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Departments of 1 Molecular Pharmacology and Toxicology and 2 Medicine, Will Rogers Institute Pulmonary Research Center, University of Southern California, Los Angeles, California 90033; and 3 Department of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599
Glutathione (GSH)
is a potentially important component of antioxidant defense in the
epithelial lung lining fluid. Cystic fibrosis (CF) patients have
chronic inflammation in which oxidative stress can be a factor. To
examine the hypothesis that the transport of GSH content was defective
in CF patients, intracellular and extracellular GSH were measured by
HPLC. Four cell lines were used: CFT1 cells [with defective CF
transmembrane conductance regulator (CFTR), 
F508 homozygous, two
clones] and one of the CFT1 clones transfected with either normal
CFTR (CFTR repleted) or 
-galactosidase. GSH content in the apical
fluid was 55% lower in CFTR-deficient cultures than in CFTR-repleted
cells (P < 0.001). In contrast,
intracellular GSH content was similar in CFT1 cells and CFTR-repleted
cells. 
-Glutamyl transpeptidase activity, which degrades
extracellular GSH, did not account for differences in apical GSH.
Rather, GSH efflux of CFTR-deficient cells was lower than that of
CFTR-repleted cells. These studies suggested that decreased GSH content
in the apical fluid in CF resulted from abnormal GSH transport
associated with a defective CFTR.
-glutamyl transpeptidase; epithelial lung lining fluid; cystic
fibrosis transmembrane conductance regulator; thiol
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