Antioxidant Mechanism of Mitochondria-Targeted Plastoquinone SkQ1 Is Suppressed in Aglycemic HepG2 Cells Dependent on Oxidative Phosphorylation
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Previously suggested antioxidant mechanisms for mitochondria-targeted plastoquinone SkQ1 included: i) ion-pairing of cationic SkQ1+ with free fatty acid anions resulting in uncoupling; ii) SkQ1H 2 ability to interact with lipoperoxyl radical; iii) interference with electron flow at the inner ubiquinone (Q) binding site of Complex III (Q i), involving the reduction of SkQ1 to SkQ1H 2 by ubiquinol. We elucidated SkQ1 antioxidant properties by confocal fluorescence semi-quantification of mitochondrial superoxide (J m) and cytosolic H 2 O 2 (J c) release rates in HepG2 cells. Only in glycolytic cells, SkQ1 prevented the rotenone-induced enhancement of J m and J c but not basal releases without rotenone. The effect ceased in glutaminolytic aglycemic cells, in which the redox parameter NAD(P)H/FAD increased after rotenone in contrast to its decrease in glycolytic cells. Autofluorescence decay indicated decreased NADPH/NADH ratios with rotenone in both metabolic modes. SkQ1 did not increase cell respiration and diminished J m established high by antimycin or myxothiazol but not by stigmatellin. The revealed SkQ1 antioxidant modes reflect its reduction to SkQ1H 2 at Complex I I Q or Complex III Q i site. Both reductions diminish electron diversions to oxygen thus attenuating superoxide formation. Resulting SkQ1H 2 oxidizes back to SkQ1at the second (flavin) Complex I site, previously indicated for MitoQ 10. Regeneration proceeds only at lower NAD(P)H/FAD in glycolytic cells. In contrast, cyclic SkQ1 reduction/SkQ1H 2 oxidation does not substantiate antioxidant activity in intact cells in the absence of oxidative stress (neither pro-oxidant activity, representing a great advantage). A targeted delivery to oxidative-stressed tissues is suggested for the effective antioxidant therapy based on SkQ1.
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SkQ1 exerts its antioxidant properties by fatty acid co-mediated uncoupling, through interference with lipoperoxyl radicals and via regulating electron flow at the level of mitochondria.
“Mechanistically, SkQ1 exerts its antioxidant properties by fatty acid co-mediated uncoupling, through interference with lipoperoxyl radicals and via regulating the electron flow at the level of mitochondria [102].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [102]
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- Authors
- Ježek, J., Engstová, H., & Ježek, P.
- Affiliations
- Czech Academy of Sciences (CZ)
- Corresponding author
- Ježek, Petr
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 1858
- Issue
- 9
- Pages
- 750-762
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2618949193
- Cited by
- 30
- References
- 66
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 6 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 4
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- ASEP (submittedVersion, public-domain)
- Funders
- Grant Agency of the Czech Republic (17-01813S)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- SkQ1, antioxidant defense, mitochondrial superoxide, hydrogen peroxide, rotenone, ubiquinone binding site, cytochrome bc1 complex, complex I, electron flow, mitochondrial respiration, HepG2 cells
- MeSH terms
- Antimycin A, Antioxidants, Flavin-Adenine Dinucleotide, Glycolysis, Humans, Methacrylates, Mitochondria, NAD, Oxidation-Reduction, Oxidative Phosphorylation, Plastoquinone, Polyenes, Rotenone, Superoxides, Thiazoles, Electron Transport Complex III, Oxidative Stress, Electron Transport Complex I, Hep G2 Cells
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