Literature DB >> 26032482

Quercetin supplementation does not enhance cerebellar mitochondrial biogenesis and oxidative status in exercised rats.

Rafael A Casuso1, Antonio Martínez-Amat2, Fidel Hita-Contreras3, Daniel Camiletti-Moirón4, Pilar Aranda5, Emilio Martínez-López6.   

Abstract

The present study tested the hypothesis that quercetin may inhibit the mitochondrial and antioxidant adaptations induced by exercise in cerebellar tissue. Thirty-five 6-week-old Wistar rats were randomly allocated into the following groups: quercetin, exercised (Q-Ex; n = 9); quercetin, sedentary (Q-Sed; n = 9); no quercetin, exercised (NQ-Ex; n = 9); and no quercetin, sedentary (NQ-Sed; n = 8). After 6 weeks of quercetin supplementation and/or exercise training, cerebellums were collected. Protein carbonyl content (PCC), sirtuin 1, peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), messenger RNA levels, citrate synthase (CS), and mitochondrial DNA were measured. When Q-Sed was compared with NQ-Sed, PCC (P < .005) showed decreased levels, whereas PGC-1α, sirtuin 1 (both, P < .01), mitochondrial DNA (P < .001), and CS (P < .01) increased. However, when Q-Ex was compared with Q-Sed, PCC showed increased levels (P < .001), whereas CS decreased (P < .01). Furthermore, the NQ-Ex group experienced an increase in PGC-1α messenger RNA levels in comparison with NQ-Sed (P > .01). This effect, however, did not appear in Q-Ex (P < .05). Therefore, we must hypothesize that either the dose (25 mg/kg) or the length of the quercetin supplementation period that was used in the present study (or perhaps both) may impair exercise-induced adaptations in cerebellar tissue.
Copyright © 2015 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Flavonoids; Oxidative stress; PGC-1α; SIRT1; Training; Wistar rats

Mesh:

Substances:

Year:  2015        PMID: 26032482     DOI: 10.1016/j.nutres.2015.05.007

Source DB:  PubMed          Journal:  Nutr Res        ISSN: 0271-5317            Impact factor:   3.315


  4 in total

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4.  Galangin Induces Autophagy via Deacetylation of LC3 by SIRT1 in HepG2 Cells.

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  4 in total

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