Respiratory uncoupling by UCP1 and UCP2 and superoxide generation in endothelial cell mitochondria
Abstract
Mitochondria represent a major source of reactive oxygen species (ROS), particularly during resting or state 4 respiration wherein ATP is not generated. One proposed role for respiratory mitochondrial uncoupling proteins (UCPs) is to decrease mitochondrial membrane potential and thereby protect cells from damage due to ROS. This work was designed to examine superoxide production during state 4 (no ATP production) and state 3 (active ATP synthesis) respiration and to determine whether uncoupling reduced the specific production of this radical species, whether this occurred in endothelial mitochondria per se, and whether this could be modulated by UCPs. Superoxide formation by isolated bovine aortic endothelial cell (BAE) mitochondria, determined using electron paramagnetic resonance spectroscopy, was approximately fourfold greater during state 4 compared with state 3 respiration. UCP1 and UCP2 overexpression both increased the proton conductance of endothelial cell mitochondria, as rigorously determined by the kinetic relationship of respiration to inner membrane potential. However, despite uncoupling, neither UCP1 nor UCP2 altered superoxide formation. Antimycin, known to increase mitochondrial superoxide, was studied as a positive control and markedly enhanced the superoxide spin adduct in our mitochondrial preparations, whereas the signal was markedly impaired by the powerful chemical uncoupler p-(trifluoromethoxyl)-phenyl-hydrazone. In summary, we show that UCPs do have uncoupling properties when expressed in BAE mitochondria but that uncoupling by UCP1 or UCP2 does not prevent acute substrate-driven endothelial cell superoxide as effluxed from mitochondria respiring in vitro.
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Overexpression of UCP1 or UCP2 in BAE cells had no effect on ROS detected by EPR.
“Moreover, in past work in our laboratory (105), we were unable to show any effect of overexpression of UCPs (either UCP1 or UCP2) in BAE cells on ROS.”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [105]
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- Authors
- Fink, B. D., Reszka, K. J., Herlein, J. A., Mathahs, M. M., & Sivitz, W. I.
- Affiliations
- University of Iowa (US)
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2005-01
- Volume
- 288
- Issue
- 1
- Pages
- E71-E79
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2048297654
- Cited by
- 53
- References
- 35
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2020: 3 · 2018: 1 · 2017: 3 · 2015: 4 · 2014: 3 · 2013: 3 · 2012: 9
- FWCI
- 0.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- Office of Research and Development
- National Heart, Lung, and Blood Institute (R01-HL-073166-01, R01HL073166)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- respiratory uncoupling, UCP1, UCP2, superoxide production, mitochondrial reactive oxygen species, state 4 respiration, state 3 respiration, mitochondrial membrane potential, proton conductance, antimycin, bovine aortic endothelial cells
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 1, Adenosine Triphosphate, Animals, Aorta, Carrier Proteins, Cattle, Cells, Cultured, Electron Spin Resonance Spectroscopy, Endothelium, Vascular, Fatty Acids, Ion Channels, Membrane Proteins, Mitochondria, Superoxides, Oxidative Stress, Cell Respiration, Mitochondrial Proteins, Membrane Transport Proteins
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