Autocrine/paracrine pattern of superoxide production through NAD(P)H oxidase in coronary arterial myocytes
Abstract
The present study tested the hypothesis that membrane-bound NAD(P)H oxidase in coronary arterial myocytes (CAMs) is capable of producing superoxide (O 2•−) toward extracellular space to exert an autocrine- or paracrine-like action in these cells. Using a high-speed wavelength-switching fluorescent microscopic imaging technique, we simultaneously monitored the binding of dihydroethidium-oxidizing product to exogenous salmon testes DNA trapped outside CAMs and to nuclear DNA as indicators of extra- and intracellular O 2•−production. It was found that a muscarinic agonist oxotremorine (OXO; 80 μM) increased O 2•−levels more rapidly outside than inside CAMs. In the presence of superoxide dismutase (500 U/ml) plus catalase (400 U/ml) and NAD(P)H oxidase inhibitor diphenylene iodonium (50 μM) or apocynin (100 μM), these increases in extra- and intracellular O 2•−levels were substantially abolished or attenuated. The O 2•−increase outside CAMs was also confirmed by detecting oxidation of nitro blue tetrazolium and confocal microscopic localization of Matrigel-trapped OxyBURST H 2 HFF Green BSA staining around these cells. By electron spin resonance spectrometry, the extracellular accumulation of O 2•−was demonstrated as a superoxide dismutase-sensitive component outside CAMs. Furthermore, RNA interference of NAD(P)H oxidase subunits Nox1 or p47 markedly blocked OXO-induced increases in both extra- and intracellular O 2•−levels, whereas small inhibitory RNA of Nox4 only attenuated intracellular O 2•−accumulation. These results suggest that Nox1 represents a major NAD(P)H oxidase isoform responsible for extracellular O 2•−production. This rapid extracellular production of O 2•−seems to be unique to OXO-induced M 1-receptor activation, since ANG II-induced intra- and extracellular O 2•−increases in parallel. It is concluded that the outward production of O 2•−via NAD(P)H oxidase in CAMs may represent an important producing pattern for its autocrine or paracrine actions.
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COX are proteins from the peroxidase family, evolutionarily related to the peroxidase enzymes of the immune system.
“COX are proteins from the peroxidase family, evolutionarily related to the peroxidase enzymes of the immune system (1052).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1052]
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- Authors
- Zhang, G., Zhang, F., Muh, R., Yi, F., Chalupsky, K., Cai, H., & Li, P.-L.
- Affiliations
- Virginia Commonwealth University Medical Center (US)
- Venue
- American Journal of Physiology-Heart and Circulatory Physiology
- Publisher
- American Physiological Society
- Published
- 2007-01
- Volume
- 292
- Issue
- 1
- Pages
- H483-H495
- ISSN
- 0363-6135 (ISSN-L)
- 1522-1539
- OpenAlex
- W2114143085
- Cited by
- 42
- References
- 60
- Citations by year
- 2024: 1 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 1 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 3
- FWCI
- 3.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Heart and Circulatory Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-70726, R01HL077440, HL 57244, R01HL070726, HL-75316, R01HL075316)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- NADPH oxidase, superoxide production, autocrine signaling, paracrine signaling, NOX1, NOX4, p47phox, M1 muscarinic receptor, oxotremorine, angiotensin II, extracellular superoxide, diphenyleneiodonium, apocynin, superoxide dismutase, catalase
- MeSH terms
- Animals, Cattle, Cells, Cultured, Coronary Vessels, Oxidation-Reduction, Superoxides, NADPH Oxidases, Paracrine Communication, Myocytes, Cardiac, In Vitro Techniques
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