Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
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Neutrophils release decondensed chromatin termed neutrophil extracellular traps (NETs) to trap and kill pathogens extracellularly. Reactive oxygen species are required to initiate NET formation but the downstream molecular mechanism is unknown. We show that upon activation, neutrophil elastase (NE) escapes from azurophilic granules and translocates to the nucleus, where it partially degrades specific histones, promoting chromatin decondensation. Subsequently, myeloperoxidase synergizes with NE in driving chromatin decondensation independent of its enzymatic activity. Accordingly, NE knockout mice do not form NETs in a pulmonary model of Klebsiella pneumoniae infection, which suggests that this defect may contribute to the immune deficiency of these mice. This mechanism provides for a novel function for serine proteases and highly charged granular proteins in the regulation of chromatin density, and reveals that the oxidative burst induces a selective release of granular proteins into the cytoplasm through an unknown mechanism.
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Intracellular ROS drive NETotic cell death by triggering release of ELANE and MPO from neutrophil granules to cytosol, followed by their translocation to nucleus.
“intracellular ROS would drive NETotic cell death (1) by triggering the release of elastase, neutrophil expressed (ELANE), and myeloperoxidase (MPO) from neutrophil granules to the cytosol, followed by their translocation to the nucleus”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [740]
Intracellular ROS promote MPO-dependent proteolytic activity of ELANE.
“(2) by promoting the MPO-dependent proteolytic activity of ELANE [740].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [740]
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 [28]
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 [28]
Cathepsin G is not just an effector of NET functions but participates in the release of NETs, similar to neutrophil elastase.
“Our data also suggest that cathepsin G is not just an effector of NET functions but participates in the release of NETs, similar to what is reported for neutrophil elastase (28).”
From Cancer cells induce metastasis-supporting neutrophil extracellular DNA traps (2016) · cites this paper as [28]
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- Authors
- Papayannopoulos, V., Metzler, K. D., Hakkim, A., & Zychlinsky, A.
- Affiliations
- Max Planck Institute for Infection Biology (DE)
- Corresponding author
- Zychlinsky, Arturo
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-10-25
- Volume
- 191
- Issue
- 3
- Pages
- 677-691
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3003309
- OpenAlex
- W2115959782
- Cited by
- 2,103
- References
- 74
- Citations by year
- 2026: 166 · 2025: 204 · 2024: 177 · 2023: 186 · 2022: 181 · 2021: 204 · 2020: 151 · 2019: 139 · 2018: 139 · 2017: 121 · 2016: 120 · 2015: 83 · 2014: 81 · 2013: 61 · 2012: 63
- FWCI
- 20.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion, cc-by-nc-sa)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Blood disorders and treatments
- Keywords
- neutrophil elastase, myeloperoxidase, neutrophil extracellular traps, chromatin decondensation, histone degradation, neutrophil respiratory burst, serine protease, azurophilic granules, Klebsiella pneumoniae infection, neutrophil-mediated immunity, immunodeficiency
- MeSH terms
- Animals, Disease Models, Animal, Extracellular Space, Humans, Klebsiella Infections, Klebsiella pneumoniae, Peroxidase, Neutrophils, Reference Values, Mice, Knockout, Leukocyte Elastase, Mice
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