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Laryngoscope. 2018 Dec;128(12):E393-E401. doi: 10.1002/lary.27510. Epub 2018 Oct 16.

ROS Is Involved in Disruption of Tight Junctions of Human Nasal Epithelial Cells Induced by HRV16.

Author information

1
Department of Otolaryngology-Head & Neck Surgery, Gachon University Gil Medical Center, Incheon, Republic of Korea.

Abstract

OBJECTIVE:

Rhinoviruses (RV), which are responsible for the majority of common colds, induce mucus overproduction, increased vascular permeability, and secondary bacterial infection. These symptoms are primarily caused by barrier function disruption, which is controlled by intercellular junctions. In this study, we investigated whether reactive oxygen species (ROS) are closely involved in tight junction disruption of primary human nasal epithelial (HNE) cells induced by infection of RV .

METHODS AND RESULTS:

Incubation with RV resulted in disruption of tight junction proteins (ZO-1, E-cadherin, claudin-1, and occludin) in HNE cells. Pretreatment with diphenylene iodonium (DPI) decreased RV-induced disruption of tight junction in HNE cells. RV-induced generation of ROS was diminished by DPI. However, rotenone was not inhibited in HNE cells following incubation with RV. Rhinoviruses resulted in a marked decrease in protein phosphatases activity and an increase in protein tyrosine phosphorylation levels in HNE cells. Diphenylene iodonium inhibited the RV-induced inactivation of phosphatases and phosphorylation of protein tyrosine. In addition, inhibition of protein tyrosine phosphatases with phenylarsine oxide resulted in a marked decrease in protein phosphatase activity and disruption of tight junction proteins in HNE cells.

CONCLUSION:

Our results suggest that ROS-mediated inhibition of phosphatases plays a crucial role in disruption of tight junctions in HNE cells by RV. The data suggest that RV infection may damage nasal epithelial barrier function.

LEVEL OF EVIDENCE:

NA Laryngoscope, 128:E393-E401, 2018.

KEYWORDS:

Human rhinovirus; ROS; human nasal epithelial cells; protein tyrosine phosphatases; tight junction proteins

PMID:
30325507
DOI:
10.1002/lary.27510
[Indexed for MEDLINE]

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