Abstract

Cell penetrating peptide derived from human eosinophil cationic protein (CPPecp) is a 10-amino-acid peptide containing a core heparan sulfate (HS)-binding motif of human eosinophil cationic protein (ECP). It binds and penetrates bronchial epithelial cells without cytotoxic effects. Here we investigated airway-protective effects of CPPecp in BEAS-2B cell line and mite-induced airway allergic inflammation in BALB/c mice. In BEAS-2B cell, CPPecp decreases ECP-induced eotaxin mRNA expression. CPPecp also decreases eotaxin secretion and p-STAT6 activation induced by ECP, as well as by IL-4. In vivo studies showed CPPecp decreased mite-induced airway inflammation in terms of eosinophil and neutrophil count in broncho-alveolar lavage fluid, peri-bronchiolar and alveolar pathology scores, cytokine production in lung protein extract including interleukin (IL)-5, IL-13, IL-17A/F, eotaxin; and pause enhancement from methacholine stimulation. CPPecp treated groups also showed lower serum mite-specific IgE level. In this study, we have demonstrated the in vitro and in vivo anti-asthma effects of CPPecp.

Details

Title
Cell Penetrating Peptide Derived from Human Eosinophil Cationic Protein Decreases Airway Allergic Inflammation
Author
Lin-shien Fu 1   VIAFID ORCID Logo  ; Yu-Rou Wu 2 ; Shun-lung Fang 2 ; Tsai, Jaw-ji 3 ; Heng-kuei Lin 4 ; Yee-jun, Chen 4 ; Ting-Yu, Chen 2 ; Margaret Dah-Tsyr Chang 5 

 Pediatric Department, Taichung Veterans General Hospital, Taichung, Taiwan; Pediatrics Department, National Yang-Ming Medical University, Taipei, Taiwan 
 Institute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, Taiwan 
 Medical Research Department, Taichung Veterans General Hospital, Taichung, Taiwan 
 Pediatric Department, Taichung Veterans General Hospital, Taichung, Taiwan 
 Institute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, Taiwan; Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan 
Pages
1-11
Publication year
2017
Publication date
Sep 2017
Publisher
Nature Publishing Group
e-ISSN
20452322
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1957776743
Copyright
© 2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.