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Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention
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There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.
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“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
In the citing paper
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
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“Hypochlorous acid HOCl and hypothiocyanous acid HOSCN synthesized through the enzyme myeloperoxidase MPO, which catalyzes the reaction between H2O2 and Cl− or SCN−, are important inorganic bactericidal molecules, effective against a wide range of microbes.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
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Self-citationChen, F., Wang, H., Zhao, J., Yan, J., Meng, H., Zhan, H., Chen, L., & Yuan, L. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.01.013 · Cited by 48
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Metadata
- Authors
- Davies, M. J.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Davies, Michael J.
- ORCID
- Davies, Michael J.
- Venue
- Journal of Clinical Biochemistry and Nutrition
- Published
- 2010
- Volume
- 48
- Issue
- 1
- Pages
- 8-19
- ISSN
- 0912-0009 (ISSN-L)
- 1880-5086
- PMC
- PMC3022070
- OpenAlex
- W2028031080
- Cited by
- 412
- References
- 227
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 31 · 2023: 30 · 2022: 34 · 2021: 40 · 2020: 41 · 2019: 37 · 2018: 27 · 2017: 29 · 2016: 23 · 2015: 21 · 2014: 19 · 2013: 16 · 2012: 24
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Biochemistry and Nutrition (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation pour la Recherche Médicale
- Medical Research Council
- Australian Research Council (CE0561607, DP0988311)
- National Health and Medical Research Council (570829)
- 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
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- myeloperoxidase, heme peroxidase, eosinophil peroxidase, lactoperoxidase, oxidative damage, oxidative damage biomarkers, enzyme inhibitors
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