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Comparative processing and function of human and ferret cystic fibrosis transmembrane conductance regulator
Journal article   Open access   Peer reviewed

Comparative processing and function of human and ferret cystic fibrosis transmembrane conductance regulator

John T Fisher, Xiaoming Liu, Ziying Yan, Meihui Luo, Yulong Zhang, Weihong Zhou, Ben J Lee, Yi Song, Chenhong Guo, Yujiong Wang, …
The Journal of biological chemistry, Vol.287(26), pp.21673-21685
06/22/2012
DOI: 10.1074/jbc.M111.336537
PMCID: PMC3381131
PMID: 22570484
url
https://doi.org/10.1074/jbc.M111.336537View
Published (Version of record) Open Access

Abstract

The most common cystic fibrosis transmembrane conductance regulator (CFTR) gene mutation is ΔF508, and this causes cystic fibrosis (CF). New CF models in the pig and ferret have been generated that develop lung, pancreatic, liver, and intestinal pathologies that reflect disease in CF patients. Species-specific biology in the processing of CFTR has demonstrated that pig and mouse ΔF508-CFTR proteins are more effectively processed to the apical membrane of airway epithelia than human ΔF508-CFTR. The processing behavior of ferret WT- and ΔF508-CFTR proteins remains unknown, and such information is important to predicting the utility of a ΔF508-CFTR ferret. To this end, we sought to compare processing, membrane stability, and function of human and ferret WT- and ΔF508-CFTR proteins in a heterologous expression system using HT1080, HEK293T, BHK21, and Cos7 cells as well as human and ferret CF polarized airway epithelia. Analysis of the protein processing and stability by metabolic pulse-chase and surface On-Cell Western blots revealed that WT-fCFTR half-life and membrane stability were increased relative to WT-hCFTR. Furthermore, in BHK21, Cos7, and CuFi cells, human and ferret ΔF508-CFTR processing was negligible, whereas low levels of processing of ΔF508-fCFTR could be seen in HT1080 and HEK293T cells. Only the WT-fCFTR, but not ΔF508-fCFTR, produced functional cAMP-inducible chloride currents in both CF human and ferret airway epithelia. Further elucidation of the mechanism responsible for elevated fCFTR protein stability may lead to new therapeutic approaches to augment CFTR function. These findings also suggest that generation of a ferret CFTR(ΔF508/ΔF508) animal model may be useful.
Recombinant Proteins - metabolism Cell Line Cricetinae Phosphorylation Species Specificity Humans Cystic Fibrosis Transmembrane Conductance Regulator - physiology Glycosylation Chlorides - chemistry Permeability Ferrets Animals HEK293 Cells Cystic Fibrosis Transmembrane Conductance Regulator - genetics Golgi Apparatus - metabolism Cell Membrane - metabolism Protein Processing, Post-Translational Mutation COS Cells

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