Inhibitory Effect of Ginsenosides Rh1 and Rg2 on Oxidative Stress in LPS-Stimulated RAW 264.7 Cells

Minor ginsenosides Rh1 and Rg2 were isolated from Korean red ginseng and reported to have various biological effects on anti-inflammatory and anti-stress activities. However, the effects of Rh1 and Rg2 on antioxidant activity and their regulatory effects on the antioxidant enzymes have not been studied. Since oxidative stress is one of the major toxic inflammatory responses stimulated by lipopolysaccharides (LPS), the present study investigated the role of minor ginsenosides Rh1 and Rg2 on antioxidant effects in LPS-treated RAW 264.7 cells. In this study, we found that treatment with ginsenosides Rh1 and Rg2 strongly inhibited LPS-stimulated intracellular ROS production in cells. Luciferase assay showed that treatment with LPS reduced antioxidant response element (ARE) encoding the pARE-luc promoter activity, while ginsenosides inhibited the pARE-luc promoter activity. Moreover, ginsenosides Rh1 and Rg2 exhibited anti-oxidative activity in LPS-induced cells by upregulating antioxidant enzymes including superoxide dismutase, catalase, and glutathione peroxidase. Our results suggest that minor ginsenosides Rh1 and Rg2 may be potential bio-active compounds for antioxidative effects by inhibiting the generation of ROS in RAW 264.7 cells.

Effects of LPS on the organization and localization of VE-cadherin and F-actin in cultured endothelial cells / 中国病理生理杂志

AIM: This experiment is to investigate the effects of LPS on the organization and localization of VE-cadherin and F-actin in cultured human umbilical endothelial cells.METHODS: The human umbilical vein endothelial cell lines ECV-304 were incubated with LPS at different concentrations for 30 min. VE-cadherin was detected by immunofluorescence with primary mAb of VE-cadherin and FITC-conjugated secondary antibody. F-actin was detected with fluorescence staining with rodamine-phalloidin. RESULTS: At high concentration, LPS could induce reorganization of VE-cadherin with the formation of serrata cellular border and enlargement of intercellular gaps, which were apparently different from that in normal conditions with the high fluorescence intensity at cell-cell junction. F-actin depolymerization could also be induced by LPS at high concentration with the formation of stress fiber and filopodia. CONCLUSION: LPS(300 ?g/L) could induce reorganization of VE-cadherin and F-actin in human umbilical vein endothelial cells.