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Mitochondrial permeability transition pore is involved in oxidative burst and NETosis of human neutrophils
Open accessAbstract
Neutrophils release neutrophil extracellular traps (NETs) in response to numerous pathogenic microbes as the last suicidal resource (NETosis) in the fight against infection. Apart from the host defense function, NETs play an essential role in the pathogenesis of various autoimmune and inflammatory diseases. Therefore, understanding the molecular mechanisms of NETosis is important for regulating aberrant NET release. The initiation of NETosis after the recognition of pathogens by specific receptors is mediated by an increase in intracellular Ca 2+ concentration, therefore, the use of Ca 2+ ionophore A23187 can be considered a semi-physiological model of NETosis. Induction of NETosis by various stimuli depends on reactive oxygen species (ROS) produced by NADPH oxidase, however, NETosis induced by Ca 2+ ionophores was suggested to be mediated by ROS produced in mitochondria (mtROS). Using the mitochondria-targeted antioxidant SkQ1 and specific inhibitors of NADPH oxidase, we showed that both sources of ROS, mitochondria and NADPH oxidase, are involved in NETosis induced by A23187 in human neutrophils. In support of the critical role of mtROS, SkQ1-sensitive NETosis was demonstrated to be induced by A23187 in neutrophils from patients with chronic granulomatous disease (CGD). We assume that Ca 2+-triggered mtROS production contributes to NETosis either directly (CGD neutrophils) or by stimulating NADPH oxidase. The opening of the mitochondrial permeability transition pore (mPTP) in neutrophils treated by A23187 was revealed using the electron transmission microscopy as a swelling of the mitochondrial matrix. Using specific inhibitors, we demonstrated that the mPTP is involved in mtROS production, NETosis, and the oxidative burst induced by A23187.
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“Mitochondrial ROS are involved in NOx activation and in the induction of classical NETosis by various stimuli [63,64].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [64]
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Metadata
- Authors
- Vorobjeva, N., Galkin, I., Pletjushkina, O., Golyshev, S., Zinovkin, R., Prikhodko, A., Pinegin, V., Kondratenko, I., Pinegin, B., & Chernyak, B.
- Affiliations
- Lomonosov Moscow State University (RU)
- Sechenov University (RU)
- Federal Medical-Biological Agency (RU)
- Corresponding author
- Vorobjeva, Nina
- ORCID
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2020-05
- Volume
- 1866
- Issue
- 5
- Pages
- 165664
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2999533595
- Cited by
- 136
- References
- 61
- Citations by year
- 2026: 16 · 2025: 29 · 2024: 25 · 2023: 23 · 2022: 24 · 2021: 10 · 2020: 9
- FWCI
- 5.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Russian Foundation for Basic Research
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- mitochondrial permeability transition pore, neutrophil extracellular traps, NETosis, respiratory burst, neutrophils, mitochondrial reactive oxygen species, NADPH oxidase, A23187, chronic granulomatous disease, SkQ1, mitochondrial swelling, intracellular calcium
- MeSH terms
- Calcimycin, Loss of Function Mutation, NADPH Oxidase 2, Mitochondrial Permeability Transition Pore, Adolescent, Calcium, Cations, Divalent, Cells, Cultured, Child, Electron Transport, Granulomatous Disease, Chronic, Humans, Male, Mitochondria, Neutrophils, Oxidation-Reduction, Plastoquinone, Free Radical Scavengers, Respiratory Burst, Reactive Oxygen Species, Mitochondrial Membrane Transport Proteins, Membrane Potential, Mitochondrial, Primary Cell Culture, Healthy Volunteers, Extracellular Traps
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