Abstract
Glycyrrhhizic acid (GA), including 18α-glycyrrhizic acid (18α-GA) and 18β-glycyrrhizic acid (18β-GA), is the main active ingredient of licorice. GA is generally considered an effective pharmacological strategy protecting against hepatic disease; however, the optimal compatibility proportion of 18α-GA and 18β-GA against alcoholic liver disease (ALD) and the underlying mechanism are not well established. Hence, this study was designed to explore the optimal compatibility proportion of 18α-GA and 18β-GA against ALD, followed by investigating the underlying mechanisms. SD rats were administered 40% ethanol once a day, accompanied by treatment with different proportions of 18α-GA and 18β-GA for four weeks. Then all rats were anesthetized with chloral hydrate and blood samples were taken from the abdominal aorta for biochemical assay. Livers were also collected and the liver function, lipid profile, ROS production, and mRNA and protein levels of related genes involved in lipid metabolism were assessed. The results showed that 18α-GA and 18β-GA, particularly at a proportion of 4:6, significantly reduced liver damage, lipid accumulation, and oxidative stress in ethanol-induced rats, as indicated by the decreased levels of alanine aminotransferase (ALT) and aminotransferase (AST) in serum, improvement of liver histopathological changes, regulation of total cholesterol (TC), total triglyceride (TG), high-density lipoprotein cholesterol (HDL-C), and low-density lipoprotein cholesterol (LDL-C), and modulation of superoxide dismutase (SOD), glutathione (GSH), and malonaldehyde (MDA). Moreover, the combination treatment with 18α-GA and 18β-GA substantially reduced the mRNA and protein levels of sterol regulatory element-binding protein-1c (SREBP-1c) and acetyl-coal carboxylase (ACC); meanwhile, increased levels of peroxisome proliferators activated receptor-α (PPAR-α) and carnitine palmitoy transferase-1 (CTP-1) in the liver tissues of ethanol-induced rats. In conclusion, our results indicated that the optimal compatibility proportion of 18α-GA and 18β-GA protecting against ALD was 4:6, and the mechanism was associated with the regulation of oxidative stress and lipid metabolism.
Highlights
Alcoholic liver disease (ALD) remains a leading cause of morbidity and mortality worldwide [1,2].The cause of ALD is not well established; several studies indicate that alcohol-induced hepatotoxicity, oxidative stress, and complex interactions between alcohol metabolism, hepatic cells, and multiple cytokines may be responsible for the progression of ALD [3,4,5]
These results indicated that 18α-Glycyrrhhizic acid (GA) combined with 18β-glycyrrhizic acid (18β-GA) at the ratio of 4:6 and 2:8 effectively ameliorated ethanol-induced liver injury by modulation oxidative stress via suppressing MDA and increasing levels of superoxide dismutase (SOD) and GSH
The present study mainly focused on investigating the ameliorative effects of 18α-glycyrrhizic acid (18α-GA) and 18β-GA on ethanol-induced liver injury, and further exploring the mechanisms of action
Summary
Alcoholic liver disease (ALD) remains a leading cause of morbidity and mortality worldwide [1,2]. A retraction notice was published on 9 March 2019 in Molecules 2019, 5, 969; doi:10.3390/molecules24050969. The roots and stolons of some Glycyrrhiza species, has been widely used for medicinal purposes for thousands of years [12]. It is used worldwide in food products as a sweetening and flavoring component owing to its sweet taste. The optimal compatibility proportion of 18α-GA and 18β-GA protecting against ALD has not been studied and the molecular mechanism underlying the effect of GA on ALD remains to be elucidated. The present study was, designed to investigate the optimal compatibility proportion of 18α-GA and 18β-GA protecting against liver injury induced by ethanol. Additional study revealed that the possible mechanism was associated with its prevention on the development of hepatic steatosis by modulating oxidative stress and hepatic lipid accumulation via regulation of sterol regulatory element-binding protein-1c (SREBP-1c), Acetyl-CoA carboxylase (ACC), peroxisome proliferator-activated receptor-α (PPAR-α), and carnitine palmitocyl transferase-1a (CPT-1a)
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