The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Export by red blood cells of nitric oxide bioactivity
Abstract
Previous studies support a model in which the physiological O2 gradient is transduced by haemoglobin into the coordinate release from red blood cells of O2 and nitric oxide (NO)-derived vasoactivity to optimize oxygen delivery in the arterial periphery. But whereas both O2 and NO diffuse into red blood cells, only O2 can diffuse out. Thus, for the dilation of blood vessels by red blood cells, there must be a mechanism to export NO-related vasoactivity, and current models of NO-mediated intercellular communication should be revised. Here we show that in human erythrocytes haemoglobin-derived S-nitrosothiol (SNO), generated from imported NO, is associated predominantly with the red blood cell membrane, and principally with cysteine residues in the haemoglobin-binding cytoplasmic domain of the anion exchanger AE1. Interaction with AE1 promotes the deoxygenated structure in SNO-haemoglobin, which subserves NO group transfer to the membrane. Furthermore, we show that vasodilatory activity is released from this membrane precinct by deoxygenation. Thus, the oxygen-regulated cellular mechanism that couples the synthesis and export of haemoglobin-derived NO bioactivity operates, at least in part, through formation of AE1-SNO at the membrane-cytosol interface.
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“This view changed radically after the discovery of RBC-mediated hypoxic vasodilation: under conditions of decreased oxygen saturation, RBCs were shown to induce vasodilation of vessel strips by exporting NO bioactivity (146).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [146]
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Protein S-nitrosylation: Purview and parameters
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Nitric Oxide: The Versatility of an Extensive Signal Molecule
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Metadata
- Authors
- Pawloski, J. R., Hess, D. T., & Stamler, J. S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Stamler, Jonathan S.
- ORCID
- Stamler, Jonathan S.
- Venue
- Nature
- Published
- 2001-02
- Volume
- 409
- Issue
- 6820
- Pages
- 622-626
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2118023300
- Cited by
- 579
- References
- 28
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 13 · 2023: 13 · 2022: 22 · 2021: 20 · 2020: 17 · 2019: 17 · 2018: 10 · 2017: 19 · 2016: 12 · 2015: 18 · 2014: 16 · 2013: 27 · 2012: 22
- FWCI
- 16.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- American Heart Association
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- nitric oxide, erythrocytes, S-nitrosothiols, hemoglobin, band 3, oxygen gradients, vasodilation, oxygen delivery, intercellular communication, cysteine residues
- MeSH terms
- Animals, Aorta, Biological Transport, Erythrocyte Membrane, Erythrocytes, Hemoglobins, Humans, Mercaptoethanol, Nitric Oxide, Nitroso Compounds, Rabbits, Vasoconstriction, 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, Antiporters, S-Nitrosothiols, Chloride-Bicarbonate Antiporters, In Vitro Techniques
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