Cited by 359Nitric Oxide and Endothelin EffectsHemoglobin structure and functionMetal-Catalyzed Oxygenation Mechanisms

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Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis

Shiva, Sruti, Wang, Xunde, Ringwood, Lorna A, Xu, Xueying, Yuditskaya, Susan, Annavajjhala, Vidhya, Miyajima, Hiroaki, Hogg, Neil, Harris, Zena Leah, Gladwin, Mark T·2006·Nature Chemical Biology

DOI 10.1038/nchembio813

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Abstract

Nitrite represents a bioactive reservoir of nitric oxide (NO) that may modulate vasodilation, respiration and cytoprotection after ischemia-reperfusion injury. Although nitrite formation is thought to occur via reaction of NO with oxygen, this third-order reaction cannot compete kinetically with the reaction of NO with hemoglobin to form nitrate. Indeed, the formation of nitrite from NO in the blood is limited when plasma is substituted with physiological buffers, which suggests that plasma contains metal-based enzymatic pathways for nitrite synthesis. We therefore hypothesized that the multicopper oxidase, ceruloplasmin, could oxidize NO to NO+, with subsequent hydration to nitrite. Accordingly, plasma NO oxidase activity was decreased after ceruloplasmin immunodepletion, in ceruloplasmin knockout mice and in people with congenital aceruloplasminemia. Compared to controls, plasma nitrite concentrations were substantially reduced in ceruloplasmin knockout mice, which were more susceptible to liver infarction after ischemia and reperfusion. The extent of hepatocellular infarction normalized after nitrite repletion. These data suggest new functions for the multicopper oxidases in endocrine NO homeostasis and nitrite synthesis, and they support the hypothesis that physiological concentrations of nitrite contribute to hypoxic signaling and cytoprotection.

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Authors: Shiva, S., Wang, X., Ringwood, L. A., Xu, X., Yuditskaya, S., Annavajjhala, V., Miyajima, H., Hogg, N., Harris, Z. L., & Gladwin, M. T.
Affiliations: National Institutes of Health (US)
Johns Hopkins University (US)
Hamamatsu University (JP)
Medical College of Wisconsin (US)
Corresponding author: Gladwin, Mark T
ORCID: Shiva, Sruti
Xu, Xueying
Annavajjhala, Vidhya
Miyajima, Hiroaki
Hogg, Neil
Harris, Zena Leah
Gladwin, Mark T
Venue: Nature Chemical Biology
Publisher: Springer Science and Business Media LLC
Published: 2006-08-13
Volume: 2
Issue: 9
Pages: 486-493
ISSN: 1552-4450 (ISSN-L)
1552-4469
DOI: 10.1038/nchembio813
OpenAlex: W1973480138
Cited by: 359
References: 52
Citations by year: 2026: 6 · 2025: 7 · 2024: 6 · 2023: 17 · 2022: 22 · 2021: 22 · 2020: 17 · 2019: 13 · 2018: 13 · 2017: 15 · 2016: 19 · 2015: 22 · 2014: 24 · 2013: 28 · 2012: 24
FWCI: 13.40
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Chemical Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: ceruloplasmin, nitric oxide homeostasis, multicopper oxidase, aceruloplasminemia, ischemia-reperfusion injury, liver infarction, hypoxia signaling, cytoprotection, nitrate
MeSH terms: Animals, Catalysis, Ceruloplasmin, Endocrine System, Erythrocytes, Female, Homeostasis, Humans, Liver, Male, Mice, Transgenic, Nitric Oxide, Nitrites, Oxidation-Reduction, Plasma, Vasodilation, Reperfusion Injury, Nitric Oxide Synthase, Mice, In Vitro Techniques

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Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis

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