Beneficial suicide: Why neutrophils die to make NETs

Nature Reviews Microbiology

Volumn 5, Issue 8, 2007, Pages 577-582

  Brinkmann, Volke ^a   Zychlinsky, Arturo ^a  

^a MAX PLANCK INSTITUTE FOR INFECTION BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE; HISTONE; HISTONE H2A; HYDROGEN PEROXIDE; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL VIRULENCE; CELL DEATH; CHEMICAL STRUCTURE; CHROMATIN; CHRONIC GRANULOMATOUS DISEASE; FERTILIZATION; FUNGUS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; GRANULOCYTE; HUMAN; INFECTION CONTROL; INNATE IMMUNITY; INTRACELLULAR KILLING; NECROTIZING FASCIITIS; NEUTROPHIL; NEUTROPHIL CHEMOTAXIS; NONHUMAN; PHAGOCYTOSIS; PREECLAMPSIA; PRIORITY JOURNAL; SEPSIS; STREPTOCOCCUS PNEUMONIAE;

ANIMALS; BACTERIA; CATTLE; CELL DEATH; CHROMATIN; COMMUNICABLE DISEASES; EXTRACELLULAR SPACE; FUNGI; HUMANS; IMMUNITY, NATURAL; MICE; MICROSCOPY, ELECTRON; NEUTROPHIL ACTIVATION; NEUTROPHILS; RABBITS;

EID: 34447525439     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1710     Document Type: Article

References (39)

1. Bainton, D. F., Ullyot, J. L & Farquhar, M. G. The development of neutrophilic polymorphonuclear leukocytes in human bone marrow: Origin and content of azurophil and specific granules. J. Exp. Med. 134, 907-934 (1971).
2. Nathan, C. Neutrophils and immunity: Challenges and opportunities. Nature Rev. Immunol. 6, 173-182 (2006).
3. Borregaard, N., Sehested, M., Nielsen, B. S., Sengelov, H. & Kjeldsen, L. Biosynthesis of granule proteins in normal human bone-marrow cells - gelatinase is a marker of terminal neutrophil differentiation. Blood 85, 812-817 (1995).
4. Borregaard, N. & Cowland, J. B. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 89, 3503-3521 (1997).
5. Delves, P. J. & Roitt, I. M. The immune system-first of two parts. New Engl. J. Med. 343, 37-49 (2000).
6. Metchnikoff, E. Llimmunité Dans Les Maladies Infectieuses (Masson and Cie, Paris, 1901).
7. Coxon, A. et al. A novel role for the β-2 integrin CD11b/CD18 in neutrophil apoptosis: A homeostatic mechanism in inflammation. Immunity 5, 653-666 (1996).
8. Zhang, B., Hirahashi, J., Cullere, X. & Mayadas, T. N. Elucidation of molecular events leading to neutrophil apoptosis following phagocytosis: cross-talk between caspase 8, reactive oxygen species, and MAPK/ERK activation. J. Biol. Chem. 278, 28443-28454 (2003).
9. Serhan, C. N. & Savill, J. Resolution of inflammation: The beginning programs the end. Nature Immunol. 6, 1191-1197 (2005).
10. Haslett, C. Granulocyte apoptosis and inflammatory disease. Br. Med. Bull. 53, 669-683 (1997).
11. Lehrer. R. I. & Ganz, T. Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27 (1999).
12. Hampton, M. B., Kettle, A. J. & Winterbourn, C. C. Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing. Blood 92, 3007-3017 (1998).
13. Heyworth, P. G., Cross, A. R. & Curnutte, J. T. Chronic granulomatous disease. Curr. Opin. Immunol. 15, 578-584 (2003).
14. Brinkmann, V. et al. Neutrophil extracellular traps kill bacteria. Science 303, 1532-1535 (2004).
15. Clark, S. R. et al. Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood. Nature Med. 13, 463-469 (2007).
16. Fuchs, T. A. et al. Novel cell death program leads to neutrophil extracellular traps. J. Cell Biol. 176, 231-241 (2007).
17. Droge, W. Free radicals in the physiological control of cell function. Physiol. Rev. 82, 47-95 (2002).
18. Tonks, N. K. Redox redux: Revisiting PTPs and the control of cell signaling. Cell 121, 667-670 (2005).
19. Steinberg. B. E. & Grienstein, S. Unconventional roles of the NADPH oxidase: Signaling, ion homeostasis, and cell death. Sci. STKE pe11 (2007).
20. Buchanan, J. T. et al. DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps. Curr. Biol. 16. 396-400 (2006).
21. Beiter, K. et al. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellolar traps. Curr. Biol. 16, 401-407 (2006).
22. Wartha, F. et al. Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cell. Microbial. 9, 1162-1171 (2007).
23. Urban, C. F.. Reichard, U., Brinkmann, V. & Zychlinsky, A. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell. Microbiol. 8, 668-676 (2006).
24. Hirsch, J. G. Bactericidal action of histone. J. Exp. Med. 108 925-944 (1958).
25. Cho, J. H. et al. Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. FASEB J. 16. 429-431 (2002).
26. Kim, H. S., Park, C. B., Kim, M. S. & Kim, S. C. cDNA cloning and characterization of buforin I, an antimicrobial peptide: A cleavage product of histone H2A. Biochem. Biophys. Res. Commun. 229, 381-387 (1996).
27. Kim, H. S. et al. Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I. J. Immunol. 165, 3268-3274 (2000).
28. Park, C. B., Yi, K. S., Matsuzaki, K., Kim, M. S. & Kim, S. C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl Acad. Sci. USA 97, 8245-8250 (2000).
29. Patat, S. A. et al. Antimicrobial activity of histones from hemocytes of the Pacific white shrimp. Eur. J. Biochem. 271. 4825-4833 (2004).
30. Sumby, P. et al. Extracellular deoxyribonuclease made by group A Streptococcus assists pathogenesis by enhancing evasion of the innate immune response. Proc. Natl Acad. Sci. USA 102, 1679-1684 (2005).
31. Cupta, A. K., Hasler, P., Holzgreve, W, Gebhardt, S. & Hahn, S. Induction of neutrophil extracellular DNA lattices by placental microparticles and IL-8 and their presence in preeclampsia. Hum. Immunol. 66, 1146-1154 (2005).
32. Alghamdi, A. S. & Foster, D. N. Seminal DNase frees spermatozoa entangled in neutrophil extracellular traps. Biol. Reprod. 73 1174-1181 (2005).
33. Lippolis, J. D., Reinhardt, T. A., Goff. J. P. & Horst, R. L. Neutrophil extracellular trap formation by bovine neutrophils is not inhibited by milk. Vet. Immunol. Immunopathol. 113, 248-255 (2006).
34. Palic, D., Andreasen, C. B., Ostojic, J., Tell, R. M. & Roth, J. A. Zebrafish (Danio rerio) whole kidney assays to measure neutrophil extracellular trap release and degranulation of primary granules. J. Immunol. Meth. 319, 87-97 (2007).
35. Fairhurst, A. M., Wandstrat, A. E. & Wakeland, E. K. Systemic lupus erythematosus: Multiple immunological phenotypes in a complex ganetic disease. Adv. Immunol. 92, 1-69 (2006).
36. Duranton, J. et al. Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA. FEBS Lett. 473, 154-156 (2000).
37. McCauley, T. C., Zhang, H. M., Bellin, M. E. & Ax, R. L. Purification and characterization of fertility-associated antigen (FAA) in bovine seminal fluid. Mol. Reprod. Dev. 54, 145-153 (1999).
38. Zhong, X. Y. et al. Elevation of both maternal and fetal extracellular circulating deoxyribonucleic acid concentrations in the plasma of pregnant women with preeclampsia. Am. J. Obst. Gynecol. 184, 414-419 (2001).
39. Redman, C. W. & Sargent, I. L. Latest advances in understanding preeclampsia. Science 308, 1592-1594 (2005).