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Investigating antibody-catalyzed ozone generation by human neutrophils
Open accessAbstract
Recent studies have suggested that antibodies can catalyze the generation of previously unknown oxidants including dihydrogen trioxide (H 2 O 3 ) and ozone (O 3 ) from singlet oxygen ( 1 O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{*}}}\end{equation*}\end{document} ) and water. Given that neutrophils have the potential both to produce 1 O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{*}}}\end{equation*}\end{document} and to bind antibodies, we considered that these cells could be a biological source of O 3 . We report here further analytical evidence that antibody-coated neutrophils, after activation, produce an oxidant with the chemical signature of O 3 . This process is independent of surface antibody concentration down to 50% of the resting concentration, suggesting that surface IgG is highly efficient at intercepting the neutrophil-generated 1 O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{*}}}\end{equation*}\end{document} . Vinylbenzoic acid, an orthogonal probe for ozone detection, is oxidized by activated neutrophils to 4-carboxybenzaldehyde in a manner analogous to that obtained for its oxidation by ozone in solution. This discovery of the production of such a powerful oxidant in a biological context raises questions about not only the capacity of O 3 to kill invading microorganisms but also its role in amplification of the inflammatory response by signaling and gene activation.
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Citations
Cited by
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Babior, B. M. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2003.12.001 · Cited by 705
Self-citationModeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome
Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 631
Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 560
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468
Metadata
- Authors
- Babior, B. M., Takeuchi, C., Ruedi, J., Gutierrez, A., & Wentworth, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-02-24
- Volume
- 100
- Issue
- 6
- Pages
- 3031-3034
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2028868364
- Cited by
- 211
- References
- 0
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- green
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- Babior, B. M., Takeuchi, C., Ruedi, J., Gutierrez, A., & Wentworth, P. (2003). Investigating antibody-catalyzed ozone generation by human neutrophils. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0530251100
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