Ginsenoside Re Protects Rhinovirus-Induced Disruption Of Tight Junction Through Inhibition Of ROS-Mediated Phosphatases Inactivation In Human Nasal Epithelial Cells

RATIONALE: Maintaining tight junction integrity contributes significantly to epithelial barrier function. If the barrier function is destroyed, the permeability of the cells increases, and the movement of the pathogens is promoted, thereby further increasing susceptibility the secondary infection. Here, we examined the protective effects of Ginsenoside Re on rhinovirus (RV)-induced tight junction disruption in primary human nasal epithelial cells (HNE).

METHODS: Primary human nasal epithelial cells grown at an air-liquid interface were infected apically with RV. After RV infection and subsequent treatment with Ginsenoside Re, Rb1 and Rc, changes in the expression of tight junction proteins were determined using western blot analysis. ROS production was measured by staining cells with H₂DCF-DA and analyzed by flow cytometry and confocal microscopy. Phosphatase activity was measured using a Tyrosine Phosphatase Assay System kit.

RESULTS: Incubation with RV resulted in disruption of tight junction proteins (ZO-1, E-cadherin, claudin-1, and occludin) in HNE cells. Pretreatment with Ginsenoside Re decreased RV-induced disruption of tight junction in HNE cells. RV-induced generation of ROS was diminished by Ginsenoside Re. However, Ginsenoside Rb1 and Rc were not inhibited tight junction disruption and ROS generation in nasal epithelial cells following incubation with RV. RV resulted in a marked decrease in protein phosphatases activity and an increase in protein tyrosine phosphorylation levels in HNE cells. Ginsenoside Re inhibited the RV-induced inactivation of phosphatases and phosphorylation of protein tyrosine.

CONCLUSIONS: Our results identified Ginsenoside Re as an effective compound that prevents RV-induced tight junction disruption in HNE cells.