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Front Pharmacol
2019 Jun 14;10:686. doi: 10.3389/fphar.2019.00686.
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Ginkgo biloba Extract Modulates the Retroperitoneal Fat Depot Proteome and Reduces Oxidative Stress in Diet-Induced Obese Rats.
Hirata BKS
,
Pedroso AP
,
Machado MMF
,
Neto NIP
,
Perestrelo BO
,
de Sá RDCC
,
Alonso-Vale MIC
,
Nogueira FN
,
Oyama LM
,
Ribeiro EB
,
Tashima AK
,
Telles MM
.
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The rapid increase in the number of individuals with obesity, over the past four decades, is triggered by a number of complex interactions among factors. Despite the plethora of treatments available, side effects are commonly observed and, in this context, herbal medicines have been employed as an alternative form of therapy. Ginkgo biloba extract (GbE) has been described as a promising new pharmacological approach to treat obesity. In order to better comprehend the mechanisms involved with this potential effect, the present study evaluated the effects of GbE treatment on diet-induced obese rats, focusing on the proteome and the oxidative stress defense system of visceral adipose tissue. After 14 days treatment, GbE significantly modulated 25 proteins. Retroperitoneal adipose tissue of treated animals exhibited higher amounts of proteins associated with adipogenesis (decorin), carbon metabolism and mitochondrial function (citrate synthase), and a concomitant reduction in adipocyte hypertrophy. In parallel, GbE down-regulated proteins involved in oxidative stress (peroxiredoxin) and the inflammatory response (complement C3, mast cell protease 1, and Ig gamma-2B chain C region). Moreover, also related to oxidative stress defense, GbE stimulated catalase activity, reduced malondialdehyde levels (lipid peroxidation indicator), and increased lactoylglutathione lyase levels. It was concluded that GbE acts as an antioxidant agent, and improved the proteome profile and oxidative stress response in the adipose tissue of diet-induced obese rats.
Figure 1. The chemical structures of the Ginkgo biloba extract (GbE) based on the high-performance liquid chromatography (HPLC) profile of the extract performed by the manufacturer: (A) quercetin; (B) kaempferol; (C) gingkolide A; (D) ginkgolide B; (E) ginkgolide C; (F) (-) bilobalide.
Figure 2.
(A) Levels of malondialdehyde (MDA) measured in retroperitoneal adipose tissue of the HFD and HFD+GbE groups (µM/mg protein); (B) retroperitoneal adipocyte volume of the HFD and HFD+GbE groups (ρL). Values are expressed as the mean ± SEM (n = 5–7).
Figure 3. Graphic representation of the protein-protein interaction networks with significant differences between the HFD and HFD+GbE groups in retroperitoneal adipose tissue. Nodes represent individual proteins annotated with common gene names: Got2, Aspartate aminotransferase; Blvra, biliverdin reductase A; Hnrnph1, heterogeneous nuclear ribonucleoprotein H; Hrg, histidine-rich glycoprotein; Kng1, T-kininogen 1; rMCP-1, mast cell protease 1; S100a1, protein S100-A1; Acaa1a, 3-ketoacyl-CoA thiolase B; Tkt, transketolase; Apoa1, apolipoprotein A-I; C3, complement C3; Hadha, trifunctional enzyme subunit alpha; Fetub, fetuin-B; Arhgdia, Rho GDP-dissociation inhibitor 1; Igh-1a, Ig gamma-2B chain C region, Prdx-1, peroxiredoxin-1; S100a11, protein S100-A11; Sdpr, caveolae-associated protein 2; Serpina3k, serine protease inhibitor A3K; Ctsd, cathepsin D; Cs, citrate synthase, mitochondrial; Glo1, lactoylglutathione lyase, Dcn, decorin; Tuba1b, tubulin. Vectors between nodes are color coded to represent different levels of information: black, evidence of co-expression; pink, interactions experimentally determined; blue, association in curated databases; yellow, co-mentioned in PubMed abstracts; green, neighborhood in the genome.
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