A Myeloperoxidase-Containing Complex Regulates Neutrophil Elastase Release and Actin Dynamics during NETosis
Open accessAbstract
Neutrophils contain granules loaded with antimicrobial proteins and are regarded as impermeable organelles that deliver cargo via membrane fusion. However, during the formation of neutrophil extracellular traps (NETs), neutrophil elastase (NE) translocates from the granules to the nucleus via an unknown mechanism that does not involve membrane fusion and requires reactive oxygen species (ROS). Here, we show that the ROS triggers the dissociation of NE from a membrane-associated complex into the cytosol and activates its proteolytic activity in a myeloperoxidase (MPO)-dependent manner. In the cytosol, NE first binds and degrades F-actin to arrest actin dynamics and subsequently translocates to the nucleus. The complex is an example of an oxidative signaling scaffold that enables ROS and antimicrobial proteins to regulate neutrophil responses. Furthermore, granules contain protein machinery that transports and delivers cargo across membranes independently of membrane fusion.
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Cytosolic ELANE catalyzes proteolysis of F-actin, followed by impairment of cytoskeleton dynamics.
“the cytosolic pool of ELANE would catalyze the proteolysis of F-actin, followed by an impairment of cytoskeleton dynamics [741].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [741]
Cathepsin G may have a similar role to neutrophil elastase in NET release.
“Cleavage of histones by neutrophil elastase is required for chromatin de-condensation and NET release (28, 29), and cathepsin G may have a similar role.”
From Cancer cells induce metastasis-supporting neutrophil extracellular DNA traps (2016) · cites this paper as [29]
Cleavage of histones by neutrophil elastase is required for chromatin de-condensation and NET release.
“Cleavage of histones by neutrophil elastase is required for chromatin de-condensation and NET release (28, 29), and cathepsin G may have a similar role.”
From Cancer cells induce metastasis-supporting neutrophil extracellular DNA traps (2016) · cites this paper as [29]
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Manfredi, A. A., Ramirez, G. A., Rovere, P. Q., & Maugeri, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00288 · Cited by 220 · see citing works
“The existence of independent pathways leading to the generation of NETs endowed with potent biological action in the microenvironment that might compensate one for the other (13, 19, 182) supports the evolutionary importance of neutrophil activation.”
BackgroundPieterse, E., Rother, N., Yanginlar, C., Hilbrands, L. B., & van der Vlag, J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00484 · Cited by 214 · see citing works
“As an explanation for this observation, it can be hypothesized that LPS-exposed platelets are internalized by neutrophils, thereby delivering NE to phagosomes and sequestering NE from the nucleus, which in turn inhibits “suicidal” NETosis since nuclear elastase is required in this pathway (18, 19).”
BackgroundNeutrophil intrinsic and extrinsic regulation of NETosis in health and disease
Poli, V., & Zanoni, I. (2022) · Trends in Microbiology · doi:10.1016/j.tim.2022.10.002 · Cited by 217 · see citing works
The role of neutrophils in host defense and disease
Lehman, H. K., & Segal, B. H. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.02.038 · Cited by 218 · see citing works
Cell death in the pathogenesis of systemic lupus erythematosus and lupus nephritis
Mistry, P., & Kaplan, M. J. (2016) · Clinical Immunology · doi:10.1016/j.clim.2016.08.010 · Cited by 207 · see citing works
Chapman, E. A., Lyon, M., Simpson, D. M., Mason, D. Y., Beynon, R. J., Moots, R. J., & Wright, H. L. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00423 · Cited by 205 · see citing works
“Elastase does not seem to be required for NOX2-independent NETosis (30), and neither are F-actin or histones cleaved (23, 31).”
BackgroundNeutrophil extracellular traps: protagonists of cancer progression?
Erpenbeck, L., & Schön, M. P. (2017) · Oncogene · doi:10.1038/onc.2016.406 · Cited by 199 · see citing works
Immune Evasion byStaphylococcus aureus
de Jong, N. W. M., van Kessel, K. P. M., & van Strijp, J. A. G. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0061-2019 · Cited by 200 · see citing works
“There are current studies to address the molecular mechanism behind NET formation, but more research is needed to fully understand this phenomenon (142).”
BackgroundOkeke, E. B., Louttit, C., Fry, C., Najafabadi, A. H., Han, K., Nemzek, J. A., & Moon, J. J. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.119836 · Cited by 196 · see citing works
“Activated GSDMD perforates the granule membrane, increasing the release of NE and enabling the translocation of NE to the nucleus, where it processes histones and allows nuclear expansion [40,64].”
BackgroundExtracellular DNA NET-Works With Dire Consequences for Health
Sorvillo, N., Cherpokova, D., Martinod, K., & Wagner, D. D. (2019) · Circulation Research · doi:10.1161/circresaha.119.314581 · Cited by 196 · see citing works
Martinod, K., Witsch, T., Farley, K., Gallant, M., Remold‐O'Donnell, E., & Wagner, D. D. (2016) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.13239 · Cited by 188 · see citing works
Extracellular DNA traps in inflammation, injury and healing
Daniel, C., Leppkes, M., Munoz, L. E., Schley, G., Schett, G. A., & i, M. H. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0163-2 · Cited by 189 · see citing works
The emerging roles of neutrophil extracellular traps in wound healing
Zhu, S.-N., Yu, Y., Ren, Y., Xu, L.-Y., Wang, H., Ling, X.-M., Jin, L., Hu, Y., Zhang, H., Miao, C., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04294-3 · Cited by 174 · see citing works
Neutrophil Extracellular Traps in Host DefensePreprint
Burgener, S. S., & Schroder, K. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a037028 · Cited by 193 · see citing works
“This induces the release of NE into the cytosol through an unclear mechanism that requires MPO activity within the cell (Metzler et al. 2014).”
BackgroundInfluentialNeutrophil-Mediated Regulation of Innate and Adaptive Immunity: The Role of Myeloperoxidase
Odobasic, D., Kitching, A. R., & Holdsworth, S. R. (2016) · Journal of Immunology Research · doi:10.1155/2016/2349817 · Cited by 191 · see citing works
“Together with elastase, MPO has been demonstrated to associate with nuclear DNA/histones and play a role in NET formation as well as NET-mediated bacterial killing [38–40].”
InfluentialNeutrophil Extracellular Traps and Cardiovascular Diseases: An Update
Bonaventura, A., Vecchié, A., Abbate, A., & Montecucco, F. (2020) · Cells · doi:10.3390/cells9010231 · Cited by 190 · see citing works
“Once GSDMD activates, it is able to form pores in the membrane of granules favoring NE release into the cytoplasm toward the nucleus, where it gets processed with histones and increases nuclear expansion [91].”
BackgroundBjörnsdóttir, H., Welin, A., Michaëlsson, E., Osla, V., Berg, S., Christenson, K., Sundqvist, M., Dahlgren, C., Karlsson, A., & Bylund, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.398 · Cited by 183 · see citing works
Reactive Oxygen Species Localization Programs Inflammation to Clear Microbes of Different Size
Warnatsch, A., Tsourouktsoglou, T.-D., Branzk, N., Wang, Q., Reincke, S., Herbst, S., Gutierrez, M. G., & Papayannopoulos, V. (2017) · Immunity · doi:10.1016/j.immuni.2017.02.013 · Cited by 183 · see citing works
“To test this hypothesis, we employed mice deficient in the ROS-producing enzyme myeloperoxidase (MPO) that is required for NET formation (Branzk et al., 2014; Kolaczkowska et al., 2015; Metzler et al., 2011, 2014; Papayannopoulos et al., 2010).”
MethodSelf-citationNeutrophils and redox stress in the pathogenesis of autoimmune disease
Glennon-Alty, L., Hackett, A. P., Chapman, E. A., & Wright, H. L. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.049 · Cited by 181 · see citing works
Platelets: New Bricks in the Building of Neutrophil Extracellular Traps
Carestia, A., Kaufman, T., & Schattner, M. A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00271 · Cited by 183 · see citing works
“After disintegration of the nuclear envelope and rupture of the cytoplasmic membrane, NETs are released (19, 20).”
BackgroundRoles of neutrophil granule proteins in orchestrating inflammation and immunity
Othman, A., Sekheri, M., & Filep, J. G. (2021) · FEBS Journal · doi:10.1111/febs.15803 · Cited by 184 · see citing works
Novel findings in neutrophil biology and their impact on cardiovascular disease
Bonaventura, A., Montecucco, F., Dallegri, F., Carbone, F., Lüscher, T. F., Camici, G. G., & Liberale, L. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz084 · Cited by 173 · see citing works
Neutrophil extracellular traps enhance macrophage killing of bacterial pathogens
Monteith, A. J., Miller, J. M., Maxwell, C. N., Chazin, W., & Skaar, E. P. (2021) · Science Advances · doi:10.1126/sciadv.abj2101 · Cited by 167 · see citing works
“Release of enzymes from primary granules into the cytosol is a precursor to NETosis ( 45 , 46 ); therefore, reduced primary degranulation could imply elevated NETosis.”
The roles of NADPH oxidase in modulating neutrophil effector responses
Zeng, M. Y., Miralda, I., Armstrong, C. L., Uriarte, S. M., & Bagaitkar, J. (2019) · Molecular Oral Microbiology · doi:10.1111/omi.12252 · Cited by 173 · see citing works
Frangou, E. A., Vassilopoulos, D., Boletis, J., & Boumpas, D. T. (2019) · Autoimmunity Reviews · doi:10.1016/j.autrev.2019.06.011 · Cited by 171 · see citing works
The pathway of neutrophil extracellular traps towards atherosclerosis and thrombosis
Moschonas, I. C., & Tselepis, A. D. (2019) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2019.06.919 · Cited by 166 · see citing works
Untangling “NETosis” from NETs
Yousefi, S., Stojkov, D., Germič, N., Simon, D., Wang, X., Benarafa, C., & Simon, H. (2019) · European Journal of Immunology · doi:10.1002/eji.201747053 · Cited by 160 · see citing works
Menegazzo, L., Scattolini, V., Cappellari, R., Bonora, B. M., Albiero, M., Bortolozzi, M., Romanato, F., Ceolotto, G., de Kreutzeberg, S. V., Avogaro, A., et al. (2018) · Acta Diabetologica · doi:10.1007/s00592-018-1129-8 · Cited by 162 · see citing works
The role of neutrophils in the pathogenesis of systemic lupus erythematosus
Smith, C. K., & Kaplan, M. J. (2015) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000000197 · Cited by 155 · see citing works
Lazzaretto, B., & Fadeel, B. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1800159 · Cited by 146 · see citing works
“The mechanisms of NET formation have been studied in considerable detail (70, 71), but less is known about the interplay between NETs and other immune-competent cells and, in particular, regarding the clearance of these extracellular structures.”
BackgroundWong, S. L., & Wagner, D. D. (2018) · The FASEB Journal · doi:10.1096/fj.201800691r · Cited by 145 · see citing works
“Neutrophil elastase (17, 18), together with other proteases (19), contributes to NETosis by cleaving histones to unfold chromatin.”
BackgroundROS and glutathionylation balance cytoskeletal dynamics in neutrophil extracellular trap formation
Stojkov, D., Amini, P., Oberson, K., Sokollik, C., Duppenthaler, A., Simon, H.-U., & Yousefi, S. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201611168 · Cited by 142 · see citing works
“Moreover, neutrophil elastase has been reported to promote F-actin degradation, liberating the protease to enter the nucleus (Metzler et al., 2014).”
BackgroundRelief of tumor hypoxia unleashes the tumoricidal potential of neutrophils
Mahiddine, K., Blaisdell, A., Ma, S., Créquer-Grandhomme, A., Lowell, C. A., & Erlebacher, A. (2019) · Journal of Clinical Investigation · doi:10.1172/jci130952 · Cited by 140 · see citing works
“A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis.”
BackgroundNeutrophil Activated by the Famous and Potent PMA (Phorbol Myristate Acetate)
Damascena, H. L., Silveira, W. A. A., Castro, M. S., & Fontes, W. (2022) · Cells · doi:10.3390/cells11182889 · Cited by 138 · see citing works
Yan, H., Zhou, H., Akk, A. M., Hu, Y., Springer, L. E., Ennis, T. L., & Pham, C. T. N. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.116.307786 · Cited by 137 · see citing works
“It is thought that NE translocation to the nucleus, where it partially degrades specific histones and promotes chromatin decondensation, represents an essential step in NET formation.(24,25) Recent studies, however, suggest that NE is dispensable for NET formation in mice,(44) corroborating our findings.”
ResultThe Role of Neutrophil NETosis in Organ Injury: Novel Inflammatory Cell Death Mechanisms
Cahilog, Z., Zhao, H., Wu, L., Alam, A., Eguchi, S., Weng, H., & Ma, D. (2020) · Inflammation · doi:10.1007/s10753-020-01294-x · Cited by 136 · see citing works
Johnson, C. J., Cabezas‐Olcoz, J., Kernien, J. F., Wang, S. X., Beebe, D. J., Anna Huttenlocher, A., Ansari, H., & Nett, J. E. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005884 · Cited by 132 · see citing works
“The generation of ROS and its subsequent processing by myeloperoxidase are key steps in production of NETs [33, 34].”
Histone Acetylation Promotes Neutrophil Extracellular Trap Formation
Hamam, H. J., Khan, M. A., & Palaniyar, N. (2019) · Biomolecules · doi:10.3390/biom9010032 · Cited by 133 · see citing works
“During NET formation (NETosis), increased intracellular levels of reactive oxygen species (ROS) promote pathway-specific kinase activation, promoter melting, transcriptional firing, extensive chromatin decondensation and eventual NET release [3,6,7].”
BackgroundEosinophil extracellular traps drive asthma progression through neuro-immune signals
Lu, Y., Huang, Y.-J., Jiang, L., Huang, J., Zhang, L., Feng, J., Li, J., Xia, Q., Zhao, Q., Huang, L., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00762-2 · Cited by 133 · see citing works
The Neutrophil Nucleus: An Important Influence on Neutrophil Migration and Function
Manley, H. R., Keightley, M.-C., & Lieschke, G. J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02867 · Cited by 131 · see citing works
“Actin polymerisation is modulated by myeloperoxidase and neutrophil elastase, with a myeloperoxidase-containing granule protein complex called the “azurosome” mediating neutrophil elastase nuclear translocation that ultimately inhibits actin extension into the cytoplasm (151).”
BackgroundUnraveling Cell Death Pathways during Malaria Infection: What Do We Know So Far?
Sena-dos-Santos, C., Braga-da-Silva, C., Marques, D., Pinheiro, J. A. D. S., Ribeiro‐dos‐Santos, Â., & Cavalcante, G. C. (2021) · Cells · doi:10.3390/cells10020479 · Cited by 130 · see citing works
Neutrophil Extracellular Traps Exacerbate Ischemic Brain Damage
Li, C., Xing, Y., Zhang, Y., Yan, H., Jian, H., & Bai, Y. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02635-z · Cited by 129 · see citing works
de Bont, C. M., Koopman, W. J. H., Boelens, W. C., & Pruijn, G. J. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.08.014 · Cited by 130 · see citing works
Autophagy in Neutrophils: From Granulopoiesis to Neutrophil Extracellular Traps
Skendros, P., Mitroulis, I., & Ritis, K. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00109 · Cited by 129 · see citing works
Islam, M. M., & Takeyama, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115805 · Cited by 130 · see citing works
“MPO triggers the stimulation and translocation of NE from azurophilic granules to the nucleus and decorates the chromatin [39–41].”
BackgroundEosinophil ETosis and DNA Traps: a New Look at Eosinophilic Inflammation
Ueki, S., Tokunaga, T., Fujieda, S., Honda, K., Hirokawa, M., Spencer, L. A., & Weller, P. F. (2016) · Current Allergy and Asthma Reports · doi:10.1007/s11882-016-0634-5 · Cited by 124 · see citing works
Targeting Neutrophils for Promoting the Resolution of Inflammation
Filep, J. G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.866747 · Cited by 128 · see citing works
A novel image-based quantitative method for the characterization of NETosis
Zhao, W., Fogg, D. K., & Kaplan, M. J. (2015) · Journal of Immunological Methods · doi:10.1016/j.jim.2015.04.027 · Cited by 122 · see citing works
“A hallmark of early stage ‘suicidal’ NETosis is the nuclear translocation of the azurophilic granule proteins neutrophil elastase (NE) and myeloperoxidase (MPO), followed by histone degradation leading to chromatin decondensation (Papayannopoulos et al., 2010; Metzler et al., 2014).”
Yang, J., Wu, Z., Long, Q., Huang, J., Hong, T., Liu, W., & Lin, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.610696 · Cited by 121 · see citing works
Neutrophil serine proteases in antibacterial defense
Stapels, D. A. C., Geisbrecht, B. V., & Rooijakkers, S. H. M. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.11.002 · Cited by 121 · see citing works
Free DNA in Cystic Fibrosis Airway Fluids Correlates with Airflow Obstruction
Marcos, V., Zhou-Suckow, Z., Yildirim, A. Ö., Bohla, A., Hector, A., Vitkov, L., Krautgartner, W. D., Stoiber, W., Griese, M., Eickelberg, O., et al. (2015) · Mediators of Inflammation · doi:10.1155/2015/408935 · Cited by 120 · see citing works
“A recent study analyzing neutrophils from a patient with Papillon-Lefevre syndrome (PLS), lacking serine proteases, showed that neutrophils from this patient failed to produce NETs [51], corroborating the concept that serine proteases, particularly elastase, regulate NET formation [50, 52–54].”
BackgroundNeutrophil extracellular traps in fungal infection
Urban, C. F., & Nett, J. E. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.020 · Cited by 124 · see citing works
“In the cytoplasm, NE degrades actin filaments to arrest cellular movement and facilitate NE’s nuclear translocation (18).”
BackgroundGiaglis, S., Stoikou, M., Chowdhury, C. S., Schaefer, G., Grimolizzi, F., Rossi, S. W., Hoesli, I. M., Lapaire, O., Hasler, P., & Hahn, S. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00565 · Cited by 120 · see citing works
“MPO, also originating from the azurophilic granules, consumes H2O2 to generate HOCl and other oxidants and is required for translocation of NE to the nucleus during NETosis by regulating actin dynamics (18, 23).”
BackgroundThe Role of Serine Proteases and Antiproteases in the Cystic Fibrosis Lung
Twigg, M. S., Brockbank, S., Lowry, P., Fitzgerald, S., Taggart, C. C., & Weldon, S. (2015) · Mediators of Inflammation · doi:10.1155/2015/293053 · Cited by 117 · see citing works
“[63, 64].”
de Souza, C. N., Breda, L. C. D., Khan, M. A., de Almeida, S. R., Câmara, N. O. S., Sweezey, N., & Palaniyar, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01849 · Cited by 116 · see citing works
“It cleaves histone 4 (9, 47); histone cleavage has been linked to chromatin decondensation, and considered as an important step in NET formation (9, 47, 48).”
Post-Translational Modifications in NETosis and NETs-Mediated Diseases
Hamam, H. J., & Palaniyar, N. (2019) · Biomolecules · doi:10.3390/biom9080369 · Cited by 115 · see citing works
“Careful analysis reveals that acetylated levels of H4-K8, 12, 16 and H2B-K12 significantly increase as neutrophils derived from SLE patients are activated with PMA for 2 h. Interestingly, H3K27me3 levels show the greatest increase when compared to other PTMs in the same experimental conditions.”
BackgroundInfluentialDesai, J., Mulay, S. R., Nakazawa, D., & Anders, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2195-0 · Cited by 115 · see citing works
“Upon activation of neutrophils, ROS triggers the MPOdependent proteolytic activity of NE [15].”
Neutrophil Extracellular Traps, Angiogenesis and Cancer
Poto, R., Cristinziano, L., Modestino, L., de Paulis, A., Marone, G., Loffredo, S., Galdiero, M. R., & Varricchi, G. (2022) · Biomedicines · doi:10.3390/biomedicines10020431 · Cited by 115 · see citing works
- Authors
- Metzler, K. D., Goosmann, C., Lubojemska, A., Zychlinsky, A., & Papayannopoulos, V.
- Affiliations
- Max Planck Institute for Infection Biology (DE)
- Medical Research Council (GB)
- Corresponding author
- Papayannopoulos, Venizelos
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 8
- Issue
- 3
- Pages
- 883-896
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC4471680
- OpenAlex
- W2011145349
- Cited by
- 741
- References
- 40
- Citations by year
- 2026: 64 · 2025: 79 · 2024: 83 · 2023: 92 · 2022: 91 · 2021: 75 · 2020: 61 · 2019: 46 · 2018: 54 · 2017: 34 · 2016: 42 · 2015: 17 · 2014: 3
- FWCI
- 14.63
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Max Planck Digital Library (submittedVersion)
- Funders
- Medical Research Council (MC_UP_1202/13)
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- neutrophil extracellular traps, neutrophil elastase, myeloperoxidase, neutrophil granules, reactive oxygen species, actin dynamics, antimicrobial proteins
- MeSH terms
- Actins, Cell Membrane, Cell Nucleus, Humans, Peroxidase, Neutrophils, Protein Binding, Reactive Oxygen Species, Leukocyte Elastase, Active Transport, Cell Nucleus, Proteolysis, Extracellular Traps
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