Staphylococcus aureus in chronic rhinosinusitis: the effect on the epithelial chloride channel (cystic fibrosis transmembrane conductance regulator, CFTR) and the epithelial sodium channel (ENaC) physiology

2019 ◽  
Vol 139 (7) ◽  
pp. 652-658
Author(s):  
Amanj Saber ◽  
Sravya Sowdamini Nakka ◽  
Rashida Hussain ◽  
Svante Hugosson
Keyword(s):  
Cystic Fibrosis ◽  
Staphylococcus Aureus ◽  
Sodium Channel ◽  
Chronic Rhinosinusitis ◽  
Chloride Channel ◽  
Epithelial Sodium Channel ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Cystic Fibrosis Transmembrane ◽  
Epithelial Sodium Channel Enac

Association of Cystic Fibrosis Transmembrane Conductance Regulator with Epithelial Sodium Channel Subunits Carrying Liddle's Syndrome Mutations

2021 ◽  
Author(s):  
Arun K. Rooj ◽  
Estelle Cormet-Boyaka ◽  
Edlira B. Clark ◽  
Yawar J. Qadri ◽  
William Lee ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Sodium Channel ◽  
Epithelial Sodium Channel ◽  
Fluorescence Lifetime Imaging ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Physical Association ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Cystic Fibrosis Transmembrane

The association of the cystic fibrosis transmembrane conductance regulator (CFTR) and epithelial sodium channel (ENaC) in the pathophysiology of cystic fibrosis (CF) is controversial. Previously, we demonstrated a close physical association between wild type (WT) CFTR and WT ENaC. We have also shown that the F508del CFTR fails to associate with ENaC unless the mutant protein is rescued pharmacologically or by low temperature. In this study, we present the evidence for a direct physical association between WT CFTR and ENaC subunits carrying Liddle's syndrome mutations. We show that all three ENaC subunits bearing Liddle's syndrome mutations (both point mutations and the complete truncation of the carboxy terminus), could be co-immunoprecipitated with WT CFTR. The biochemical studies were complemented by fluorescence lifetime imaging microscopy (FLIM), a distance-dependent approach that monitors protein-protein interactions between fluorescently labeled molecules. Our measurements revealed significantly increased FRET between CFTR and all tested ENaC combinations as compared to controls (ECFP and EYFP co-transfected cells). Our findings are consistent with the notion that CFTR and ENaC are within reach of each other even in the setting of Liddle's syndrome mutations, suggestive of a direct intermolecular interaction between these two proteins.

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