Expression of gp91phDX/Nox2 in COS-7 cells: Cellular localization of the protein and the detection of outward proton currents

Biochemical Journal

Volumn 385, Issue 3, 2005, Pages 649-657

  Murillo, Isabel ^a   Henderson, Lydia M ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Confocal microscopy; COS 7 cell; Green fluorescent protein; NADPH oxidase; Nox2; Proton current

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; ELECTRIC CURRENTS; ELECTRIC POTENTIAL; FUSION REACTIONS; PROTONS;

CHINESE HAMSTER OVARY (CHO) CELLS; INTRACELLULAR MEMBRANES; PLASMA MEMBRANES; PROTON CURRENTS;

PROTEINS;

ENHANCED GREEN FLUORESCENT PROTEIN; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; ZINC; CYBB PROTEIN, HUMAN; MEMBRANE PROTEIN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL STRAIN COS7; CHO CELL; CONTROLLED STUDY; CYTOPLASM; ELECTRIC CURRENT; ELECTRIC POTENTIAL; GENETIC TRANSFECTION; INTRACELLULAR MEMBRANE; NONHUMAN; PH MEASUREMENT; PIPETTE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; WHOLE CELL; ANIMAL; CELL MEMBRANE POTENTIAL; CELL STRAIN COS1; ELECTRIC CONDUCTIVITY; GENETICS; HAMSTER; HUMAN; METABOLISM; PATCH CLAMP; PH; PHYSIOLOGY; PROTEIN TRANSPORT; TIME;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

ANIMALS; CHO CELLS; COS CELLS; CRICETINAE; ELECTRIC CONDUCTIVITY; HUMANS; HYDROGEN-ION CONCENTRATION; MEMBRANE GLYCOPROTEINS; MEMBRANE POTENTIALS; NADPH OXIDASE; PATCH-CLAMP TECHNIQUES; PROTEIN TRANSPORT; PROTONS; TIME FACTORS; TRANSFECTION;

EID: 13444251169     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040829     Document Type: Article

References (33)

1. + channel. Biochem. J. 246, 325-329
2. Schrenzel, J., Serrander, L., Banfi, B., Nusse, D. Fouyouzi, R., Lew, D. P., Demaurex, N. and Krause, K. H. (1998) Electron currents generated by the human phagocyte NADPH oxidase. Nature (London) 392, 734-737
3. Jankowski, A. and Grinsfein, 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
4. + Ilux. Nature (London) 416, 291-297
5. + channel is essential for innate immunity. Nature (London) 427, 853-858
6. Henderson, L. M., Chappell, J. B. and Jones, O. T. (1988) Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge. Biochem. J. 255, 285-290
7. Roos, O., De Boer, M., Kuribayashi, F., Meischl, C., Weening, R. S., Segal, A. W., Ahlin, A., Nemet, K., Hossle, J. P., Bernatowska-Matuszkiewicz, E. and Middleton-Price, H. (1996) Mutations in the X-linked and autosomal recessive forms of chronic granulomatous disease. Blood 87, 1663-1681
8. Lambeth, J. D., Cheng, G., Arnold, R. S. and Edens, W. A. (2000) Novel homologs of gp91phox. Trends Biochem. Sci. 10, 459-461
9. Banfi, B., Clark, R. A., Steger, K. and Krause, K. H. (2003) Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J. Biol. Chem. 278, 3510-3513
10. phox support superoxide production by NAO(P)H oxidase 1 in colon epithelial cells. J. Biol. Chem. 278, 20006-20012
11. phox participate in activation of superoxide-producing NAOPH oxidase. J. Biol. Chem. 278, 25234-25246
12. + pathway. J. Gen. Physiol. 114, 771-786
13. phox functions as an essential part of the channel. J. Biol. Chem. 270, 5909-5916
14. + channel is contained within the multi-membrane-spanning N-terminal region of gp91-phox. Biochem. J. 325, 701-705
15. + channel. J. Biol. Chem. 273, 33216-33223
16. phox requires histidine 115. Protoplasma 221, 101-108
17. phox modulate proton conduction by the phagocyte NADPH oxidase. J. Biol. Chem. 276, 30277-30284
18. + channel generated through alternative splicing of the NADPH oxidase homolog NOH-1. Science 287, 138-142
19. 2+-activated NADPH oxidase in festis, spleen, and lymph nodes. J. Biol. Chem. 276, 37594-37601
20. phox component of NADPH oxidase is not the voltage-gated proton channel in phagocytes, but it helps. J. Biol. Chem. 276, 36063-36066
21. Morgan, D., Cherny, V. V., Price, M. O., Dinauer, M. C. and DeCoursey, T. E. (2002) Absence of profon channels in COS-7 cells expressing functional NADPH oxidase components. J. Gen. Physiol. 119, 571-580
22. phox the flavocytochrome of the NADPH oxidase, by site directed mutagenesis and translation in vitro. Biochem. J. 321, 583-585
23. phox is the heme binding subunit of the superoxide-generating NADPH oxidase. Proc. Natl. Acad. Sci. U.S.A. 95, 7993-7998
24. Price, M. D., 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
25. 558. Identification of two juxtaposed extracellular domains. J. Biol. Chem. 276, 2053-2061
26. phox. J. Gen. Physiol. 120, 1-8
27. Cherny, V. V., Markin, V. S. and DeCoursey, T. E. (1995) The voltage activated hydrogen ion conductances in rat alveolar epithelial cells is determined by the pH gradient. J. Gen. Physiol. 105, 861-896
28. DeCoursey, T. E. and Cherny, V. V. (1995) Voltage-activated proton currents in membrane patches of rat alveolar epithelial cells. J. Physiol. (Cambridge, U.K.) 489, 299-307
29. Byerly, L. and Suen, Y. (1989) Characterization of proton currents in neurones of the snail, Lymnaea stagnalis. J Physiol. (Cambridge, U.K.) 413, 75-89
30. Byerly, L. and Moody, W. J. (1986) Membrane currents of internally perfused neurons of the snail, Lymnaea stagnalis, at low intracellular pH. J. Physiol. (Cambridge, U.K.) 376, 477-491
31. phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269, 131-140
32. Geiszt, M., Kopp, J. B., Varnai, P. and Leto, T. L. (2000) Identification of renox, an NAO(P)H oxidase in kidney. Proc. Natl. Acad. Sci. U.S.A. 97, 8010-8014
33. Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y. and Sumimoto, H. (2001) A novel superoxide-producing NAD(P)H oxidase in kidney. J. Biol. Chem. 276, 1417-1423