Oxidative killing of microbes by neutrophils

Microbes and Infection

Volumn 5, Issue 14, 2003, Pages 1307-1315

  Roos, Dirk ^a   Van Bruggen, Robin ^a   Meischl, Christof ^a,b  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b VU UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

Chronic granulomatous disease; Killing; Microbes; NADPH oxidase; Neutrophils

Indexed keywords

GLYCOPROTEIN; ISOPROTEIN; PROTEIN P40; PROTEIN P47; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

CHRONIC DISEASE; CLINICAL FEATURE; CORRELATION ANALYSIS; DEATH; ENZYME ACTIVATION; ENZYME ACTIVITY; GENOTYPE; GRANULOMATOSIS; MICROORGANISM; MOLECULAR DYNAMICS; NEUTROPHIL; NONHUMAN; OXIDATION; PHAGOCYTOSIS; PHENOTYPE; PRIORITY JOURNAL; REVIEW;

EID: 0242460542     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micinf.2003.09.009     Document Type: Review

References (31)

1. Roos D., Curnutte J.T. Chronic Granulomatous Disease. Ochs H.D., Smith C.I.E., Puck J.M. Primary Immunodeficiency Diseases. A Molecular and Genetic Approach. 1999;353-374 Oxford University Press, New York, Oxford.
2. + flux. Nature. 416:2002;291-297.
3. Ambruso D.R., Knall C., Abell A.N., Panepinto J., Kurkchubasche A., Thurman G., Gonzalez-Aller C., Hiester A., de Boer M., Harbeck R.J., Oyer R., Johnson G.L., Roos D. Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc. Natl. Acad. Sci. USA. 97:2000;4654-4659.
4. Abo A., Pick E., Hall A., Totty N.N., Teahan C.G., Segal A.W. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature. 353:1991;668-670.
5. Knaus U.G., Heyworth P.G., Evans T., Curnutte J.T., Bokoch G.M. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2. Science. 254:1991;1512-1515.
6. βγ-regulated guanine-nucleotide exchange factor for Rac. Cell. 108:2002;809-821.
7. Gabig T.G., Crean C.D., Mantel P.L., Rosli R. Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated HL60 cell NADPH oxidase activation. Blood. 85:1995;804-811.
8. phox of neutrophil NADPH oxidase. Biochem. Biophys. Res. Commun. 276:2000;1186-1190.
9. 2 for activation of the phagocyte NADPH oxidase. J. Biol. Chem. 273:1998;441-445.
10. Heyworth P.G., Curnutte J.T., Rae J., Noack J.D., Roos D., van Koppen E., Cross A.R. Hematologically important mutations: X-linked chronic granulomatous disease (second update). Blood Cells Mol. Dis. 27:2001;16-26.
11. phox gene in human peripheral neutrophils, monocytes, and B lymphocytes. Proc. Natl. Acad. Sci. USA. 95:1998;6085-6090.
12. phox gene expression by transcription factors GATA-1 and GATA-2. J. Biol. Chem. 275:2000;9425-9432.
13. Cross A.R., Noack D., Rae J., Curnutte J.T., Heyworth P.G. Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease (first update). Blood Cells Mol. Dis. 26:2000;561-565.
14. phox causes chronic granulomatous disease. J. Exp. Med. 184:1996;1243-1249.
15. Foster C.B., Lehrnbecher T., Mol F., Steinberg S.M., Venzon D.J., Walsh T.J., Noack D., Rae J., Winkelstein J.A., Curnutte J.T., Chanock S.J. Host defense molecule polymorphisms influence the risk for immune-mediated complications in chronic granulomatous disease. J. Clin. Invest. 102:1998;2146-2155.
16. Segal A.W., Geisow M., Garcia R., Harper A., Miller R. The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH. Nature. 290:1991;406-409.
17. phoxG. J. Gen. Physiol. 120:2002;759-765.
18. Roos D., Winterbourn C.C. Lethal weapons. Science. 296:2002;669-671.
19. Ehrt S., Shiloh M.U., Ruan J., Choi M., Gunzburg S., Nathan C., Xie Q.-W., Riley L.W. A novel antioxidant gene from Mycobacterium tuberculosisG. J. Exp. Med. 186:1997;1885.
20. Vazquez-Torres A., Xu Y., Jones-Carson J., Holden D.W., Lucia S.M., Dinauer M.C., Mastroeni P., Fang F.C. Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase. Science. 287:2000;1655-1658.
21. Gallois A., Klein J.R., Allen L.A., Jones B.D., Nauseef W.M. Salmonella pathogenicity island 2-encoded type III secretion system mediates exclusion of NADPH oxidase assembly from phagosomal membrane. J. Immunol. 166:2001;5741-5748.
22. Carlyon J.A., Chan W.-T., Galán J., Roos D., Fikrig E. Repression of rac2 mRNA expression by Anaplasma phagocytophila is essential to the inhibition of superoxide production and bacterial proliferation. J. Immunol. 169:2002;7009-7018.
23. van Heerebeek L., Meischl C., Stooker W., Meijer C.J.L.M., Niessen H.W.M., Roos D. NADPH oxidase(s): new source(s) of reactive oxygen species in the vascular system? J. Clin. Pathol. 55:2002;561-568.
24. 558 molecules involved in the fibroblast and polymorphonuclear leukocyte superoxide-generating NADPH oxidase systems are structurally and genetically distinct. Biochem. J. 289:1993;481-486.
25. Suh Y.A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B., Griendling K.K., Lambeth J.D. Cell transformation by the superoxide-generating oxidase Mox1. Nature. 401:1999;79-82.
26. Geiszt M., Kopp J.B., Varnai P., Leto T.L. Identification of renox, an NAD(P)H oxidase in the kidney. Proc. Natl. Acad. Sci. USA. 97:2000;8010-8014.
27. Banfi B., Clark R.A., Steger K., Krause K.-H. Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J. Biol. Chem. 278:2003;3510-3513.
28. phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J. Biol. Chem. 278:2003;20006- 20012.
29. de Deken X., Wang D., Many M.C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275:2000;23227-23233.
30. Blouin E., Halbwachs-Mecarelli L., Rieu P. Redox regulation of β2-integrin CD11b/CD18 activation. Eur. J. Immunol. 29:1999;3419-3431.
31. Meischl C., Roos D. The molecular basis of chronic granulomatous disease. Springer Semin. Immunopathol. 19:1998;417-434.