Abstract
Resveratrol (RSV) is a bioactive natural molecule that induces antioxidant activity and increases protection against oxidative damage. RSV could be used to mitigate damages associated to metabolic diseases and aging. Particularly, RSV regulates different aspects of mitochondrial metabolism. However, no information is available about the effects of RSV on Coenzyme Q (CoQ), a central component in the mitochondrial electron transport chain. Here, we report for the first time that RSV modulates COQ genes and parameters associated to metabolic syndrome in mice. Mice fed with high fat diet (HFD) presented a higher weight gain, triglycerides (TGs) and cholesterol levels while RSV reverted TGs to control level but not weight or cholesterol. HFD induced a decrease of COQs gene mRNA level, whereas RSV reversed this decrease in most of the COQs genes. However, RSV did not show effect on CoQ9, CoQ10 and total CoQ levels, neither in CoQ-dependent antioxidant enzymes. HFD influenced mitochondrial dynamics and mitophagy markers. RSV modulated the levels of PINK1 and PARKIN and their ratio, indicating modulation of mitophagy. In summary, we report that RSV influences some of the metabolic adaptations of HFD affecting mitochondrial physiology while also regulates COQs gene expression levels in a process that can be associated with mitochondrial dynamics and turnover.
Highlights
Coenzyme Q (CoQ) is a redox lipidic component of cell membranes
It has been demonstrated that a mitochondrial protein, ferroptosis suppressor protein 1 (FSP1, formerly known as apoptosis-inducing factor mitochondrial 2, AIF2), can move from mitochondria to plasma membrane to maintain the antioxidant capacity of ubiquinol in this membrane [8,9]
We introduce a new aspect of this modulation, the regulation of the expression of the genes involved in the synthesis of CoQ that are repressed in RSV has shown clear activity to influence mitochondrial function in many models showing mitochondrial dysfunction [20,21,25,33,42]
Summary
Coenzyme Q (CoQ) is a redox lipidic component of cell membranes. It is mainly located within mitochondria but significant amounts are found in sub-cellular organelles such as lysosomes, peroxisomes, the endoplasmic reticulum and Golgi apparatus [1]. Inside and outside cells to maintain their respective antioxidant activity. To perform this antioxidant activity, membrane linked redox enzymes such as Cytochrome b5 reductase (CYTB5 R) and NAD(P)H. Antioxidants 2020, 9, 431 quinone dehydrogenase 1 (NQO1) [6] transfer electrons from cytosolic NAD(P)H to CoQ to maintain high levels of the reduced form, ubiquinol, the active form [7]. A new oxidoreductase enzyme linked to the outer side of plasma membrane of hepatocytes has been discovered to reduce CoQ located in blood plasma lipoproteins [10]
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