Nitric oxide, an endothelial cell relaxation factor, inhibits neutrophil superoxide anion production via a direct action on the NADPH oxidase.
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Nitric oxide provokes vasodilation and inhibits platelet aggregation. We examined the effect of nitric oxide on superoxide anion production by three sources: activated intact neutrophils, xanthine oxidase/hypoxanthine, and the NADPH oxidase. Nitric oxide significantly inhibited the generation of superoxide anion by neutrophils exposed to either FMLP (10(-7)M) or PMA (150 ng/ml) (IC50 = 30 microM). To determine whether the effect of nitric oxide on the respiratory burst was due to simple scavenging of O2+, kinetic studies that compared effects on neutrophils and the cell-free xanthine oxidase system were performed. Nitric oxide inhibited O2+ produced by xanthine oxidase only when added simultaneously with substrate, consistent with the short half-life of NO in oxygenated solution. In contrast, the addition of nitric oxide to neutrophils 20 min before FMLP resulted in the inhibition of O2+ production, which suggests formation of a stable intermediate. The effect of nitric oxide on the cell-free NADPH oxidase superoxide-generating system was also examined: The addition of NO before arachidonate activation (t = -6 min) significantly inhibited superoxide anion production. Nitric oxide did not inhibit O2+ when added at NADPH initiation (t = 0). Treatment of the membrane but not cytosolic component of the oxidase was sufficient to inhibit O2+ generation. The data suggest that nitric oxide inhibits neutrophil O2+ production via direct effects on membrane components of the NADPH oxidase. This action must occur before the assembly of the activated complex.
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NO, through its high affinity for heme groups or via S-nitrosation, can act as an important modulator of NOX or can modulate the insertion of heme in the receptor sGC.
“In another example, NO, through its high affinity for heme groups or via S-nitrosation, can act as an important modulator of NOX (176, 315, 846) or can also modulate the insertion of heme in the receptor sGC.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [176]
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- Authors
- Clancy, R. M., Leszczynska-Piziak, J., & Abramson, S. B.
- Affiliations
- NYU Langone Health (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1992-09-01
- Volume
- 90
- Issue
- 3
- Pages
- 1116-1121
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC329973
- OpenAlex
- W2139533485
- Cited by
- 686
- References
- 54
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 1 · 2021: 3 · 2020: 5 · 2019: 8 · 2018: 6 · 2017: 9 · 2016: 6 · 2015: 11 · 2014: 10 · 2013: 5 · 2012: 9
- FWCI
- 13.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- nitric oxide, neutrophils, superoxide production, NADPH oxidase, respiratory burst, fMLP, PMA, arachidonic acid, oxygen radical scavenging
- MeSH terms
- Calcium, Cells, Cultured, Humans, NADH, NADPH Oxidoreductases, Neutrophils, Nitric Oxide, Superoxides, Xanthine Oxidase, Cell Degranulation, NADPH Oxidases
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