Cited by 536Nitric Oxide and Endothelin EffectsRedox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium

Mohazzab, K. M., Kaminski, P. M., Wolin, M. S.·1994·American Journal of Physiology-Heart and Circulatory Physiology

Abstract

In this study we examined the intracellular sources of superoxide anion (O2-.) in cultured bovine coronary endothelium, employing lucigenin (250 microM)-elicited chemiluminescence (CL). In the homogenate from these cells, 100 microM NADPH increased O2-. by 81% from 8.9 +/- 1.5 to 16.0 +/- 1.5 x 10(5) cpm/mg protein (P < 0.01, n = 8). In the presence of 100 microM NADH, however, CL increased by 458% from 8.9 +/- 1.6 to 49.6 +/- 12.0 x 10(5) cpm/mg protein (P < 0.01, n = 8). Scavengers of O2-., superoxide dismutase (100 micrograms/ml), or 4,5-dihydroxy-1,3-benzenedisulfonic acid disodium salt (Tiron, 10 mM) inhibited NADH-mediated CL by 70 and 83%, respectively. Neither hypoxanthine (100 microM) nor antimycin (10 microM)+succinate (5 mM) had any significant effect on basal CL levels, thereby excluding xanthine oxidase and mitochondria, respectively, as a detectable sources of O2-. generation. The presence of NAD+ (100 microM) and lactate (1 mM) increased CL by 88% (n = 8, P < 0.01). In the intact cells, basal production of CL was increased by 205% (P < 0.01) by 5 mM lactate, but not by 5 mM pyruvate, and CL was inhibited by 10 mM Tiron, suggesting the reduction of cytosolic NAD by lactate dehydrogenase stimulates O2-. production. Diphenyliodonium at 1 and 10 microM inhibited both NADH-mediated CL in homogenate and lactate-mediated CL in intact endothelium by 50 and 33%, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

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Crossref · 10.1152/ajpheart.1994.266.6.h2568

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  • ADMA was recognized as an important marker for cardiovascular disease progression soon after its discovery in cells and tissue.

    “Soon after its discovery in cells and tissue, ADMA was recognized as an important marker for cardiovascular disease progression (656, 829, 961, 1011, 1053, 1068).”

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Authors
Mohazzab, K. M., Kaminski, P. M., & Wolin, M. S.
Affiliations
  • Department of Physiology, New York Medical College, Valhalla 10595.
  • New York Medical College (US)
Venue
American Journal of Physiology-Heart and Circulatory Physiology
Published
1994-06-01
Volume
266
Issue
6
Pages
H2568-H2572
ISSN
  • 0363-6135 (ISSN-L)
  • 1522-1539
OpenAlex
W143010615
Cited by
536
References
0
Citations by year
2025: 2 · 2024: 3 · 2023: 4 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 10 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 7 · 2014: 12 · 2013: 13 · 2012: 13
FWCI
7.93
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 (P01HL043023, HL 43023, HL-31069)
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
NADH oxidoreductase, superoxide, coronary endothelium, NADH, lactate, NAD+ reduction, lactate dehydrogenase, diphenyliodonium, superoxide dismutase, Tiron, xanthine oxidase, mitochondria, chemiluminescence
MeSH terms
Acridines, Animals, Anions, Cattle, Cells, Cultured, Coronary Vessels, Endothelium, Vascular, Lactates, Luminescent Measurements, NADH, NADPH Oxidoreductases, Superoxides, Xanthine Oxidase, Arachidonic Acid, Reactive Oxygen Species, Lactic Acid

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