Four novel mutations in the gene encoding gp91-phox of human NADPH oxidase: Consequences for oxidase assembly

Blood

Volumn 95, Issue 2, 2000, Pages 666-673

  Leusen, J H W ^b   Meischl, C ^b   Eppink, M H M ^b   Hilarius, P M ^b   De Boer, M ^b   Weening, R S ^b   Ahlin A ^b   Sanders, L ^b   Goldblatt, D ^b   Skopczynska, H ^b   Bernatowska, E ^b   Palmblad, J ^b   Verhoeven, A J ^b   Van Berkel, W J H ^b   Roos, D ^a  

^a CENTRAL LABORATORY   (Netherlands)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYTOCHROME B558; DNA; FLAVINE ADENINE NUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RNA;

AMINO ACID SUBSTITUTION; ARTICLE; CHRONIC GRANULOMATOUS DISEASE; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; GENE; GENE MUTATION; HUMAN; HUMAN CELL; PHAGOCYTE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN BINDING;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CELL-FREE SYSTEM; CHILD, PRESCHOOL; CYTOSOL; GRANULOMATOUS DISEASE, CHRONIC; HUMANS; INFANT; LEUKOCYTES, MONONUCLEAR; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADPH OXIDASE; NEUTROPHILS; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; REFERENCE VALUES; RESPIRATORY BURST; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUPEROXIDES; TETRADECANOYLPHORBOL ACETATE;

EID: 12944257362     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (65)

1. Parkos CA, Allen RA, Cochrane CG, Jesaitis AJ. Purified cytochrome b from human plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000. J Clin Invest. 1987;80:732-742.
2. Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH. 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. 1990; 86:1729-1737.
3. Volpp BD, Nauseef WM, Donelson JE, Moser DR, Clark RA: Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase [erratum in Proc Natl Acad Sci U S A. 1989; 86:9563.]. Proc Natl Acad Sci U S A. 1989;86: 7195-7199.
4. Leto TL, Lomax KJ, Volpp BD, et al. Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src. Science. 1990; 248:727-730.
5. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991;254:1512-1515.
6. rac1. Nature. 1991;353:668-670.
7. Wientjes FB, Hsuan JJ, Totty NF, Segal AW. p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem J. 1993;296: 557-561.
8. Tsunawaki S, Mizunari H, Nagata M, Tatsuzawa O, Kuratsuji T. A novel cytosolic component, p40phox, of respiratory burst oxidase associates with p67phox and is absent in patients with chronic granulomatous disease who lack p67phox. Biochem Biophys Res Commun. 1994; 199:1378-1387.
9. rac1 and cytochrome C-245. J Biol Chem. 1992;267:16,767-16,770.
10. 559 in human neutrophils [erratum in Eur J Haematol. 1989;8:270]. Eur J Haematol. 1989; 43:67-77.
11. Johansson A, Jesaitis AJ, Lundqvist H, et al. Different subcellular localization of cytochrome b and the dormant NADPH oxidase in neutrophils and macrophages: effects on the production of reactive oxygen species during phagocytosis. Cell Immunol. 1995;161:61-71.
12. Park JW, Ma M, Ruedi JM, Smith RM, Babior BM. The cytosolic components of the respiratory burst oxidase exist as a M(r) approximately 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system. J Biol Chem. 1992;267:17,327-17,332.
13. Clark RA, Volpp BD, Leidal KG, Nauseef WM. Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation. J Clin Invest. 1990;85:714-721.
14. 2 oxidoreductase in human neutrophils after stimulation with phorbol myristate acetate [erratum in J Biol Chem. 1990;265:19,370.] J Biol Chem. 1990;265:924-930.
15. Roos D, de Boer M, Kuribayashi F, et al. Mutations in the X-linked and autosomal recessive forms of chronic granulomatous disease. Blood. 1996;87:1663-1681.
16. Meischl C, Roos D. The molecular basis of chronic granulomatous disease. Springer Semin Immunopathol. 1998;19:417-434.
17. Leusen JH, Verhoeven AJ, Roos D. Interactions between the components of the human NADPH oxidase: intrigues in the phox family. J Lab Clin Med. 1996;128:461-476.
18. +) with partially functional cytochrome b. J Biol Chem. 1995;270:8194-8200.
19. Ariga T, Sakiyama Y, Tomizawa K, Imajoh-Ohmi S, Kanegasaki S, Matsumoto S. A newly recognized point mutation in the cytochrome b558 heavy chain gene replacing alanine57 by glutamic acid, in a patient with cytochroma b positive X-linked chronic granulomatous disease. Eur J Pediatr. 1993;152:469-472.
20. Segal AW, West I, Wientjes F, et al. Cytochrome b-245 is a flavocytochrome containing FAD and the N ADPH-binding site of the microbicidal oxidase of phagocytes. Biochem J. 1992;284:781-788.
21. Rotrosen D, Yeung CL, Leto TL, Malech HL, Kwong CH. Cytochrome b558: the flavin-binding component of the phagocyte NADPH oxidase. Science. 1992;256:1459-1462.
22. Sumimoto H, Sakamoto N, Nozaki M, Sakaki Y, Takeshige K, Minakami S. Cytochrome b558, a component of the phagocyte NADPH oxidase, is a flavoprotein. Biochem Biophys Res Commun. 1992;186:1368-1375.
23. Dinauer MC, Curnutte JT, Rosen H, Orkin SH. A missense mutation in the neutrophil cytochrome b heavy chain in cytochrome-positive X-linked chronic granutomatous disease. J Clin Invest. 1989;84:2012-2016.
24. Azuma H, Oomi H, Sasaki K, et al. A new mutation in exon 12 of the gp91-phox gene leading to cytochrome b-positive X-linked chronic granulomatous disease. Blood. 1995;85:3274-3277.
25. Schapiro BL, Newburger PE, Klempner MS, Dinauer MC. Chronic granulomatous disease presenting in a 69-year-old man. N Engl J Med. 1991;325:1786-1790.
26. 558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-pnox. J Clin Invest. 1994; 93:2120-2126.
27. Taylor WR, Jones DT, Segal AW. A structural model for the nucleotide binding domains of the flavocytochrome b-245 beta-chain. Protein Sci. 1993;2:1675-1685.
28. 558 of human neutrophils. Blood. 1989;73:1686-1694.
29. Meerhof LJ, Roos D. Heterogeneity in chronic granulomatous disease detected with an improved nitroblue tetrazolium slide test. J Leukoc Biol. 1986;39:699-711.
30. Weening, RS, Roos D, Loos J. Oxygen consumption of phagocytizing cells in human leukocyte and granulocyte preparations: a comparative study. J Lab Clin Med. 1974;83:570-577.
31. Weening RS, Corbeel L, De Boer M, et al. Cytochrome b deficiency in an autosomal form of chronic granulomatous disease: a third form of chronic granulomatous disease recognized by monocyte hybridization. J Clin Invest. 1985;75: 915-920.
32. Lutter R, van Schaik ML, van Zwieten R, Wever R, Roos O, Hamers MN. Purification and partial characterization of the b-type cytochrome from human polymorphonuclear leukocytes. J Biol Chem. 1985;260:2237-2244.
33. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
34. Chirgwin JM, Przybyla AE, MacDonald RJ, Flutter WJ. Isolation of biological active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979;18:5294-5299.
35. Bolscher BGJM, de Boer M, de Klein A, Weening RS, Roos D. Point mutations in the beta-subunit of cytochrome b558 leading to X-linked chronic granulomatous disease. Blood. 1991;77:2482-2487.
36. de Boer M, Bolscher BGJM, Sijmons RH, Scheffer H, Weening RS, Roos D. Prenatal diagnosis in a family with X-linked chronic granulomatous disease with the use of the polymerase chain reaction. Prenat Diagn. 1992;12:773-777.
37. de Boer M, Bolscher BQJM, Dinauer MC, et al. Splice site mutations are a common cause of X-linked chronic granulomatous disease. Blood. 1992;80:1553-1558.
38. Roos D, de Boer M. Purification and cryopreservation of phagocytes from human blood. In: Di Sabato G, Everse J, eds. Immunochemical Techniques Part J Phagocytosis and Cell-Mediated Cytotoxicity. Methods Enzymol. Vol 132. New York, NY: Academic Press; 1986:225-243.
39. Leusen JHW, Bolscher BGJM, Hilarius PM, et al. 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. 1994;180:2329-2334.
40. Leusen JHW, de Klein A, Hilarius PM, et al. Disturbed interaction of p21-rac with mutated p67-phox causes chronic granulomatous disease. J Exp Med 1996;184:1243-1249.
41. Koshkin V, Pick E. Generation of Superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators. FEBS Lett. 1993; 327:57-62.
42. Lu G: A WWW service system for automatic comparison of protein structures. Protein Data Bank Newsletter. 1996;78:10-11.
43. Finegold AA, Shatwell KP, Segal AW, Klausner RD, Dancis A. Intrarnembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase. J Biol Chem. 1996;271:31,021-31,024.
44. + reductase family? J Biol Chem. 1996; 271:16,656-16,661.
45. + reductase: prototype for a structurally novel flavoenzyme family. Science. 1991;251:60-66.
46. Bruns CM, Karplus PA. Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: oxidized, reduced and 2′-phospho-5′-AMP bound states. J Mol Biol. 1995;247:125-145.
47. + reductase: structure-function relationship as studied by site-directed mutagenesis and X-ray crystallography. Biochemistry. 1995;34:8371-8379.
48. Correll CC, Ludwig ML, Bruns CM, Karplus PA. Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Sci. 1993;2:2112-2133.
49. 558 using site-directed mutagenesis. J Biol Chem. 1998;273:6575-6581.
50. Quinn MT, Mullen ML, Jesaitis AJ. Human neutrophil cytochrome b contains multiple hemes: evidence for heme associated with both subunits. J Biol Chem. 1992;267:7303-7309.
51. 558 of the human NADPH oxidase. J Biol Chem. 1998.273:27,879-27,886.
52. Smith RM, Connor JA, Chen LM, Babior BM. The cytosolic subunit p67phox contains an NADPH binding site that participates in catalysis by the leukocyte NADPH oxidase. J Clin Invest. 1996; 98:977-983.
53. 558. J Biol Chem. 1990;265:8745-8750.
54. 558 91-kilodalton subunit functional domain: identification of peptide sequence and amino acids essential for activity. Biochemistry. 1992;31:2686-2690.
55. DeLeo FR, Nauseef WM, Jesaitis AJ, Burritt JB, Clark RA, Quinn MT. A domain of p47phox that interacts with human neutrophil flavocytochrome b558. J Biol Chem. 1995;270:26,246-26,251.
56. Zhen L, King AA, Xiao Y, Chanock SJ, Orkin SH, Dinauer MC. Gene targeting of X chromosome-linked chronic granulomatous disease locus in a human myeloid leukemia cell line and rescue by expression of recombinant gp91phox. Proc Natl Acad Sci U S A. 1993;90:9832-9836.
57. + reductase. In: Stevenson KJ, Massey V, Williams CH Jr, eds. Flavins and Flavoproteins XII. Calgary, Canada: University Press; 1997:509-512.
58. + reductase from Anabaena PCC 7119. Biochemistry. 1998;37:2715-2728.
59. Sridhar Prasad G, Kresge N, Muhlberg AB, et al. The crystal structure of NADPH: ferredoxin reductase from Azotobacter vinelandii. Protein Sci. 1998;7:2541-2549.
60. Serre L, Vellieux FMD, Medina M, Gomez-Moreno C, Fontecilla-Camps JC, Frey M. X-ray structure of the ferredoxin NADP reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution and crystallographic studies of NADP binding at 2.25 Å resolution. J Mol Biol. 1996;263:20-39.
61. Lu G, Campbell WH, Schneider G, Lindqvist Y. Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 Å resolution: relationship to other flavoprotein reductases. Structure. 1994;2:809-821.
62. Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K. Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 Å resolution. Biochemistry. 1995;34:2763-2767.
63. Ermler U, Siddiqui RA, Gramm R, Friedrich B. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 1995;14:6067-6077.
64. Ingelman M, Bianchi V, Eklund H. The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution. J Mol Biol. 1997;268:147-157.
65. Carson M. Ribbons 2.0. J Appl Crystallogr. 1991; 24:958-961.