISORDER; HUMAN; HUMAN CELL; OXYGEN TRANSPORT; PHAGOCYTOSIS; PROTEIN STRUCTURE; PROTON TRANSPORT; REDUCTION; RESPIRATORY BURST; REVIEW; SIGNAL TRANSDUCTION; SOLUBILITY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYTOCHROME B GROUP; ELECTRON TRANSPORT; ENZYME ACTIVATION; HUMANS; MOLECULAR SEQUENCE DATA; NADPH OXIDASE; NEUTROPHILS; PHOSPHOPROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RAC GTP-BINDING PROTEINS; RAP1 GTP-BINDING PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUPEROXIDES;

EID: 0036710445     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-002-8520-9     Document Type: Review

References (328)

1. Cross A. R., Parkinson J. E and Jones O. T. (1984) The superoxide-generating oxidase of leucocytes: NADPH-dependent reduction of flavin and cytochrome b in solubilized preparations. Biochem. J. 223: 337-344
2. Wood P. M. (1987) The two redox potentials for oxygen reduction to superoxide. Trends Biochem. Sci. 12: 250-251
3. Kakinuma K., Kaneda M., Chiba T. and Ohnishi T. (1986) Electron spin resonance studies on a flavoprotein in neutrophil plasma membranes: Redox potentials of the flavin and its participation in NADPH oxidase. J. Biol. Chem. 261: 9426-9432
4. Abo A., Boyhan A., West I., Thrasher A. J. and Segal A. W. (1992) Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by four components: p67-phox, p47-phox, p21rac1, and cytochrome b-245. J. Biol. Chem. 267: 16767-16770
5. Wientjes F. B., Hsuan J. J., Totty N. F. and Segal A. W. (1993) p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem. J. 296: 557-561
6. Sathyamoorthy M., Mendez I. de, Adams A. G. and Leto T. L. (1997) p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain. J. Biol. Chem. 272: 9141-9146
7. Cross A. R. (2000) p40(phox) participates in the activation of NADPH oxidase by increasing the affinity of p47(phox) for flavocytochrome b(558). Biochem. J. 349: 113-117
8. Weiss J., De Leo F. and Nauseef W. M. (2002) Antimicrobial activity of host cells. In: Methods in Microbiology, vol. 31, pp. 477-505, Sansonetti P. and Zychlinsky A. (eds), Academic Press, San Diego
9. Thrasher A. J., Keep N. H., Wientjes F. and Segal A. W. (1994) Chronic granulomatous disease. Biochim. Biophys. Acta. 1227: 1-24
10. Ambruso D. R., Knall C., Abell A. N., Panepinto J., Kurkchubasche A., Thurman G. et al. (2000) Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc. Natl. Acad. Sci. USA 97: 4654-4659
11. Williams D. A., Tao W., Yang F., Kim C., Gu Y., Mansfield P. et al. (2000) Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency. Blood 96: 1646-1654
12. Royer-Pokora B., Kunkel L. M., Monaco A. P., Goff S. C., Newburger P. E., Baehner R. L. et al. (1986) Cloning the gene for an inherited human disorder - Chronic granulomatous disease - On the basis of its chromosomal location. Nature 322: 32-38
13. Teahan C., Rowe P., Parker P., Totty N. and Segal A. W. (1987) The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome b-245. Nature 327: 720-721
14. Parkos C. A., Allen R. A., Cochrane C. G. and Jesaitis A. J. (1987) Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000. J. Clin. Invest. 80: 732-742
15. Segal A. W. and Jones O. T. (1978) Novel cytochrome b system in phagocytic vacuoles of human granulocytes. Nature 276: 515-517
16. Cross A. R., Jones O. T., Harper A. M. and Segal A. W. (1981) Oxidation-reduction properties of the cytochrome b found in the plasma-membrane fraction of human neutrophils: A possible oxidase in the respiratory burst. Biochem. J. 194: 599-606
17. Cross A. R., Curnutte J. T., Rae J. and Heyworth P. G. (1996) Hematologically important mutations: X-linked chronic granulomatous disease. Blood Cells Mol. Dis. 22: 90-95
18. Roos D., Boer M. de, Kuribayashi F., Meischl C., Weening R. S., Segal A. W. et al. (1996) Mutations in the X-linked and autosomal recessive forms of chronic granulomatous disease. Blood 87: 1663-1681
19. Roesler J., Curnutte J. T., Rae J., Barrett D., Patino P., Chanock S. J. et al. (2000) Recombination events between the p47-phox gene and its highly homologous pseudogenes are the main cause of autosomal recessive chronic granulomatous disease. Blood 95: 2150-2156
20. Volkman D. J., Buescher E. S., Gallin J. I. and Fauci A. S. (1984) B cell lines as models for inherited phagocytic diseases: Abnormal superoxide generation in chronic granulomatous disease and giant granules in Chediak-Higashi syndrome. J. Immunol. 133: 3006-3009
21. --generating oxidase of B lymphocytes: Epstein-Barr virus-immortalized B lymphocytes as a tool for the identification of defective components of the oxidase in chronic granulomatous disease. Biochim. Biophys. Acta. 1182: 101-109
22. Bjorgvinsdottir H., Ding C., Pech N., Gifford M. A., Li L. L. and Dinauer M. C. (1997) Retroviral-mediated gene transfer of gp91phox into bone marrow cells rescues defect in host defense against Aspergillus fumigatus in murine X-linked chronic granulomatous disease. Blood 89: 41-48
23. Dinauer M. C., Li L. L., Bjorgvinsdottir H., Ding C. and Pech N. (1999) Long-term correction of phagocyte NADPH oxidase activity by retroviral-mediated gene transfer in murine X-linked chronic granulomatous disease. Blood 94: 914-922
24. Mardiney M. 3rd, Jackson S. H., Spratt S. K., Li F., Holland S. M. and Malech H. L. (1997) Enhanced host defense after gene transfer in the murine p47phox-deficient model of chronic granulomatous disease. Blood 89: 2268-2275
25. Cavazzana-Calvo M. and Hacein-Bey-Abina S. (2001) Correction of genetic blood defects by gene transfer. Curr. Opin. Hematol. 8: 360-367
26. Bromberg Y. and Pick E. (1984) Unsaturated fatty acids stimulate NADPH-dependent superoxide production by cell-free system derived from macrophages. Cell. Immunol. 88: 213-221
27. Khwaja A., Carver J. E. and Linch D. C. (1992) Interactions of granulocyte-macrophage colony-stimulating factor (CSF), granulocyte CSF, and tumor necrosis factor alpha in the priming of the neutrophil respiratory burst. Blood 79: 745-753
28. Kodama T., Hazeki K., Hazeki O., Okada T. and Ui M. (1999) Enhancement of chemotactic peptide-induced activation of phosphoinositide 3-kinase by granulocyte-macrophage colony-stimulating factor and its relation to the cytokine-mediated priming of neutrophil superoxide-anion production. Biochem. J. 337: 201-209
29. Boulay F., Tardif M., Brouchon L. and Vignais P. (1990) Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA. Biochem. Biophys. Res. Commun. 168: 1103-1109
30. Boulay F., Tardif M., Brouchon L. and Vignais P. (1990) The human N-formylpeptide receptor: Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors. Biochemistry 29: 11123-11133
31. Ye R. D. and Boulay F. (1997) Structure and function of leukocyte chemoattractant receptors. Adv. Pharmacol. 39: 221-289
32. Berton G. (1999) Tyrosine kinases in neutrophils. Curr. Opin. Hematol. 6: 51-58
33. Greenberg S. (1999) Modular components of phagocytosis. J. Leukoc. Biol. 66: 712-717
34. Kwiatkowska K. and Sobota A. (1999) Signaling pathways in phagocytosis. Bioessays 21: 422-431
35. Greenberg S. and Grinstein S. (2002) Phagocytosis and innate immunity. Curr. Opin. Immunol. 14: 136-145
36. 2 and lactoferrin release in adherent human neutrophils. J. Biol. Chem. 269: 8063-8068
37. Exton J. H. (1999) Regulation ofphospholipase D. Biochim. Biophys. Acta. 1439: 121-133
38. Gillooly D. J., Simonsen A. and Stenmark H. (2001) Phosphoinositides and phagocytosis. J. Cell Biol. 155: 15-17
39. Marshall J. G., Booth J. W., Stambolic V., Mak T., Balla T., Schreiber A. D. et al. (2001) Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis. J. Cell Biol. 153: 1369-1380
40. Vieira O. V., Botelho R. J., Rameh L., Brachmann S. M., Matsuo T., Davidson H. W. et al. (2001) Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation. J. Cell Biol. 155: 19-25
41. Ellson C. D., Anderson K. E., Morgan G., Chilvers E. R., Lipp P., Stephens L. R. et al. (2001) Phosphatidylinositol 3-phosphate is generated in phagosomal membranes. Curr. Biol. 11: 1631-1635
42. Mansfield P. J., Hinkovska-Galcheva V., Carey S. S., Shayman J. A. and Boxer L. A. (2002) Regulation of polymorphonuclear leukocyte degranulation and oxidant production by ceramide through inhibition of phospholipase D. Blood 99: 1434-1441
43. + flux. Nature 416: 291-297
44. Maly F. E., Cross A. R., Jones O. T., Wolf-Vorbeck G., Walker C., Dahinden C. A. et al. (1988) The superoxide generating system of B cell lines: Structural homology with the phagocytic oxidase and triggering via surface Ig. J. Immunol. 140: 2334-2339
45. Maly F. E., Nakamura M., Gauchat J. F., Urwyler A., Walker C., Dahinden C. A. et al. (1989) Superoxide-dependent nitroblue tetrazolium reduction and expression of cytochrome b-245 components by human tonsillar B lymphocytes and B cell lines. J. Immunol. 142: 1260-1267
46. Meier B., Jesaitis A. J., Emmendorffer A., Roesler J. and Quinn M. T. (1993) The cytochrome b-558 molecules involved in the fibroblast and polymorphonuclear leucocyte superoxide-generating NADPH oxidase systems are structurally and genetically distinct. Biochem. J. 289: 481-486
47. Ushio-Fukai M., Zafari A. M., Fukui T., Ishizaka N. and Griendling K. K. (1996) p22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells. J. Biol. Chem. 271: 23317-23321
48. Meyer J. W., Holland J. A., Ziegler L. M., Chang M. M., Beebe G. and Schmitt M. E. (1999) Identification of a functional leukocyte-type NADPH oxidase in human endothelial cells: A potential atherogenic source of reactive oxygen species. Endothelium 7: 11-22
49. Bayraktutan U., Blayney L. and Shah A. M. (2000) Molecular characterization and localization of the NAD(P)H oxidase components gp91-phox and p22-phox in endothelial cells. Arterioscler Thromb. Vasc. Biol. 20: 1903-1911
50. 2 sensor protein in the rat carotid body. Biochem. J. 272: 743-747
51. Youngson C., Nurse C., Yeger H. and Cutz E. (1993) Oxygen sensing in airway chemoreceptors. Nature 365: 153-155
52. + current modulation in wild-type and oxidase-deficient mice. Proc. Natl. Acad. Sci. USA 97: 4374-4379
53. Cui X. L. and Douglas J. G. (1997) Arachidonic acid activates c-jun N-terminal kinase through NADPH oxidase in rabbit proximal tubular epithelial cells. Proc. Natl. Acad. Sci. USA 94: 3771-3776
54. Radeke H. H., Cross A. R., Hancock J. T., Jones O. T., Nakamura M., Kaever V. et al. (1991) Functional expression of NADPH oxidase components (alpha- and beta-subunits of cytochrome b558 and 45-kDa flavoprotein) by intrinsic human glomerular mesangial cells. J. Biol. Chem. 266: 21025-21029
55. Tenhaken R., Levine A., Brisson L. F., Dixon R. A. and Lamb C. (1995) Function of the oxidative burst in hypersensitive disease resistance. Proc. Natl. Acad. Sci. USA 92: 4158-4163
56. Dwyer S. C., Legendre L., Low P. S. and Leto T. L. (1996) Plant and human neutrophil oxidative burst complexes contain immunologically related proteins. Biochim. Biophys. Acta 1289: 231-237
57. 2- binding motifs. Plant Cell 10: 255-266
58. Lamb C. and Dixon R. A. (1997) The oxidative burst in plant disease resistance. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48: 251-275
59. Lambeth J. D., Cheng G., Arnold R. S. and Edens W. A. (2000) Novel homologs of gp91phox. Trends Biochem. Sci. 25: 459-461
60. Lambeth J. D. (2002) Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr. Opin. Hematol. 9: 11-17
61. Morel F., Doussiere J. and Vignais P. V. (1991) The superoxide-generating oxidase of phagocytic cells: Physiological, molecular and pathological aspects. Eur. J. Biochem. 201: 523-546
62. Babior B. M. (1992) The respiratory burst oxidase. Adv. Enzymol. Relat. Areas Mol. Biol. 65: 49-95
63. Dinauer M. C. (1993) The respiratory burst oxidase and the molecular genetics of chronic granulomatous disease. Crit. Rev. Clin. Lab. Sci. 30: 329-369
64. Segal A. W. (1993) Structure of the NADPH-oxidase: Membrane components. Immunodeficiency 4: 167-179
65. Jesaitis A. J. (1995) Structure of human phagocyte cytochrome b and its relationship to microbicidal superoxide production. J. Immunol. 155: 3286-3288
66. Robinson J. M. and Badwey J. A. (1995) The NADPH oxidase complex of phagocytic leukocytes: A biochemical and cytochemical view. Histochem. Cell. Biol. 103: 163-180
67. Henderson L. M. and Chappel J. B. (1996) NADPH oxidase of neutrophils. Biochim. Biophys. Acta. 1273: 87-107
68. De Leo F. R. and Quinn M. T. (1996) Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins. J. Leukoc. Biol. 60: 677-691
69. Babior B. M. (1999) NADPH oxidase: An update. Blood 93: 1464-1476
70. Clark R. A. (1999) Activation of the neutrophil respiratory burst oxidase. J. Infect. Dis. 179: S309-S317
71. Borregaard N., Heiple J. M., Simons E. R. and Clark R. A. (1983) Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: Translocation during activation. J. Cell Biol. 97: 52-61
72. Morel E, Doussiere J., Stasia M. J. and Vignais P. V. (1985) The respiratory burst of bovine neutrophils: Role of a b type cytochrome and coenzyme specificity. Eur. J. Biochem. 152: 669-679
73. Kobayashi T., Robinson J. M. and Seguchi H. (1998) Identification of intracellular sites of superoxide production in stimulated neutrophils. J. Cell Sci. 111: 81-91
74. Johansson A., Jesaitis A. J., Lundqvist H., Magnusson K. E., Sjolin C., Karlsson A. et al. (1995) Different subcellular localization of cytochrome b and the dormant NADPH-oxidase in neutrophils and macrophages: Effect on the production of reactive oxygen species during phagocytosis. Cell Immunol. 161: 61-71
75. Roberts P. J., Cross A. R., Jones O. T. and Segal A. W. (1982) Development of cytochrome b and an active oxidase system in association with maturation of a human promyelocytic (HL60) cell line. J. Cell Biol. 95: 720-726
76. Hancock J. T., Maly F. E. and Jones O. T. G. (1989) Properties of the superoxide-generating oxidase of B-lymphocyte cell lines. Biochem. J. 262: 373-375
77. Cohen-Tanugi L., Morel F., Pilloud-Dagher M. C., Seigneurin J. M., Francois P., Bost M. et al. (1991) Activation of O2(-)generating oxidase in an heterologous cell-free system derived from Epstein-Barr-virus-transformed human B lymphocytes and bovine neutrophils: Application to the study of defects in cytosolic factors in chronic granulomatous disease. Eur. J. Biochem. 202: 649-655
78. Kleinberg M. E., Rotrosen D. and Malech H. L. (1989) Asparagine-linked glycosylation of cytochrome b558 large subunit varies in different human phagocytic cells. J. Immunol. 143: 4152-4157
79. Orkin S. H. (1987) X-linked chronic granulomatous disease: From chromosomal position to the in vivo gene product. Trends Genet. 3: 149-151
80. Orkin S. H. (1989) Molecular genetics of chronic granulomatous disease. Annu. Rev. Immunol. 7: 277-307
81. Hossle J. P., Berthet F., Erny C. and Seger R. A. (1993) Molecular genetic analysis of phagocyte oxidase cytochrome b558 mutations leading to chronic granulomatous disease. Immunodeficiency 4: 303-306
82. Davis A. R., Mascolo P. L., Bunger P. L., Sipes K. M. and Quinn M. T. (1998) Cloning and sequencing of the bovine flavocytochrome b subunit proteins, gp91-phox and p22phox: Comparison with other known flavocytochrome b sequences. J. Leukoc. Biol. 64: 114-123
83. Huang J., Hitt N. D. and Kleinberg M. E. (1995) Stoichiometry of p22-phox and gp91-phox in phagocyte cytochrome b558. Biochemistry 34: 16753-16757
84. Quinn M. T., Mullen M. L. and Jesaitis A. J. (1992) Human neutrophil cytochrome b contains multiple hemes: Evidence for heme associated with both subunits. J. Biol. Chem. 267: 7303-7309
85. Cross A. R., Rae J. and Curnutte J. T. (1995) Cytochrome b245 of the neutrophil superoxide-generating system contains two nonidentical hemes: Potentiometric studies of a mutant form of gp91phox. J. Biol. Chem. 270: 17075-17077
86. Yu L., Quinn M. T., Cross A. R. and Dinauer M. C. (1998) Gp91(phox) is the heme binding subunit of the superoxidegenerating NADPH oxidase. Proc. Natl. Acad. Sci. USA 95: 7993-7998
87. Babior B. M. and Kipnes R. S. (1977) Superoxide-forming enzyme from human neutrophils: Evidence for a flavin requirement. Blood 50: 517-524
88. 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
89. Sumimoto H., Sakamoto N., Nozaki M., Sakaki Y., Takeshige K. and Minakami S. (1992) Cytochrome b558, a component of the phagocyte NADPH oxidase, is a flavoprotein. Biochem. Biophys. Res. Commun. 186: 1368-1375
90. Rotrosen D., Yeung C. L., Leto T. L., Malech H. L. and Kwong C. H. (1992) Cytochrome b558: The flavin-binding component of the phagocyte NADPH oxidase. Science 256: 1459-1462
91. Escriou V., Laporte F. and Vignais P. V. (1996) Assessment of the flavoprotein nature of the redox core of neutrophil NADPH oxidase. Biochem. Biophys. Res. Commun. 219: 930-935
92. Koshkin V. and Pick E. (1993) Generation of superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators. FEBS Lett. 327: 57-62
93. Koshkin V. and Pick E. (1994) Superoxide production by cytochrome b559: Mechanism of cytosol-independent activation. FEBS Lett. 338: 285-289
94. Nisimoto Y., Otsuka-Murakami H. and Lambeth D. J. (1995) Reconstitution of flavin-depleted neutrophil flavocytochrome b558 with 8-mercapto-FAD and characterization of the flavinreconstituted enzyme. J. Biol. Chem. 270: 16428-16434
95. Doussiere J., Buzenet G. and Vignais P. V. (1995) Photoaffinity labeling and photoinactivation of the O2(-)-generating oxidase of neutrophils by an azido derivative of FAD. Biochemistry 34: 1760-1770
96. Segal A. W., West I., Wientjes F., Nugent J. H., Chavan A. J., Haley B. et al. (1992) Cytochrome b-245 is a flavocytochrome containing FAD and the NADPH-binding site of the microbicidal oxidase of phagocytes. Biochem. J. 284: 781-788
97. 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
98. Rotrosen D., Kleinberg M. E., Nunoi H., Leto T., Gallin J. I. and Malech H. L. (1990) Evidence for a functional cytoplasmic domain of phagocyte oxidase cytochrome b558. J. Biol. Chem. 265: 8745-8750
99. Nakanishi A., Imajoh-Ohmi S., Fujinawa T., Kikuchi H. and Kanegasaki S. (1992) Direct evidence for interaction between COOH-terminal regions of cytochrome b558 subunits and cytosolic 47-kDa protein during activation of an O(2-)-generating system in neutrophils. J. Biol. Chem. 267: 19072-19074
100. Imajoh-Ohmi S., Tokita K., Ochiai H., Nakamura M. and Kanegasaki S. (1992) Topology of cytochrome b558 in neutrophil membrane analyzed by anti-peptide antibodies and proteolysis. J. Biol. Chem. 267: 180-184
101. De Leo F. R., Yu L., Burritt J. B., Loetterle L. R., Bond C. W., Jesaitis A. J. et al. (1995) Mapping sites of interaction of p47phox and flavocytochrome b with random-sequence peptide phage display libraries. Proc. Natl. Acad. Sci. USA 92: 7110-7114
102. Burritt J. B., Quinn M. T., Jutila M. A., Bond C. W. and Jesaitis A. J. (1995) Topological mapping of neutrophil cytochrome b epitopes with phage-display libraries. J. Biol. Chem. 270: 16974-16980
103. Burritt J. B., Busse S. C., Gizachew D., Siemsen D. W., Quinn M. T., Bond C. W. et al. (1998) Antibody imprint of a membrane protein surface. Phagocyte flavocytochrome b. J. Biol. Chem. 273: 24847-24852
104. Burritt J. B., DeLeo F. R., McDonald C. L., Prigge J. R., Dinauer M. C., Nakamura M. et al. (2001) Phage display epitope mapping of human neutrophil flavocytochrome b558: Identification of two juxtaposed extracellular domains. J. Biol. Chem. 276: 2053-2061
105. Paclet M. H., Coleman A. W., Vergnaud S. and Morel F. (2000) P67-phox-mediated NADPH oxidase assembly: Imaging of cytochrome b558 liposomes by atomic force microscopy. Biochemistry 39: 9302-9310
106. Doussiere J., Brandolin G., Derrien V. and Vignais P. V. (1993) Critical assessment of the presence of an NADPH binding site on neutrophil cytochrome b558 by photoaffinity and immunochemical labeling. Biochemistry 32: 8880-8887
107. Ravel P. and Lederer F. (1991) Inactivation of NADPH oxidase from human neutrophils by affinity labeling with pyridoxal 5′-diphospho-5′-adenosine. Biochem. Biophys. Res. Commun. 181: 1259-1265
108. Ravel P. and Lederer F. (1993) Affinity-labeling of an NADPH-binding site on the heavy subunit of flavocytochrome b558 in particulate NADPH oxidase from activated human neutrophils. Biochem. Biophys. Res. Commun. 196: 543-552
109. + reductase: Prototype for a structurally novel flavoenzyme family. Science 251: 60-66
110. Bjorgvinsdottir H., Zhen L. and Dinauer M. C. (1996) Cloning of murine gp91phox cDNA and functional expression in a human X-linked chronic granulomatous disease cell line. Blood 87: 2005-2010
111. Yoshida L. S., Saruta F., Yoshikawa K., Tatsuzawa O. and Tsunawaki S. (1998) Mutation at histidine 338 of gp91(phox) depletes FAD and affects expression of cytochrome b558 of the human NADPH oxidase. J. Biol. Chem. 273: 27879-27886
112. Taylor W. R., Jones D. T. and Segal A. W. (1993) A structural model for the nucleotide binding domains of the flavocytochrome b-245 beta-chain. Protein Sci. 2: 1675-1685
113. 2-terminal regions of gp91(phox) and p22(phox). J. Biol. Chem. 276: 38852-38861
114. FinegoldA. 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
115. Shatwell K. P., Dancis A., Cross A. R., Klausner R. D. and Segal A. W. (1996) The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase. J. Biol. Chem. 271: 14240-14244
116. Biberstine-Kinkade K. J., DeLeo F. R., Epstein R. I., LeRoy B. A., Nauseef W. M. and Dinauer M. C. (2001) Heme-ligating histidines in flavocytochrome b(558): Identification of specific histidines in gp91(phox). J. Biol. Chem. 276: 31105-31112
117. Dinauer M. C., Pierce E. A., Bruns G. A., Curnutte, J. T. and Orkin S. H. (1990) Human neutrophil cytochrome b light chain (p22-phox): Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. J. Clin. Invest. 86: 1729-1737
118. Harper A. M., Chaplin M. F. and Segal A. W. (1985) Cytochrome b-245 from human neutrophils is a glycoprotein. Biochem. J. 227: 783-788
119. Wallach T. M. and Segal A. W. (1997) Analysis of glycosylation sites on gp91phox, the flavocytochrome of the NADPH oxidase, by site-directed mutagenesis and translation in vitro. Biochem. J. 321: 583-585
120. Gauss K. A., Mascolo P. L., Siemsen D. W., Nelson L. K., Bunger P. L., Pagano P. J. et al. (2002) Cloning and sequencing of rabbit leukocyte NADPH oxidase genes reveals a unique p67(phox) homolog. J. Leukoc. Biol. 71: 319-328
121. Paclet M. H., Coleman A. W., Burritt J. and Morel F. (2001) NADPH oxidase of Epstein-Barr-virus immortalized B lymphocytes: Effect of cytochrome b(558) glycosylation. Eur. J. Biochem. 268: 5197-5208
122. Regier D. S., Greene D. G., Sergeant S., Jesaitis A. J. and McPhail L. C. (2000) Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms: Correlation of NADPH oxidase activity and p22phox phosphorylation. J. Biol. Chem. 275: 28406-28412
123. Quinn M. T., Mullen M. L., Jesaitis A. J. and Linner J. G. (1992) Subcellular distribution of the Rap1A protein in human neutrophils: Colocalization and cotranslocation with cytochrome b559. Blood 79: 1563-1573
124. Maridonneau-Parini I. and Gunzburg J. de (1992) Association of rap1 and rap2 proteins with the specific granules of human neutrophils: Translocation to the plasma membrane during cell activation. J. Biol. Chem. 267: 6396-6402
125. Quinn M. T., Parkos C. A., Walker L., Orkin S. H., Dinauer M. C. and Jesaitis A. J. (1989) Association of a Ras-related protein with cytochrome b of human neutrophils. Nature 342: 198-200
126. Quilliam L. A., Mueller H., Bohl B. P., Prossnitz V., Sklar L. A., Der C. J. et al. (1991) Rap1A is a substrate for cyclic AMPdependent protein kinase in human neutrophils. J. Immunol. 147:3 1628-1635
127. Bokoch G. M., Quilliam L. A., Bohl B. P., Jesaitis A. J. and Quinn M. T. (1991) Inhibition of Rap1A binding to cytochrome b558 of NADPH oxidase by phosphorylation of Rap1A. Science 254: 1794-1796
128. Eklund E. A., Marshall M., Gibbs J. B., Crean C. D. and Gabig T. G. (1991) Resolution of a low molecular weight G protein in neutrophil cytosol required for NADPH oxidase activation and reconstitution by recombinant Krev-1 protein. J. Biol. Chem. 266: 13964-13970
129. Bokoch G. M. (1994) Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins. Curr. Opin. Cell Biol. 6: 212-218
130. Labadia M. E., Bokoch G. M. and Huang C. K. (1993) The Rap1A protein enhances protein kinase C activity in vitro. Biochem. Biophys. Res. Commun. 195: 1321-1328
131. Maly F. E., Quilliam L. A., Dorseuil O., Der C. J. and Bokoch G. M. (1994) Activated or dominant inhibitory mutants of Rap1A decrease the oxidative burst of Epstein-Barr virus-transformed human B lymphocytes. J. Biol. Chem. 269: 18743-18746
132. Gabig T. G., Crean C. D., Mantel P. L. and Rosli R. (1995) Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated HL60 cell NADPH oxidase activation. Blood 85: 804-811
133. Balch W. E. (1990) Small GTP-binding proteins in vesicular transport. Trends Biochem. Sci. 15: 473-477
134. M'Rabet L., Coffer P., Zwartkruis E, Franke B., Segal A. W., Koenderman L. et al. (1998) Activation of the small GTPase rap 1 in human neutrophils. Blood 92: 2133-2140
135. Ren R., Mayer B. J., Cicchetti P. and Baltimore D. (1993) Identification of a ten-amino acid proline-rich SH3 binding site. Science 259: 1157-1161
136. Hiroaki H., Ago T., Ito T., Sumimoto H. and Kohda D. (2001) Solution structure of the PX domain, a target of the SH3 domain. Nat. Struct. Biol. 8: 526-530
137. Ellson C. D., Andrews S., Stephens L. R. and Hawkins P. T. (2002) The PX domain: A new phosphoinositide-binding module. J. Cell Sci. 115: 1099-1105
138. Kanai F., Liu H., Field S. J., Akbary H., Matsuo T., Brown G. E. et al. (2001) The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nat. Cell Biol. 3: 675-678
139. Zhan Y., Virbasius J. V., Song X., Pomerleau D. P. and Zhou G. W. (2001) The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides. J. Biol. Chem. 277: 4512-4518
140. Wishart M. J., Taylor G. S. and Dixon J. E. (2001) Phoxy lipids: Revealing PX domains as phosphoinositide binding modules. Cell 105: 817-820
141. Noack D., Rae J., Cross A. R., Ellis B. A., Newburger P. E., Curnutte J. T. et al. (2001) Autosomal recessive chronic granulomatous disease caused by defects in NCF-1, the gene encoding the phagocyte p47-phox: Mutations not arising in the NCF-1 pseudogenes. Blood 97: 305-311
142. Heyworth P. G. and Cross A. R. (2002) Chronic granulomatous disease mutations and the PX domain. Nat. Cell Biol. 4: E110
143. 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
144. El Benna J., Faust L. P. and Babior B. M. (1994) The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation: Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J. Biol. Chem. 269: 23431-23436
145. Mendez I. de, Adams A. G., Sokolic R. A., Malech H. L. and Leto T. L. (1996) Multiple SH3 domain interactions regulate NADPH oxidase assembly in whole cells. EMBO J. 15: 1211-1220
146. Mendez I. de, Homayounpour N. and Leto T. L. (1997) Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation. Mol. Cell. Biol. 17: 2177-2185
147. Sumimoto H., Hata K., Mizuki K., Ito T., KageY., SakakiY. et al. (1996) Assembly and activation of the phagocyte NADPH oxidase: Specific interaction of the N-terminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase. J. Biol. Chem. 271: 22152-22158
148. McPhail L. C., Waite K. A., Regier D. S., Nixon J. B., Qualliotine-Mann D., Zhang W. X. et al. (1999) A novel protein kinase target for the lipid second messenger phosphatidic acid. Biochim. Biophys. Acta 1439: 277-290
149. Reeves E. P., Dekker L. V., Forbes L. V., Wientjes F. B., Grogan A., Pappin D. J. et al. (1999) Direct interaction between p47phox and protein kinase C: Evidence for targeting of protein kinase C by p47phox in neutrophils. Biochem. J. 344: 859-866
150. - generation but not degranulation or adherence in differentiated HL60 cells. J. Biol. Chem. 273: 27292-27299
151. Faust L. R., El Benna J., Babior B. M. and Chanock S. J. (1995) The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase: Functions of the individual target serines as evaluated by site-directed mutagenesis. J. Clin. Invest. 96: 1499-1505
152. El Benna J., Faust R. P., Johnson J. L. and Babior B. M. (1996) Phosphorylation of the respiratory burst oxidase subunit p47phox 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: 6374-6378
153. Johnson J. L., Park J. W., El Benna J., Faust L. P., Inanami O. and Babior B. M. (1998) Activation of p47(PHOX), a cytosolic subunit of the leukocyte NADPH oxidase: Phosphorylation of ser-359 or ser-370 precedes phosphorylation at other sites and is required for activity. J. Biol. Chem. 273: 35147-35152
154. Inanami O., Johnson J. L., McAdara J. K., El Benna J., Faust L. R., Newburger P. E. et al. (1998) Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47PHOX on serine 303 or 304. J. Biol. Chem. 273: 9539-9543
155. Swain S. D., Helgerson S. L., Davis A. R., Nelson L. K. and Quinn M. T. (1997) Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy. J. Biol. Chem. 272: 29502-29510
156. Park H. S. and Park J. W. (1998) Fluorescent labeling of the leukocyte NADPH oxidase subunit p47(phox): Evidence for amphiphile-induced conformational changes. Arch. Biochem. Biophys. 360: 165-172
157. Ago T., Nunoi H., Ito T. and Sumimoto H. (1999) Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox): Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase. J. Biol. Chem. 274: 33644-33653
158. Huang J. and Kleinberg M. E. (1999) Activation of the phagocyte NADPH oxidase protein p47(phox): Phosphorylation controls SH3 domain-dependent binding to p22(phox). J. Biol. Chem. 274: 19731-19737
159. Shiose A. and Sumimoto H. (2000) Arachidonic acid and phosphorylation synergistically induce a conformational change of p47phox to activate the phagocyte NADPH oxidase. J. Biol. Chem. 275: 13793-13801
160. Pilloud-Dagher M. C. and Vignais P. V. (1991) Purification and characterization of an oxidase activating factor of 63 kilodaltons from bovine neutrophils. Biochemistry 30: 2753-2760
161. Grizot S., Grandvaux N., Fieschi F., Faure J., Massenet C., Andrieu J. P. et al. (2001) Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox. Biochemistry 40: 3127-3133
162. Lapouge K., Smith S. J., Walker P. A., Gamblin S. J., Smerdon S. J. and Rittinger K. (2000) Structure of the TPR domain of p67phox in complex with Rac-GTP. Mol. Cell 6: 899-907
163. Grizot S., Fieschi F., Dagher M. C. and Pebay-Peyroula E. (2001) The active N-terminal region of p67phox: Structure at 1.8 Å resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease. J. Biol. Chem. 276: 21627-21631
164. Diekmann D., Abo A., Johnston C., Segal A. W. and Hall A. (1994) Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 265: 531-533
165. Koga H., Terasawa H., Nunoi H., Takeshige K., Inagaki F. and Sumimoto H. (1999) Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase. J. Biol. Chem. 274: 25051-25060
166. Han C. H., Freeman J. L., Lee T., Motalebi S. A. and Lambeth J. D. (1998) Regulation of the neutrophil respiratory burst oxidase: Identification of an activation domain in p67(phox). J. Biol. Chem. 273: 16663-16668
167. Dusi S. and Rossi F. (1993) Activation of NADPH oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox. Biochem. J. 296: 367-371
168. Forbes L. V., Truong O., Wientjes F. B., Moss S. J. and Segal A. W. (1999) The major phosphorylation site of the NADPH oxidase component p67phox is Thr233. Biochem. J. 338: 99-105
169. Smith R. M., Connor J. A., Chen L. M. and Babior B. M. (1996) The cytosolic subunit p67phox contains an NADPH-binding site that participates in catalysis by the leukocyte NADPH oxidase. J. Clin. Invest. 98: 977-983
170. Dang P. M., Johnson J. L. and Babior B. M. (2000) Binding of nicotinamide adenine dinucleotide phosphate to the tetratricopeptide repeat domains at the N-terminus of p67PHOX, a subunit of the leukocyte nicotinamide adenine dinucleotide phosphate oxidase. Biochemistry 39: 3069-3075
171. Zhan S., Vazquez N., Wientjes F. B., Budarf M. L., Schrock E., Ried T. 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
172. Ellson C. D., Gobert-Gosse S., Anderson K. E., Davidson K., Erdjument-Bromage H., Tempst P. et al. (2001) PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox). Nat. Cell Biol. 3: 679-682
173. Bravo J., Karathanassis D., Pacold C. M., Pacold M. E., Ellson C. D., Anderson K. E. et al. (2001) The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell 8: 829-839
174. Ponting C. P. (1996) Novel domains in NADPH oxidase subunits, sorting nexins, and Ptdlns 3-kinases: Binding partners of SH3 domains? Protein Sci. 5: 2353-2357
175. Nakamura R., Sumimoto H., Mizuki K., Hata K., Ago T., Kitajima S. et al. (1998) The PC motif: A novel and evolutionarily conserved sequence involved in interaction between p40phox and p67phox, SH3 domain-containing cytosolic factors of the phagocyte NADPH oxidase. Eur. J. Biochem. 251: 583-589
176. Fuchs A., Bouin A. P., Rabilloud T. and Vignais P. V. (1997) The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells. Eur. J. Biochem. 249: 531-539
177. Bouin A. P., Grandvaux N., Vignais P. V. and Fuchs A. (1998) p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: Implication of a protein kinase C-type kinase in the phosphorylation process. J. Biol. Chem. 273: 30097-30103
178. Grandvaux N., Elsen S. and Vignais P. V. (2001) Oxidant-dependent phosphorylation of p40phox in B lymphocytes. Biochem. Biophys. Res. Commun. 287: 1009-1016
179. Park H. S., Lee S. M., Lee J. H., Kim Y. S., Bae Y. S. and Park J. W. (2001) Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: Conformation-dependent phosphorylation and modulation of oxidase activity. Biochem. J. 358: 783-790
180. Fuchs A., Dagher M. C. and Vignais P. V. (1995) Mapping the domains of interaction of p40phox with both p47phox and p67phox of the neutrophil oxidase complex using the two-hybrid system. J. Biol. Chem. 270: 5695-5697
181. Fuchs A., Dagher M. C., Faure J. and Vignais P. V. (1996) Topological organization of the cytosolic activating complex of the superoxide-generating NADPH-oxidase: Pinpointing the sites of interaction between p47phoz, p67phox and p40phox using the two-hybrid system. Biochim. Biophys. Acta. 1312: 39-47
182. Sumimoto H., Kage Y., Nunoi H., Sasaki H., Nose T., Fukumaki Y. et al. (1994) Role of Src homology 3 domains in assembly and activation of the phagocyte NADPH oxidase. Proc. Natl. Acad. Sci. USA 91: 5345-5349
183. Mendez I. de, Garrett M. C., Adams A. G. and Leto T. L. (1994) Role of p67-phox SH3 domains in assembly of the NADPH oxidase system. J. Biol. Chem. 269: 16326-16332
184. Finan P., Shimizu Y., Gout I., Hsuan J., Truong O., Butcher C. et al. (1994) An SH3 domain and proline-rich sequence mediate an interaction between two components of the phagocyte NADPH oxidase complex. J. Biol. Chem. 269: 13752-13755
185. Leusen J. H., Bolscher B. G., Hilarius P. M., Weening R. S., Kaulfersch W., Seger R. A. et al. (1994) 156Pro → Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox. J. Exp. Med. 180: 2329-2334
186. Wientjes F. B., Panayotou G., Reeves E. and Segal A. W. (1996) Interactions between cytosolic components of the NADPH oxidase: p40phox interacts with both p67phox and p47phox. Biochem. J. 317: 919-924
187. De Leo F. R., Ulman K. V., Davis A. R., Jutila K. L. and Quinn M. T. (1996) Assembly of the human neutrophil NADPH oxidase involves binding of p67phox and flavocytochrome b to a common functional domain in p47phox. J. Biol. Chem. 271: 17013-17020
188. Lapouge K., Smith S. J., Groemping Y. and Rittinger K. (2002) Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase: A central role for p67phox. J. Biol. Chem. 277: 10121-10128
189. Joseph G. and Pick E. (1995) 'Peptide walking' is a novel method for mapping functional domains in proteins: Its application to the Rac1-dependent activation of NADPH oxidase. J. Biol. Chem. 270: 29079-29082
190. Morozov I., Lotan O., Joseph G., Gorzalczany Y. and Pick E. (1998) Mapping of functional domains in p47(phox) involved in the activation of NADPH oxidase by 'peptide walking'. J. Biol. Chem. 273: 15435-15444
191. Gabig T. G., English D., Akard L. P. and Schell M. J. (1987) Regulation of neutrophil NADPH oxidase activation in a cell-free system by guanine nucleotides and fluoride: Evidence for participation of a pertussis and cholera toxin-insensitive G protein. J. Biol. Chem. 262: 1685-1690
192. Seifert R., Rosenthal W. and Schultz G. (1986) Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils. FEBS Lett. 205: 161-165
193. Ligeti E., Doussiere J. and Vignais P. V. (1988) Activation of the O2(-)-generating oxidase in plasma membrane from bovine polymorphonuclear neutrophils by arachidonic acid, a cytosolic factor of protein nature, and nonhydrolyzable analogues of GTP. Biochemistry 27: 193-200
194. 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
195. 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
196. Dorseuil O., Vazquez A., Lang P., Bertoglio J., Gacon G. and Leca G. (1992) Inhibition of superoxide production in B lymphocytes by rac antisense oligonucleotides. J. Biol. Chem. 267: 20540-20542
197. Didsbury J., Weber R. F., Bokoch G. M., Evans T. and Snyderman R. (1989) rac, a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264: 16378-16382
198. Dorseuil O., Reibel L., Bokoch G. M., Camonis J. and Gacon G. (1996) The Rac target NADPH oxidase p67phox interacts preferentially with Rac2 rather than Rac1. J. Biol. Chem. 271: 83-88.
199. Szaszi K., Korda A., Wolff 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
200. 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
201. Scheffzek K., Stephan I., Jensen O. N., Illenberger D. and Gierschik P. (2000) The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat. Struct. Biol. 7: 122-126
202. Grizot S., Faure J., Fieschi F., Vignais P. V., Dagher M. C. and Pebay-Peyroula E. (2001) Crystal structure of the Rac1-RhoGDI complex involved in NADPH oxidase activation. Biochemistry 40: 10007-10013
203. Di-Poi N., Faure J., Grizot S., Molnar G., Pick E. and Dagher M. C. (2001) Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex. Biochemistry 40: 10014-10022
204. Gorzalczany Y., Sigal N., Itan M., Lotan O. and Pick E. (2000) Targeting of Rac1 to the phagocyte membrane is sufficient for the induction of NADPH oxidase assembly. J. Biol. Chem. 275: 40073-40081
205. Ahmed S., Prigmore E., Govind S., Veryard C., Kozma R., Wientjes F. B. et al. (1998) Cryptic Rac-binding and p21(Cdc42Hs/Rac)-activated kinase phosphorylation sites of NADPH oxidase component p67(phox). J. Biol. Chem. 273: 15693-15701
206. Freeman J. L., Kreck M. L., Uhlinger D. J. and Lambeth J. D. (1994) Ras effector-homologue region on Rac regulates protein associations in the neutrophil respiratory burst oxidase complex. Biochemistry 33: 13431-13435
207. Diekmann D., Nobes C. D., Burbelo P.D., Abo A. and Hall A. (1995) Rac GTPase interacts with GAPs and target proteins through multiple effector sites. EMBO J. 14: 5297-5305
208. Freeman J. L., Abo A. and Lambeth J. D. (1996) Rac 'insert region' is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J. Biol. Chem. 271: 19794-19801
209. Nisimoto Y., Freeman J. L., Motalebi S. A., Hirshberg M. and Lambeth J. D. (1997) Rac binding to p67(phox): Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase. J. Biol. Chem. 272: 18834-18841
210. Diebold B. A. and Bokoch G. M. (2001) Molecular basis for Rac2 regulation of phagocyte NADPH oxidase. Nat. Immunol. 2: 211-215
211. Toporik A., Gorzalczany Y., Hirshberg M., Pick E. and Lotan O. (1998) Mutational analysis of novel effector domains in Rac1 involved in the activation of nicotinamide adenine dinucleotide phosphate (reduced) oxidase. Biochemistry 37: 7147-7156
212. Kreck M. L., Freeman J. L.,Abo A. and Lambeth J. D. (1996) Membrane association of Rac is required for high activity of the respiratory burst oxidase. Biochemistry 35: 15683-15692
213. Tsunawaki S., Kagara S., Yoshikawa K., Yoshida L. S., Kuratsuji T. and Namiki H. (1996) Involvement of p40phox in activation of phagocyte NADPH oxidase through association of its carboxyl-terminal, but not its amino-terminal, with p67phox. J. Exp. Med. 184: 893-902
214. Rinckel L. A., Faris S. L., Hitt N. D. and Kleinberg M. E. (1999) Rac1 disrupts p67phox/p40phox binding: A novel role for Rac in NADPH oxidase activation. Biochem. Biophys. Res. Commun. 263: 118-122
215. Kleinberg M. E., Malech H. L. and Rotrosen D. (1990) The phagocyte 47-kilodalton cytosolic oxidase protein is an early reactant in activation of the respiratory burst. J. Biol. Chem. 265: 15577-15583
216. Heyworth P. G., Curnutte J. T., Nauseef W. M., Volpp B. D., Pearson D. W., Rosen H. et al. (1991) Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly: Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558. J. Clin. Invest. 87: 352-356
217. Iyer S. S., Pearson D. W., Nauseef W. M. and Clark R. A. (1994) Evidence for a readily dissociable complex of p47phox and p67phox in cytosol of unstimulated human neutrophils. J. Biol. Chem. 269: 22405-22411
218. Koshkin V., Lotan O. and Pick E. (1996) The cytosolic component p47(phox) is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production. J. Biol. Chem. 271: 30326-30329
219. Freeman J. L. and Lambeth J. D. (1996) NADPH oxidase activity is independent of p47phox in vitro. J. Biol. Chem. 271: 22578-22582
220. Ebisu K., Nagasawa T., Watanabe K., Kakinuma K., Miyano K. and Tamura M. (2001) Fused p47phox and p67phox truncations efficiently reconstitute NADPH oxidase with higher activity and stability than the individual components. J. Biol. Chem. 276: 24498-24505
221. 558. Proc. Natl. Acad. Sci. USA 98: 3001-3005
222. 558 II. Proc. Natl. Acad. Sci. USA 99: 4262-4265
223. Prigmore E., Ahmed S., Best A., Kozma R., Manser E., Segal A. W. et al. (1995) A 68-kDa kinase and NADPH oxidase component p67phox are targets for Cdc42Hs and Rac1 in neutrophils. J. Biol. Chem. 270: 10717-10722
224. Heyworth P. G., Bohl B. P., Bokoch G. M. and Curnutte J. T. (1994) Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox: Evidence for its interaction with flavocytochrome b558. J. Biol. Chem. 269: 30749-30752
225. Dorseuil O., Quinn M. T. and Bokoch G. M. (1995) Dissociation of Rac translocation from p47phox/p67phox movements in human neutrophils by tyrosine kinase inhibitors. J. Leukoc. Biol. 58: 108-113
226. Dusi S., Donini M. and Rossi F. (1996) Mechanisms of NADPH oxidase activation: Translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox. Biochem. J. 314: 409-412
227. Vergnaud S., Paclet M. H., El Benna J., 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
228. Miyano K., Ogasawara S., Han C. H., Fukuda H. and Tamura M. (2001) A fusion protein between rac and p67phox (1-210) reconstitutes NADPH oxidase with higher activity and stability than the individual components. Biochemistry 40: 14089-14097
229. Alloul N., Gorzalczany Y., Itan M., Sigal N. and Pick E. (2001) Activation of the superoxide-generating NADPH oxidase by chimeric proteins consisting of segments of the cytosolic component p67(phox) and the small GTPase Rac1. Biochemistry 40: 14557-14566
230. Gorzalczany Y., Alloul N., Sigal N., Weinbaum C. and Pick E. (2002) A prenylated p67phox-Rac1 chimera elicits NADPH-dependent superoxide production by phagocyte membranes in the absence of an activator and of p47phox: Conversion of a pagan NADPH oxidase to monotheism. J. Biol. Chem. 277:18605-18610
231. Kim C. and Dinauer M. C. (2001) Rac2 is an essential regulator of neutrophil nicotinamide adenine dinucleotide phosphate oxidase activation in response to specific signaling pathways. J. Immunol. 166: 1223-1232
232. Welch H. C., Coadwell W. J., Ellson C. D., Ferguson G. J., Andrews S. R., Erdjument-Bromage H. et al. (2002) P-Rex1, a PtdIns(3,4,5)P3- and G beta gamma-regulated guanine-nucleotide exchange factor for Rac. Cell 108: 809-821
233. Leto T. L., Adams A. G. and Mendez I. de (1994) Assembly of the phagocyte NADPH oxidase: Binding of Src homology 3 domains to proline-rich targets. Proc. Natl. Acad. Sci. USA 91: 10650-10654
234. Dahan I., Issaeva I., Gorzalczany Y., Sigal N., Hirshberg M. and Pick E. (2002) Mapping of functional domains in the p22(phox) subunit of flavocytochrome b(559) participating in the assembly of the NADPH oxidase complex by 'peptide walking'. J. Biol. Chem. 277: 8421-8432
235. Zhen L., Yu L. and Dinauer M. C. (1998) Probing the role of the carboxyl terminus of the gp91 phox subunit of neutrophil flavocytochrome b558 using site-directed mutagenesis. J. Biol. Chem. 273: 6575-6581
236. Leusen J. H., Boer M. de, Bolscher B. G., Hilarius P. M., Weening R. S., Ochs H. D. et al. (1994) A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox. J. Clin. Invest. 93: 2120-2126
237. Biberstine-Kinkade K. J., Yu L. and Dinauer M. C. (1999) Mutagenesis of an arginine- and lysine-rich domain in the gp91 (phox) subunit of the phagocyte NADPH-oxidase flavocytochrome b558. J. Biol. Chem. 274: 10451-10457
238. Dusi S., Nadalini K. A., Donini M., Zentilin L., Wientjes F. B., Roos D. et al. (1998) Nicotinamide-adenine dinucleotide phosphate oxidase assembly and activation in EBV-transformed B lymphoblastoid cell lines of normal and chronic granulomatous disease patients. J. Immunol. 161: 4968-4974
239. Cross A. R., Yarchover J. L. and Curnutte J. T. (1994) The superoxide-generating system of human neutrophils possesses a novel diaphorase activity: Evidence for distinct regulation of electron flow within NADPH oxidase by p67-phox and p47-phox. J. Biol. Chem. 269: 21448-21454
240. Doussiere J. and Vignais P. V. (1992) Diphenylene iodonium as an inhibitor of the NADPH oxidase complex of bovine neutrophils: Factors controlling the inhibitory potency of diphenylene iodonium in a cell-free system of oxidase activation. Eur. J. Biochem. 208: 61-71
241. Cross A. R., Heyworth P. G., Rae J. and Curnutte J. T. (1995) A variant X-linked chronic granulomatous disease patient (X91+) with partially functional cytochrome b. J. Biol. Chem. 270: 8194-8200
242. Nisimoto Y., Motalebi S., Han C. H. and Lambeth J. D. (1999) The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). J. Biol. Chem. 274: 22999-23005
243. Poinas A., Gaillard J., Vignais P. and Doussiere J. (2002) Exploration of the diaphorase activity of neutrophil NADPH oxidase. Eur. J. Biochem. 269: 1243-1252
244. Cross A. R., Higson F. K., Jones O. T., Harper A. M. and Segal A. W. (1982) The enzymic reduction and kinetics of oxidation of cytochrome b-245 of neutrophils. Biochem. J. 204: 479-485
245. Morel F. and Vignais P. V. (1984) Examination of the oxidase function of the b-type cytochrome in human polymorphonuclear leucocytes. Biochim. Biophys. Acta 764: 213-225
246. 2 is necessary for the fast reduction of cytochrome b-245 by NADPH. Biochem. J. 226: 881-884
247. Koshkin V. (1995) Aerobic and anaerobic functioning of superoxide-producing cytochrome b-559 reconstituted with phospholipids. Biochim. Biophys. Acta 1232: 225-229
248. Ellis J. A., Cross A. R. and Jones O. T. (1989) Studies on the electron-transfer mechanism of the human neutrophil NADPH oxidase. Biochem. J. 262: 575-579
249. Segal A. W. and Jones O. T. (1979) Reduction and subsequent oxidation of a cytochrome b of human neutrophils after stimulation with phorbol myristate acetate. Biochem. Biophys. Res. Commun. 88: 130-134
250. Iizuka T., Kanegasaki S., Makino R., Tanaka T. and Ishimura Y. (1985) Pyridine and imidazole reversibly inhibit the respiratory burst in porcine and human neutrophils: Evidence for the involvement of cytochrome b558 in the reaction. Biochem. Biophys. Res. Commun. 130: 621-626
251. Fujii H. and Kakinuma K. (1992) Electron paramagnetic resonance studies on cytochrome b-558 and peroxidases of pig blood granulocytes. Biochim. Biophys. Acta 1136: 239-246
252. Miki T., Fujii H. and Kakinuma K. (1992) EPR signals of cytochrome b558 purified from porcine neutrophils. J. Biol. Chem. 267: 19673-19675
253. - generating activity. J. Biol. Chem. 270: 12685-12689
254. Isogai Y., Iizuka T. and Shiro Y. (1995) The mechanism of electron donation to molecular oxygen by phagocytic cytochrome b558. J. Biol. Chem. 270: 7853-7857
255. - 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
256. Doussiere J., Bouzidi F., Poinas A., Gaillard J. and Vignais P. V. (1999) Kinetic study of the activation of the neutrophil NADPH oxidase by arachidonic acid: Antagonistic effects of arachidonic acid and phenylarsine oxide. Biochemistry 38: 16394-16406
257. Bauldry S. A., Wooten R. E. and Bass D. A. (1996) Activation of cytosolic phospholipase A2 in permeabilized human neutrophils. Biochim. Biophys. Acta 1299: 223-234
258. Dana R., Leto T. L., Malech H. L. and Levy R. (1998) Essential requirement of cytosolic phospholipase A2 for activation of the phagocyte NADPH oxidase. J. Biol. Chem. 273: 441-445
259. Lowenthal A. and Levy R. (1999) Essential requirement of cytosolic phospholipase A(2) for activation of the H(+) channel in phagocyte-like cells. J. Biol. Chem. 274: 21603-21608
260. Pessach I., Leto T. L., Malech H. L. and Levy R. (2001) Essential requirement of cytosolic phospholipase A(2) for stimulation of NADPH oxidase-associated diaphorase activity in granulocyte-like cells. J. Biol. Chem. 276: 33495-33503
261. Edgeworth J., Gorman M., Bennett R., Freemont P. and Hogg N. (1991) Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells. J. Biol. Chem. 266: 7706-7713
262. 2+-binding proteins MRP8 and MRP14 binds to arachidonic acid. FEBS Lett. 408: 81-84
263. Siegenthaler G., Roulin K., Chatellard-Gruaz D., Hotz R., Saurat J. H., Hellman U. et al. (1997) A heterocomplex formed by the calcium-binding proteins MRP8 (S100A8) and MRP 14 (S100A9) binds unsaturated fatty acids with high affinity. J. Biol. Chem. 272: 9371-9377
264. Kerkhoff C., Klempt M., Kaever V. and Sorg C. (1999) The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils. J. Biol. Chem. 274: 32672-32679
265. Doussiere J., Bouzidi F. and Vignais P. V. (2001) A phenylarsine oxide-binding protein of neutrophil cytosol, which belongs to the S100 family, potentiates NADPH oxidase activation. Biochem. Biophys. Res. Commun. 285: 1317-1320
266. Le Cabec V. and Maridonneau-Parini I. (1995) Complete and reversible inhibition of NADPH oxidase in human neutrophils by phenylarsine oxide at a step distal to membrane translocation of the enzyme subunits. J. Biol. Chem. 270: 2067-2073
267. Kutsumi H., Kawai K., Johnston R. B. Jr. and Rokutan K. (1995) Evidence for participation of vicinal dithiols in the activation sequence of the respiratory burst of human neutrophils. Blood 85: 2559-2569
268. Doussiere J., Poinas A., Blais C. and Vignais P. V. (1998) Phenylarsine oxide as an inhibitor of the activation of the neutrophil NADPH oxidase - Identification of the beta subunit of the flavocytochrome b component of the NADPH oxidase as a target site for phenylarsine oxide by photoaffinity labeling and photoinactivation. Eur. J. Biochem. 251: 649-658
269. Cross A. R. and Jones O. T. G. (1986) Effect of the inhibitor diphenylene iodonium on the superoxide generating system of neutrophils: Specific labeling of a component of the oxidase. Biochem. J. 237: 111-116
270. Ellis J. A., Mayer S. J. and Jones O. T. (1988) The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils. Biochem. J. 251: 887-891
271. O'Donnell B. V., Tew D. G., Jones O. T. and England P. J. (1993) Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem. J. 290: 41-49
272. - generating oxidase of neutrophils by iodonium biphenyl in a cell free system: Effect of the redox state of the oxidase complex. Biochem. Biophys. Res. Commun. 175: 143-151
273. Doussiere J., Gaillard J. and Vignais P. V. (1999) The heme component of the neutrophil NADPH oxidase complex is a target for aryliodonium compounds. Biochemistry 38: 3694-3703
274. Mayhew S. G., Foust G. P. and Massey V. (1969) Oxidation-reduction properties of flavodoxin from Peptostreptococcus elsdenii. J. Biol. Chem. 244: 803-810
275. Mayhew S. G., O'Connell D. P., O'Farrell P. A., Yalloway G. N. and Geoghegan S. M. (1996) Regulation of the redox potentials of flavodoxins: Modification of the flavin binding. Biochem. Soc. Trans. 24: 122-127
276. - channel. Biochem. J. 246: 325-329
277. Jankowski A. and Grinstein S. (1999) A noninvasive fluorimetric procedure for measurement of membrane potential: Quantification of the NADPH oxidase-induced depolarization in activated neutrophils. J. Biol. Chem. 274: 26098-26104
278. Schrenzel J., Serrander L., Banfi B., Nusse O., Fouyouzi R., Lew D. P. et al. (1998) Electron currents generated by the human phagocyte NADPH oxidase. Nature 392: 734-737
279. - channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: Evidence for at least two target sites. Biochem. J. 358: 315-324
280. + channel is opened by arachidonate. Biochem. J. 283: 171-175
281. DeCoursey T. E. and Cherny V. V. (1993) Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils. Biophys. J. 65: 1590-1598
282. + channel: Evidence that gp91-phox functions as an essential part of the channel. J. Biol. Chem. 270: 5909-5916
283. - channel is contained within the multi-membrane-spanning N-terminal region of gp91-phox. Biochem. J. 325: 701-705
284. + channel. J. Biol. Chem. 273: 33216-33223
285. Maturana A., Arnaudeau S., Ryser S., Banfi B., Hossle J. P., Schlegel W. et al. (2001) Heme histidine ligands within gp91(phox) modulate proton conduction by the phagocyte NADPH oxidase. J. Biol. Chem. 276: 30277-30284
286. + conductance of leukocytes. J. Biol. Chem. 269: 27280-27285
287. DeCoursey T. E., Cherny V. V., Morgan D., Katz B. Z. and Dinauer M. C. (2001) The gp91phox component of NADPH oxidase is not the voltage-gated proton channel in phagocytes, but it helps. J. Biol. Chem. 276: 36063-36066
288. Hua J., Hasebe T., Someya A., Nakamura S., Sugimoto K. and Nagaoka I. (2000) Evaluation of the expression of NADPH oxidase components during maturation of HL-60 cells to neutrophil lineage. J. Leukoc. Biol. 68: 216-224
289. Mizuki K., Kadomatsu K., Hata K., Ito T., Fan Q. W., Kage Y. et al. (1998) Functional modules and expression of mouse p40(phox) and p67(phox), SH3- domain-containing proteins involved in the phagocyte NADPH oxidase complex. Eur. J. Biochem. 251: 573-582
290. 558. J. Clin. Invest. 94: 1205-1211
291. Petterson M. and Schaffner W. (1987) A purine-rich DNA sequence motif present in SV40 and lymphotropic papovavirus binds a lymphoid-specific factor and contributes to enhancer activity in lymphoid cells. Genes Dev. 1: 962-972
292. Simon M. C. (1998) PU.1 and hematopoiesis: Lessons learned from gene targeting experiments. Semin. Immunol. 10: 111-118
293. Eklund E. A., Jalava A. and Kakar R. (1998) PU.1, interferon regulatory factor 1, and interferon consensus sequence-binding protein cooperate to increase gp91(phox) expression. J. Biol. Chem. 273: 13957-13965
294. Suzuki S., Kumatori A., Haagen I. A., Fujii Y., Sadat M. A., Jun H. L. et al. (1998) PU.1 as an essential activator for the expression of gp91(phox) gene in human peripheral neutrophils, monocytes, and B lymphocytes. Proc. Natl. Acad. Sci. USA 95: 6085-6090
295. Islam M. R., Fan C., Fujii Y., Hao L. J., Suzuki S., Kumatori A. et al. (2002) PU.1 is dominant and HAF-1 supplementary for activation of the gp91(phox) promoter in human monocytic PLB-985 cells. J. Biochem. (Tokyo) 131: 533-540
296. Skalnik D. G., Strauss E. C. and Orkin S. H. (1991) CCAAT displacement protein as a repressor of the myelomonocytic-specific gp91-phox gene promoter. J. Biol. Chem. 266: 16736-16744
297. Lievens P. M., Donady J. J., Tufarelli C. and Neufeld E. J. (1995) Repressor activity of CCAAT displacement protein in HL-60 myeloid leukemia cells. J. Biol. Chem. 270: 12745-12750
298. Catt D., Hawkins S., Roman A., Luo W. and Skalnik D. G. (1999) Overexpression of CCAAT displacement protein represses the promiscuously active proximal gp91(phox) promoter. Blood 94: 3151-3160
299. Li S. L., Valente A. J., Zhao S. J. and Clark R. A. (1997) PU.1 is essential for p47(phox) promoter activity in myeloid cells. J. Biol. Chem. 272: 17802-17809
300. Li S. L., Valente A. J., Wang L., Gamez M. J. and Clark R. A. (2001) Transcriptional regulation of the p67phox gene: Role of AP-1 in concert with myeloid-specific transcription factors. J. Biol. Chem. 276: 39368-39378
301. Porter C. D., Parkar M. H., Verhoeven A. J., Levinsky R. J., Collins M. K. and Kinnon C. (1994) p22-phox-deficient chronic granulomatous disease: Reconstitution by retrovirus-mediated expression and identification of a biosynthetic intermediate of gp91-phox. Blood 84: 2767-2775
302. Porter C. D., Kuribayashi F., Parkar M. H., Roos D. and Kinnon C. (1996) Detection of gp91-phox precursor protein in B-cell lines from patients with X-linked chronic granulomatous disease as an indicator for mutations impairing cytochrome b558 biosynthesis. Biochem. J. 315: 571-575
303. Yu L., DeLeo F. R., Biberstine-Kinkade K. J., Renee J., Nauseef W. M. and Dinauer M. C. (1999) Biosynthesis of flavocytochrome b558: gp91(phox) is synthesized as a 65-kDa precursor (p65) in the endoplasmic reticulum. J. Biol. Chem. 274: 4364-4369
304. De Leo F. R., Burritt J. B., Yu L., Jesaitis A. J., Dinauer M. C. and Nauseef W. M. (2000) Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly. J. Biol. Chem. 275: 13986-13993
305. Suh Y. A., Arnold R. S., Lassegue B., Shi J., Xu X., Sorescu D. et al. (1999) Cell transformation by the superoxide-generating oxidase Mox1. Nature 401: 79-82
306. Arnold R. S., Shi J., Murad E., Whalen A. M., Sun C. Q., Polavarapu R. et al. (2001) Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1. Proc. Natl. Acad. Sci. USA 98: 5550-5555
307. Arbiser J. L., Petros J., Klafter R., Govindajaran B., McLaughlin E. R., Brown L. F. et al. (2002) Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc. Natl. Acad. Sci. USA 99: 715-720
308. Kikuchi H., Hikage M., Miyashita H. and Fukumoto M. (2000) NADPH oxidase subunit, gp91(phox) homologue, preferentially expressed in human colon epithelial cells. Gene 254: 237-243
309. + channel generated through alternative splicing of the NADPH oxidase homolog NOH-1. Science 287: 138-142
310. Cheng G., Cao Z., Xu X., Meir E. G. van and Lambeth J. D. (2001) Homologs of gp91 phox: Cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269: 131-140
311. Geiszt M., Kopp J. B., Varnai P. and Leto T. L. (2000) Identification of renox, an NAD(P)H oxidase in kidney. Proc. Natl. Acad. Sci. USA 97: 8010-8014
312. Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S. et al. (2001) A novel superoxide-producing NAD(P)H oxidase in kidney. J. Biol. Chem. 276: 1417-1423
313. Yang S., Madyastha P, Bingel S., Ries W. and Key L. (2001) A new superoxide-generating oxidase in murine osteoclasts. J. Biol. Chem. 276: 5452-5458
314. Banfi B., Molnar G., Maturana A., Steger K., Hegedus B., Demaurex N.
315. Dupuy C., Ohayon R., Valent A., Noel-Hudson M. S., Deme D. and Virion A. (1999) Purification of a novel flavoprotein involved in the thyroid NADPH oxidase: Cloning of the porcine and human cDNAs. J. Biol. Chem. 274: 37265-37269
316. De Deken X., Wang D., Many M. C., Costagliola S., Libert F., Vassart G. et al. (2000) Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275: 23227-23233
317. Dupuy C., Pomerance M., Ohayon R., Noel-Hudson M. S., Deme D., Chaaraoui M. et al. (2000) Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5. Biochem. Biophys. Res. Commun. 277: 287-292
318. De Deken X., Wang D., Dumont J. E. and Miot F. (2002) Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system. Exp. Cell Res. 273: 187-196
319. Edens W. A., Sharling L., Cheng G., Shapira R., Kinkade J. M., Lee T. et al. (2001) Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J. Cell Biol. 154: 879-891
320. Torres M. A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K. E. and Jones J. D. (1998) Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox). Plant J. 14: 365-370
321. Bestwick C. S., Brown I. R., Bennett M. H. and Mansfield J. W. (1997) Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv phaseolicola. Plant Cell 9: 209-221
322. 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
323. Price M. O., Atkinson S. J., Knaus U. G. and Dinauer M. C. (2002) Rac activation induces NADPH oxidase activity in transgenic COS phox cells, and the level of superoxide production is exchange factor-dependent. J. Biol. Chem. 277: 19220-19228
324. Grogan A., Reeves E., Keep N., Wientjes F., Totty N. F., Burlingame A. L. et al. (1997) Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils. J. Cell Sci. 110: 3071-3081
325. Tamura M., Kai T, Tsunawaki S., Lambeth J. D. and Kameda K. (2000) Direct interaction of actin with p47(phox) of neutrophil NADPH oxidase. Biochem. Biophys. Res. Commun. 276: 1186-1190
326. Wientjes F. B., Reeves E. P., Soskic V, Furthmayr H. and Segal A. W. (2001) The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain. Biochem. Biophys. Res. Commun. 289: 382-388
327. Doussiere J., Bouzidi F. and Vignais P. V. (2002) The S100A8/A9 protein as a partner for the cytosolic factors of NADPH oxidase activation in neutrophils. Eur. J. Biochem. 269: 1-10
328. Grandvaux N., Grizot S., Vignais P. V. and Dagher M. C. (1999) The Ku70 autoantigen interacts with p40phox in B lymphocytes. J. Cell Sci. 112: 503-513