Analgesic effect and related amino acids regulation of ginsenoside Rg3 in mouse pain models.

AIMS: The present study aims to evaluate the analgesic effect of ginsenoside Rg3 in different mouse pain models. MAIN METHODS: Formalin-, carrageenan- and S180 tumor cells induced mouse pain models were built in the study. The licking and biting time and PEG2 contents in the inflammatory sites were measured. The excitatory and inhibitory amino acids in the brains were determined by pre-column derivation FLD-HPLC method. KEY FINDING: We have found that ginsenoside Rg3 treated the pain phases and decreased the PGE2 in formalin and carrageenan induced models, respectively. It significantly increased the contents of EAAs (Asp and Glu) in the brains of S180 tumor inducing pain mice, meanwhile, the IAAs (Gly, Tau and GABA) decreased. SIGNIFICANCE: Our results revealed that ginsenoside Rg3 acted central and peripheral analgesic effect and regulated the inflammatory factors and pain-related amino acids. It could re-balance the abnormal EAAs/IAAs value when the pain occurred. The analgesic mechanism and the clinical application of ginsenoside Rg3 need be evaluated furtherly.

Binding effect of fluorescence labeled glycyrrhetinic acid with GA receptors in hepatocellular carcinoma cells.

Glycyrrhetinic acid (GA) is a natural active component from licorice, which is broadly used in traditional Chinese medicine. Lots of glycyrrhetinic acid receptors (GA-R) are proved to locate on the surface of liver cells. Many reports about the hepatocellular carcinoma (HCC) treatment were dependent on GA modified carriers. However, the reality of GA-R in HCC cells was not clear. In this paper, 18ß-glycyrrhetinic acid (18ß-GA) was labeled with fluorescence (FITC) by chemical synthesis. Together with the binding effect of fluorescence labeled glycyrrhetinic acid (FITC-GA), the competitive action of 18ß-GA with GA-R was investigated in HCC cells. The results showed that in HepG2 cells, 18ß-GA and FITC-GA presented similar cytotoxicity. The specific binding saturation of GA showed the dissociation constant (Kd) was 7.457±2.122pmol/L and the maximum binding counts (Bmax) was 2.385±0.175pmol/2.5×106 cells, respectively. FITC-GA bound to cytomembrane specifically and 18ß-GA competed to bind the sites significantly in HepG2 cells. Therefore, there is binding effect between fluorescence labeled GA and GA-R. The GA-R on HCC cells is confirmed as expected, which provides a useful reference of active target modified by GA and a novel approach for receptors and ligands study.