Hemoglobin-Mediated, Hypoxia-Induced Vasodilation via Nitric Oxide
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Several proposed mechanisms explain how nitrite-derived bioactivity can be exported from the red blood cell, generally involving either a compartment model with submembrane localization or formation of another nitrogen oxide such as a nitrosothiol or N2O3.
“Several proposed mechanisms have been constructed to explain how nitrite-derived bioactivity can be exported from the red blood cell and these generally involve either a compartment model with submembrane localization of the reaction allowing for inefficient free NO escape, or the formation of another nitrogen oxide such as a nitrosothiol or N2O3 that can get out of the red blood cell and carry NO”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [46]
Formation of N2O3 from nitrite would facilitate export of NO activity from the red blood cell and evidence for the formation of this species has been reported.
“Formation of N2O3 from nitrite would facilitate export of NO activity from the red blood cell and evidence for the formation of this species has been reported [45–47, 99].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [46]
Recent evidence points to dinitrogen trioxide (N2O3) as a plausible intermediate for generation of NO downstream from nitrite reduction.
“Recent evidence points towards the formation of the nitrosating agent dinitrogen trioxide (N2O3) as one such plausible intermediate for the generation of NO downstream from nitrite reduction (Scheme 2) [42-45].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [42]
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- Authors
- Robinson, J. M., & Lancaster, J. R.
- Affiliations
- University of Alabama (US)
- ORCID
- Robinson, John M.
- Venue
- American Journal of Respiratory Cell and Molecular Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-04-01
- Volume
- 32
- Issue
- 4
- Pages
- 257-261
- ISSN
- 1044-1549 (ISSN-L)
- 1535-4989
- OpenAlex
- W1943267040
- Cited by
- 104
- References
- 52
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 2 · 2022: 4 · 2020: 5 · 2019: 3 · 2017: 3 · 2016: 4 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 4
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Respiratory Cell and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- hemoglobin, hypoxia, vasodilation, nitric oxide, nitric oxide synthase, pulmonary vasculature, oxygen sensing
- MeSH terms
- Animals, Hypoxia, Erythrocytes, Hemoglobins, Humans, Models, Biological, Nitric Oxide, Nitrite Reductases, Oxygen, Vasodilation
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