Abstract
When pathogens invade the body, neutrophils create the first line of defense. Basic weaponry consists of phagocytosis and degranulation, but these cells have yet another ace in the sleeve, a unique strategy in which invading microorganisms are being destroyed. These cellular warriors are able to release nuclear chromatin and form extracellular structure, known as neutrophil extracellular traps (NET). NET formation is connected with the presence of free radicals. Research has shown that inhibition of free radical formation leads to suppression of NET release. The exact mechanisms controlling cooperation of free radicals with NET still remain unclear. New investigations in this field may contribute to discovery of NET etiology and put a new light on related disorders.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Akong-Moore K, Chow OA, von Köckritz-Blickwede M, Nizet V (2012) Influences of chloride and hypochlorite on neutrophil extracellular trap formation. PLoS One 7:e42984. doi:10.1371/journal.pone.0042984
Brinkmann V, Reichard U, Goosmann C, Fauler B, Uhlemann Y, Weiss DS, Weinrauch Y, Zychlinsky A (2004) Neutrophil extracellular traps kill bacteria. Science 303:1532–1535
Hansson M, Olsson I, Nauseef WM (2006) Biosynthesis, processing, and sorting of human myeloperoxidase. Arch Biochem Biophys 445:214–224
Imada I, Sato EF, Miyamoto M, Ichimori Y, Minamiyama Y, Konaka R, Inoue M (1999) Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012. Anal Biochem 271:53–58
Keshari RS, Jyoti A, Dubey M, Kothari N, Kohli M, Bogra J, Barthwal MK, Dikshit M (2012) Cytokines induced neutrophil extracellular traps formation: implication for the inflammatory disease condition. Clin Exp Immunol 168:153–163
Kirchner T, Möller S, Klinger M, Solbach W, Laskay T, Behnen M (2012) The impact of various reactive oxygen species on the formation of neutrophil extracellular traps. Mediators Inflamm 2012:1615–1623
Lushchak VI (2007) Free radical oxidation of proteins and its relationship with functional state of organisms. Biochem Mosc 72:809–827
Marcos V, Zhou Z, Yildirim AO, Bohla A, Hector A, Vitkov L, Wiedenbauer EM, Krautgartner WD, Stoiber W, Belohradsky BH, Reiber N, Kormann M, Koller B, Roscher A, Roos D, Griese M, Eickelberg O, Doring G, Mall MA, Harti D (2010) CXCR2 mediates NADPH oxidase-independent neutrophil extracellular trap formation in cystic fibrosis airway inflammation. Nat Med 16:1018–1023
Metzler KD, Fuchs TA, Nauseef WM, Reumaux D, Roesler J, Schulze I, Wahn V, Papayannopoulos V, Zychlinsky A (2011) Myeloperoxidae is required for neutrophil extracellular trap formation: implications for innate immunity. Blood 117:953–959
Nakaya H, Takeda Y, Tohse N, Kanno M (1992) Mechanism of the membrane depolarization induced by oxidative stress in guinea-pig ventricular cells. J Mol Cell Cardiol 24:523–534
Nishinaka Y, Arai T, Adachi S, Takaori–Konodo A, Yamashita K (2011) Singlet oxygen is essential for neutrophil extracellular trap formation. Biochem Biophys Res Commun 413:75–79
Palmer LJ, Cooper PR, Ling MR, Wright HJ, Huissoon A, Chapple IL (2012) Hypochlorous acid regulates neutrophil extracellular trap release in humans. Clin Exp Immunol 167:261–268
Papayannopoulos V, Metzler KD, Hakkim A, Zychlinsky A (2010) Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps. J Cell Biol 191:677–691
Patel S, Kumar S, Jyoti A, Srinag BS, Keshari RS, Saluja R, Verma A, Mitra K, Barthwal MK, Krishnamurthy H, Bajpai VK, Dikshit M (2010) Nitric oxide donors release extracellular traps from human neutrophils by augmenting free radical generation. Nitric Oxide 22:226–234
Petrides PE (1998) Molecular genetics of peroxidase deficiency. J Mol Med 76:688–698
Pruchniak MP, Arazna M, Demkow U (2013) Life of neutrophil: from stem cell to neutrophil extracellular trap. Respir Physiol Neurobiol 187:68–73
Qui H, Edmunds T, Baker-Malcolm J, Karey KP, Estes S (2003) Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine. J Biol Chem 278:32744–32752
Remijsen Q, Berghe TV, Wirawan E, Asselbergh B, Parthoens E, De Rycke R, Noppen S, Delforge M, Willems J, Vandenabeele P (2011) Neutrophil extracellular trap cell death requires both autophagy and superoxide generation. Cell Res 21:290–304
Sawada M, Nakashima S, Kiyono T, Nakagawa M, Yamada J, Yamakawa H, Banno Y, Shinoda J, Nishimura Y, Nozawa Y, Sakai N (2001) p53 regulates ceramide formation by neutral sphingomyelinase through reactive oxygen species in human glioma cells. Cell Death Differ 11:853–861
Scheel-Toellner D, Wang K, Craddock R, Webb PR, McGettrick HM, Assi LK, Parkes N, Clough LE, Gulbins E, Salmon M, Lord JM (2004) Reactive oxygen species limit neutrophil life span by activating death receptor signaling. Blood 104:2557–2564
Takei H, Araki A, Watanabe H, Ichinose A, Sendo F (1996) Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetate (PMA) accompanied by changes different from typical apoptosis or necrosis. J Leukoc Biol 59:229–240
Tsan MF (1980) Phorbol myristate acetate induced neutrophil autotoxicity. J Cell Physiol 105:327–334
Yipp BG, Kubes P (2013) Netosis: how vital is it? Blood 122:2784–2794
Conflicts of Interest
The authors declare no conflicts of interest in relation this article.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer International Publishing Switzerland
About this chapter
Cite this chapter
Araźna, M., Pruchniak, M.P., Demkow, U. (2014). Reactive Oxygen Species, Granulocytes, and NETosis. In: Pokorski, M. (eds) Respiratory Virology and Immunogenicity. Advances in Experimental Medicine and Biology(), vol 836. Springer, Cham. https://doi.org/10.1007/5584_2014_12
Download citation
DOI: https://doi.org/10.1007/5584_2014_12
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-10017-3
Online ISBN: 978-3-319-10018-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)