A Homogeneous Cell-Based Halide-Sensitive Yellow Fluorescence Protein Assay to Identify Modulators of the Cystic Fibrosis Transmembrane Conductance Regulator Ion Channel

2017 ◽  
Vol 15 (8) ◽  
pp. 395-406 ◽  
Author(s):  
Emery Smith ◽  
Kenneth A. Giuliano ◽  
Justin Shumate ◽  
Pierre Baillargeon ◽  
Brigid McEwan ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channel ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Yellow Fluorescence ◽  
Protein Assay ◽  
Yellow Fluorescence Protein ◽  
Homogeneous Cell ◽  
Fluorescence Protein ◽  
Cystic Fibrosis Transmembrane

Glutathione permeability of CFTR

1998 ◽  
Vol 275 (1) ◽  
pp. C323-C326 ◽  
Author(s):  
Paul Linsdell ◽  
John W. Hanrahan
Keyword(s):  
Oxidative Stress ◽  
Cystic Fibrosis ◽  
Ion Channel ◽  
Airway Epithelial Cells ◽  
Transmembrane Conductance Regulator ◽  
Airway Epithelial ◽  
Transmembrane Conductance ◽  
High Concentrations ◽  
Cystic Fibrosis Transmembrane ◽  
Glutathione Transport

The cystic fibrosis transmembrane conductance regulator (CFTR) forms an ion channel that is permeable both to Cl− and to larger organic anions. Here we show, using macroscopic current recording from excised membrane patches, that the anionic antioxidant tripeptide glutathione is permeant in the CFTR channel. This permeability may account for the high concentrations of glutathione that have been measured in the surface fluid that coats airway epithelial cells. Furthermore, loss of this pathway for glutathione transport may contribute to the reduced levels of glutathione observed in airway surface fluid of cystic fibrosis patients, which has been suggested to contribute to the oxidative stress observed in the lung in cystic fibrosis. We suggest that release of glutathione into airway surface fluid may be a novel function of CFTR.

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