Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II
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Superoxide anion (O 2 − ) plays a key role in the endogenous suppression of endothelium-derived nitric oxide (NO) bioactivity and has been implicated in the development of hypertension. In previous studies, we found that O 2 − is produced predominantly in the adventitia of isolated rabbit aorta and acts as a barrier to NO. In the present studies, we characterize the enzyme responsible for O 2 − production in the adventitia and show that this enzyme is a constitutively active NADPH oxidase with similar composition as the phagocyte NADPH oxidase. Constitutive O 2 − -generating activity was localized to aortic adventitial fibroblasts and was enhanced by the potent vasoconstrictor angiotensin II. Immunohistochemistry of aortic sections demonstrated the presence of p22 phox , gp91 phox , p47 phox , and p67 phox localized exclusively in rabbit aortic adventitia, coincident with the site of staining for O 2 − production. Furthermore, immunodepletion of p67 phox from adventitial fibroblast particulates resulted in the loss of NADPH oxidase activity, which could be restored by the addition of recombinant p67 phox . Further study into the regulation of this adventitial source of O 2 − is important in elucidating the mechanisms regulating the bioactivity of NO and may contribute to our understanding of the pathogenesis of hypertension.
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CO can be, in low concentrations, a signaling molecule.
“but CO can also be, in low concentrations, a signaling molecule (713, 739, 805, 807).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [713]
High levels of HO-1 are present in the spleen, consistent with an important role in the processing of heme from red blood cell turnover.
“High levels of HO-1 are present in the spleen, consistent with an important role in the processing of heme from red blood cell turnover (713, 805).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [713]
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- Authors
- Pagano, P. J., Clark, J. K., Cifuentes-Pagano, M. E., Clark, S. M., Callis, G. M., & Quinn, M. T.
- Affiliations
- Boston Medical Center (US)
- Vascular Biology Unit, Boston Medical Center, Boston, MA 02118; and Department of Veterinary Molecular Biology, Montana State University, Bozeman, MT 59717
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1997-12-23
- Volume
- 94
- Issue
- 26
- Pages
- 14483-14488
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC25029
- OpenAlex
- W2170708014
- Cited by
- 455
- References
- 48
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 8 · 2019: 8 · 2018: 3 · 2017: 8 · 2016: 12 · 2015: 4 · 2014: 14 · 2013: 9 · 2012: 14
- FWCI
- 12.21
- 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 (7r29hl055425-03)
- National Heart, Lung, and Blood Institute (R29 HL55425-02, R01HL055425)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR042426)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- NADPH oxidase, superoxide, aortic adventitia, adventitial fibroblasts, angiotensin II, p67phox, p22phox, gp91phox, p47phox, nitric oxide, hypertension, vasoconstriction, rabbits
- MeSH terms
- Angiotensin II, Animals, Aorta, Cells, Cultured, Immunohistochemistry, NADPH Dehydrogenase, Phagocytes, Phosphoproteins, Rabbits, Vasoconstrictor Agents, NADPH Oxidases, Membrane Transport Proteins
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