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Oxygen radical inhibition of nitric oxide-dependent vascular function in sickle cell disease
Open accessAbstract
Plasma xanthine oxidase (XO) activity was defined as a source of enhanced vascular superoxide (O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{{\cdot}-}}}\end{equation*}\end{document} ) and hydrogen peroxide (H 2 O 2 ) production in both sickle cell disease (SCD) patients and knockout-transgenic SCD mice. There was a significant increase in the plasma XO activity of SCD patients that was similarly reflected in the SCD mouse model. Western blot and enzymatic analysis of liver tissue from SCD mice revealed decreased XO content. Hematoxylin and eosin staining of liver tissue of knockout-transgenic SCD mice indicated extensive hepatocellular injury that was accompanied by increased plasma content of the liver enzyme alanine aminotransferase. Immunocytochemical and enzymatic analysis of XO in thoracic aorta and liver tissue of SCD mice showed increased vessel wall and decreased liver XO, with XO concentrated on and in vascular luminal cells. Steady-state rates of vascular O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{{\cdot}-}}}\end{equation*}\end{document} production, as indicated by coelenterazine chemiluminescence, were significantly increased, and nitric oxide ( ⋅ NO)-dependent vasorelaxation of aortic ring segments was severely impaired in SCD mice, implying oxidative inactivation of ⋅ NO. Pretreatment of aortic vessels with the superoxide dismutase mimetic manganese 5,10,15,20-tetrakis( N -ethylpyridinium-2-yl)porphyrin markedly decreased O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{{\cdot}-}}}\end{equation*}\end{document} levels and significantly restored acetylcholine-dependent relaxation, whereas catalase had no effect. These data reveal that episodes of intrahepatic hypoxia-reoxygenation associated with SCD can induce the release of XO into the circulation from the liver. This circulating XO can then bind avidly to vessel luminal cells and impair vascular function by creating an oxidative milieu and catalytically consuming ⋅ NO via O \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{2}^{{\cdot}-}}}\end{equation*}\end{document} -dependent mechanisms.
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“The binding of plasma XO to ECs can lead to vascular dysfunction (45, 71, 562, 612, 1010).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [45]
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Metadata
- Authors
- Aslan, M., Ryan, T. M., Adler, B., Townes, T. M., Parks, D. A., Thompson, J. A., Tousson, A., Gladwin, M. T., Patel, R. P., Tarpey, M. M., Batinic-Haberle, I., White, C. R., & Freeman, B. A.
- Affiliations
- National Institutes of Health (US)
- Departments of Anesthesiology, Biochemistry and Molecular Genetics, Pathology, Medicine, and Surgery, Center for Free Radical Biology, Imaging Facility and Comprehensive Sickle Cell Disease Center, University of Alabama, Birmingham, AL 35233; Critical Care Medicine Department of the Warren G. Magnuson Clinical Center, and Laboratory of Chemical Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892; and Department of...
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-12-18
- Volume
- 98
- Issue
- 26
- Pages
- 15215-15220
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC65009
- OpenAlex
- W2014093734
- Cited by
- 391
- References
- 67
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 12 · 2022: 9 · 2021: 14 · 2020: 14 · 2019: 18 · 2018: 15 · 2017: 14 · 2016: 9 · 2015: 17 · 2014: 17 · 2013: 16 · 2012: 11
- FWCI
- 9.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p60hl058418-05)
- National Heart, Lung, and Blood Institute (R01HL64937, R01HL064937, P6-HL-58418, R01HL058115, R01-HL-58115)
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- sickle cell disease, xanthine oxidase, superoxide, nitric oxide, hydrogen peroxide, hepatocyte injury, aorta, superoxide dismutase mimetic, manganese porphyrin
- MeSH terms
- Alanine Transaminase, Anemia, Sickle Cell, Animals, Endothelium, Vascular, Erythrocytes, Humans, Muscle Relaxation, Nitric Oxide, Superoxides, Xanthine Oxidase, Mice, Knockout, Mice, In Vitro Techniques
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