Resveratrol suppresses lipoprotein‐associated phospholipase A<sub>2</sub> expression by reducing oxidative stress in macrophages and animal models

Sun, Shengnan; Zhang, Mingjun; Yang, Qingbiao; Shen, Ziying; Chen, Jiahuan; Yu, Biao; Wang, He; Qu, Jiali; Pang, Daxin; Ren, Wenzhi; Ouyang, Hongsheng; Tang, Xiaochun

doi:10.1002/mnfr.201601112

Cited by 20 publications

(18 citation statements)

References 41 publications

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“…High content atherogenic diets induce significant liver damage in both humans and laboratory animals and are responsible for fatty liver disease [140,141]. Studies have demonstrated the hepatoprotective effects of resveratrol in the high-fat dietary model of liver damage [142][143][144][145].…”

Section: Resveratrol In Liver Damage Induced By Atherogenic Dietmentioning

confidence: 99%

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

et al. 2021

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Many studies have shown that resveratrol has a lot of therapeutic effects on liver disorders. Its administration can significantly increase the survival rate after liver transplantation, reduce fat deposition and ischemia-induced necrosis and apoptosis in Wistar rats. Resveratrol can provide Liver protection against chemical, cholestatic, and alcohol-mediated damage. It can improve glucose metabolism and lipid profile, reduce liver fibrosis, and steatosis. Additionally, it is capable of altering the fatty acid composition of the liver cells. Resveratrol may be a potential treatment option for the management of non-alcoholic fatty liver disease (NAFLD) due to its anti-inflammatory, antioxidant, and calorie-restricting effects. There are also studies that have evaluated the effect of resveratrol on lipid and liver enzyme profiles among patients with metabolic syndrome (MetS) and related disorders. Based on the extent of liver disease worldwide and the need to find new treatment possibilities, this review critically examines current in vitro and in vivo preclinical studies and human clinical studies related to liver protection.

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Section: Resveratrol In Liver Damage Induced By Atherogenic Dietmentioning

confidence: 99%

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

et al. 2021

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“…A sharp rise in ROS generation leads to the opening of MPTP, resulting in the imbalance of H + on the inner membrane of mitochondria, destroys membrane proteins, inhibits ATP synthesis, and causes mitochondrial swelling, all of which may exacerbate necrotic or apoptotic cascades leading to rapid cell death [91]. Resveratrol is able to reinstate SIRT1 activation which resists against oxidative stress through the upregulation of antioxidants such as superoxide dismutase 2 (SOD2), which inhibits the mitochondrial injury by swapping out excessively generated ROS [92]. It has also been found that cyclosporine A (CsA) can inhibit MPTP constitution protein cyclophilin D to protect mitochondrial functional integrity under severe shocks [93].…”

Section: Sirt1 Helps Alleviate Oxidative Stress In Dilimentioning

confidence: 99%

The Beneficial Roles of SIRT1 in Drug-Induced Liver Injury

Yan

Huang

Nisar

et al. 2019

Oxidative Medicine and Cellular Longevity

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Drug-induced liver injury (DILI) is a major cause of acute liver failure (ALF) as a result of accumulated drugs in the human body metabolized into toxic agents and helps generate heavy oxidative stress, inflammation, and apoptosis, which induces necrosis in hepatocytes and ultimately damages the liver. Sirtuin 1 (SIRT1) is said to have multiple vital roles in cell proliferation, aging, and antistress systems of the human body. The levels of SIRT1 and its activation precisely modulate its critical role in the interaction between multiple step procedures of DILI. The nuclear factor kappa-light-chain-enhancer of activated B cell- (NF-κB-) mediated inflammation signaling pathway, reactive oxygen species (ROS), DNA damage, mitochondrial membrane potential collapse, and endoplasmic reticulum (ER) stress also contribute to aggravate DILI. Apoptosis is regarded as the terminal reaction followed by multiple signaling cascades including caspases, p53, and mitochondrial dysfunction which have been said to contribute in DILI. The SIRT1 activator is regarded as a potential candidate for DILI, because the former could inhibit signaling of p53, NF-κB, and ER stress. On the other hand, overexpression of SIRT1 also enhances the activation of antioxidant responses via Kelch-like ECH-associated protein 1- (Keap1-) nuclear factor- (erythroid-derived 2-) like 2 (Nrf2) signaling. The current manuscript will highlight the mechanism of DILI and the interaction of SIRT1 with various cytoplasmic factors leading to DILI along with the summary of potent SIRT1 agonists.

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“…By contrast, healthy gingival tissues did not express SIRT1 or 8-OHdG. SIRT1 inhibits oxidative stress by upregulating superoxide dismutase 2 (44), and resveratrol reduces oxidative stress in macrophages (45). Therefore, we hypothesized that SIRT1 and 8-OHdG are co-expressed in periapical granulomas as a result of oxidative stress-mediated damage to inflammatory cells, which enhances the wound healing activity of these cells.…”

Section: Discussionmentioning

confidence: 95%

Expression of silent information regulator 2 homolog 1 (SIRT1) in periapical granulomas

et al. 2018

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Silent information regulator 2 homolog 1 (SIRT1) inhibits oxidative injury and has anti-inflammatory effects. SIRT1 may be involved in healing of periapical periodontitis; however, SIRT1 expression in periapical periodontitis lesions has not been investigated. This study evaluated SIRT1 expression and a marker of oxidative stress-8-hydroxy-2'-deoxyguanosine (8-OHdG)-in periapical granulomas. First, we used real-time polymerase chain reaction to determine whether U-937 monocytes express SIRT1. U-937 cells treated with the SIRT1 activator resveratrol exhibited the highest SIRT1 mRNA level after 6-h incubation. By contrast, treating cells with the SIRT1 inhibitor sirtinol returned SIRT1 expression level to that of the control. In addition, immunocytochemical analysis using cytospin specimens showed that U-937 cells co-expressed SIRT1 and Ki-67. Dual-color immunofluorescence imaging showed that round cells in periapical granulomas co-expressed SIRT1 and 8-OHdG; however, neither was expressed in healthy gingival tissues. The number of 8-OHdG-expressing cells was significantly greater than the number of SIRT1-expressing cells. Our findings suggest that macrophages express SIRT1 and that wound healing in periapical granulomas is enhanced by a SIRT1-mediated reduction in the level of oxidative stress.

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Resveratrol suppresses lipoprotein‐associated phospholipase A₂ expression by reducing oxidative stress in macrophages and animal models

Abstract: Based on our results, the protective effects of resveratrol on cardiovascular events may be related to its ability to suppress Lp-PLA expression.

Cited by 20 publications

References 41 publications

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

The Beneficial Roles of SIRT1 in Drug-Induced Liver Injury

Expression of silent information regulator 2 homolog 1 (SIRT1) in periapical granulomas

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Resveratrol suppresses lipoprotein‐associated phospholipase A2 expression by reducing oxidative stress in macrophages and animal models

Abstract: Based on our results, the protective effects of resveratrol on cardiovascular events may be related to its ability to suppress Lp-PLA expression.

Cited by 20 publications

References 41 publications

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

The Role of Resveratrol in Liver Disease: A Comprehensive Review from In Vitro to Clinical Trials

The Beneficial Roles of SIRT1 in Drug-Induced Liver Injury

Expression of silent information regulator 2 homolog 1 (SIRT1) in periapical granulomas

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Resveratrol suppresses lipoprotein‐associated phospholipase A₂ expression by reducing oxidative stress in macrophages and animal models