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Am J Physiol Lung Cell Mol Physiol 277: L113-L118, 1999;
1040-0605/99 $5.00
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Vol. 277, Issue 1, L113-L118, July 1999

Abnormal glutathione transport in cystic fibrosis airway epithelia

Lin Gao1, Kwang Jin Kim1,2, James R. Yankaskas3, and Henry Jay Forman1

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), Delta F508 homozygous, two clones] and one of the CFT1 clones transfected with either normal CFTR (CFTR repleted) or beta -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. gamma -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.

gamma -glutamyl transpeptidase; epithelial lung lining fluid; cystic fibrosis transmembrane conductance regulator; thiol


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