Nitric oxide synthase reduces nitrite to NO under anoxia
Open accessAbstract
Cultured bEND.3 endothelial cells show a marked increase in NO production when subjected to anoxia, even though the normal arginine pathway of NO formation is blocked due to absence of oxygen. The rate of anoxic NO production exceeds basal unstimulated NO synthesis in normoxic cells. The anoxic release of NO is mediated by endothelial nitric oxide synthase (eNOS), can be abolished by inhibitors of NOS and is accompanied by consumption of intracellular nitrite. The anoxic NO release is unaffected by the xanthine oxidase inhibitor oxypurinol. The phenomenon is attributed to anoxic reduction of intracellular nitrite by eNOS, and its magnitude and duration suggests that the nitrite reductase activity of eNOS is relevant for fast NO delivery in hypoxic vascular tissues.
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Competing reactions, namely NO scavenging by ferrous heme and NO dioxygenation, greatly decrease the amount of bioavailable NO generated by reactions of nitrite with heme proteins.
“It should be noted that competing reactions, namely the scavenging of NO by the ferrous heme [rate constants in the order of 1.7 × 107 to 1.5 × 108 M−1s−1 (180, 967), Eq. 6] and the rate of NO dioxygenation [rate constants in the order of 3.4 × 107 to 8.9 × 107 M−1s−1 for mammalian Hb/Mb (264, 341), Eq. 8] greatly decrease the amount of bioavailable NO generated by the reactions of nitrite with he”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [967]
Endothelial NOS has been shown to be capable of reducing nitrite to NO.
“Endothelial NOS has also been shown to be capable of reducing nitrite to NO [81–83].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [82]
Numerous other nitrite reduction mechanisms have been identified including aldehyde dehydrogenase, carbonic anhydrase, and endothelial nitric oxide synthase.
“Numerous other nitrite reduction mechanisms have been identified besides those discussed above including: aldehyde dehydrogenase, carbonic anhydrase, and endothelial nitric oxide synthase [130–132].”
From Inorganic nitrite therapy: historical perspective and future directions (2011) · cites this paper as [132]
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References 35 · Cited by 151
Research works printed but not linked: 5
- 2 Webb, A., Bond, R., McLean, P ., Uppal, R., Benjamin, N. and Ahluwalia, A. (2004) Reduction of nitrite to nitric oxide protects against myocardial ischemia-reperfusion damage. Proc. Natl. Acad. Sci. USA 101, 13683-13688.
- 5 Gladwin, M., Shelhamer, J., Schechter, A., Pease-Fye, M., Waclawiw, M., Panza, J., Ognibene, F. and Cannon, R. III (2000) Role of circulating nitrite and S -nitrosohemoglobin in the regulation of the regional blood flow in humans. Proc. Natl. Acad. Sci. USA 97, 11482-11487.
- 8 Lauer, T., Preik, M., Rassaf, T., Strauer, B., Deussen, A., Feelisch, M. and Kelm, M. (2001) Plasma nitrite rather than nitrate reflects regional endothelial nitric oxide synthase activity but lacks intrinsic vasodilator action. Proc. Natl. Acad. Sci. USA 98, 12814-12819.
- 10 Rodriguez, J., Maloney, R., Rassaf, T., Bryan, N. and Feelisch, J. (2003) Chemical nature of nitric oxide storage forms in rat vascular tissue. Proc. Natl. Acad. Sci. USA 100, 336-341.
- 36 Vanin, A., Bevers, L., Mikoyan, V ., Poltorakov, A., Kubrina, L. and van Faassen, E. (2006) Reduction enhances yields of nitric oxide trapping in biological systems. Nitric Oxide (in press).
- Authors
- Vanin, A. F., Bevers, L. M., Slama-Schwok, A., & van Faassen, E. E.
- Affiliations
- Russian Academy of Sciences (RU)
- University Medical Center Utrecht (NL)
- ORCID
- Vanin, A. F.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2006-12-08
- Volume
- 64
- Issue
- 1
- Pages
- 96-103
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11136343
- OpenAlex
- W1972443719
- Cited by
- 151
- References
- 35
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 6 · 2020: 3 · 2019: 4 · 2018: 11 · 2017: 9 · 2016: 6 · 2015: 8 · 2014: 11 · 2013: 12 · 2012: 12
- FWCI
- 7.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Radboud Repository (Radboud University) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- nitric oxide synthase, endothelial nitric oxide synthase, nitrite reduction, nitric oxide production, anoxia, hypoxia, bEnd.3 endothelial cells, nitrite reductase activity, oxypurinol, xanthine oxidase
- MeSH terms
- Animals, Cell Line, Cell Survival, Kinetics, Nitric Oxide, Nitrites, Oxidation-Reduction, Cell Hypoxia, Endothelial Cells, Mice, Nitric Oxide Synthase Type III
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