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Department of Physiology, McGill University, Montréal, Québec, Canada H3G 1Y6
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.
cystic fibrosis; chloride channel; lung defense; airway surface fluid; multidrug resistance protein ; cystic fibrosis transmembrane conductance regulator
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