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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S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
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Self-citationBlood Flow Regulation by S -Nitrosohemoglobin in the Physiological Oxygen Gradient
Stamler, J. S., Jia, L., Eu, J. P., McMahon, T. J., Demchenko, I. T., Bonaventura, J., Gernert, K., & Piantadosi, C. A. (1997) · Science · doi:10.1126/science.276.5321.2034 · Cited by 1,050
Self-citation(S)NO Signals: Translocation, Regulation, and a Consensus Motif
Stamler, J. S., Toone, E. J., Lipton, S. A., & Sucher, N. J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80310-4 · Cited by 679
Self-citationReactions between nitric oxide and haemoglobin under physiological conditions
Gow, A. J., & Stamler, J. S. (1998) · Nature · doi:10.1038/34402 · Cited by 562
Self-citationDiffusion-limited reaction of free nitric oxide with erythrocytes
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The oxyhemoglobin reaction of nitric oxide
Gow, A. J., Luchsinger, B. P., Pawloski, J. R., Singel, D. J., & Stamler, J. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9027 · Cited by 418
Self-citationLow, P. S. (1986) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(86)90009-2 · Cited by 407
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Erythrocytes Possess an Intrinsic Barrier to Nitric Oxide Consumption
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Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Self-citationCysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery
Paulsen, C. E., & Carroll, K. S. (2013) · Chemical Reviews · doi:10.1021/cr300163e · Cited by 1,313
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
Self-citationNitric oxide in health and disease of the respiratory system
Ricciardolo, F. L. M., Sterk, P. J., Gaston, B., & Folkerts, G. (2004) · Physiological Reviews · doi:10.1152/physrev.00034.2003 · Cited by 903
Nitric Oxide: The Versatility of an Extensive Signal Molecule
Lamattina, L., García‐Mata, C., Graziano, M., & Pagnussat, G. C. (2003) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.54.031902.134752 · Cited by 877
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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