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Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation
Open accessAbstract
The protected transport of nitric oxide (NO) by hemoglobin (Hb) links the metabolic activity of working tissue to the regulation of its local blood supply through hypoxic vasodilation. This physiologic mechanism is allosterically coupled to the O(2) saturation of Hb and involves the covalent binding of NO to a cysteine residue in the beta-chain of Hb (Cys beta93) to form S-nitrosohemoglobin (SNO-Hb). Subsequent S-transnitrosation, the transfer of NO groups to thiols on the RBC membrane and then in the plasma, preserves NO vasodilator activity for delivery to the vascular endothelium. This SNO-Hb paradigm provides insight into the respiratory cycle and a new therapeutic focus for diseases involving abnormal microcirculatory perfusion. In addition, the formation of S-nitrosothiols in other proteins may regulate an array of physiological functions.
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“The evidence for nitrite reactions with erythrocytic hemoglobin and stimulation of hypoxic blood flow remains more limited and is the subject of much debate [16, 61].”
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 [61]
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Metadata
- Authors
- Allen, B. W., Stamler, J. S., & Piantadosi, C. A.
- Affiliations
- Duke University (US)
- Corresponding author
- Allen, Barry W.
- ORCID
- Stamler, Jonathan S.
- Venue
- Trends in Molecular Medicine
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 15
- Issue
- 10
- Pages
- 452-460
- ISSN
- 1471-4914 (ISSN-L)
- PMC
- PMC2785508
- OpenAlex
- W2033703576
- Cited by
- 165
- References
- 100
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 7 · 2023: 7 · 2022: 11 · 2021: 12 · 2020: 8 · 2019: 4 · 2018: 5 · 2017: 5 · 2016: 10 · 2015: 8 · 2014: 12 · 2013: 9 · 2012: 23
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Molecular Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL091876)
- Office of Naval Research
- National Institute of Allergy and Infectious Diseases (R01AI064789)
- 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, hemoglobin, hypoxic vasodilation, S-nitrosohemoglobin, S-nitrosothiols, oxygen saturation, erythrocyte membrane, microvascular blood flow, respiratory cycle, endothelium
- MeSH terms
- Animals, Endothelium, Vascular, Hemoglobins, Humans, Nitric Oxide, Oxygen, Vasodilation, Nitrosation, Cell Hypoxia, S-Nitrosothiols
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