Augmentation of Cystic Fibrosis Transmembrane Conductance Regulator Function in Human Bronchial Epithelial Cells via SLC6A14-Dependent Amino Acid Uptake. Implications for Treatment of Cystic Fibrosis

• Published in: American journal of respiratory cell and molecular biology Vol. 61; no. 6; pp. 755 - 764
• Main Authors: Ahmadi, Saumel, Wu, Yu-Sheng, Li, Mingyuan, Ip, Wan, Lloyd-Kuzik, Andrew, Di Paola, Michelle, Du, Kai, Xia, Sunny, Lew, Alexandria, Bozoky, Zoltan, Forman-Kay, Julie, Bear, Christine E, Gonska, Tanja
• Format: Journal Article
• Language: English
• Published: United States American Thoracic Society 01.12.2019
• Subjects: Airway management; Amino Acid Transport Systems - antagonists & inhibitors; Amino Acid Transport Systems - genetics; Amino Acid Transport Systems - physiology; Amino acids; Arginine; Arginine - metabolism; Biological Transport; Bronchi - cytology; Bronchi - metabolism; Cells, Cultured; Cystic fibrosis; Cystic Fibrosis - metabolism; Cystic Fibrosis - therapy; Cystic Fibrosis Transmembrane Conductance Regulator - deficiency; Cystic Fibrosis Transmembrane Conductance Regulator - genetics; Cystic Fibrosis Transmembrane Conductance Regulator - physiology; Epithelial cells; Epithelial Cells - drug effects; Epithelial Cells - metabolism; Genes, Reporter; Humans; Lung diseases; Nitric Oxide - metabolism; Nitric Oxide Synthase Type II - antagonists & inhibitors; Nitric Oxide Synthase Type II - metabolism; Recombinant Proteins - metabolism; Surface Properties; Transduction, Genetic; Tryptophan - analogs & derivatives; Tryptophan - pharmacology; nitric oxide pathway; F508del-CFTR; human bronchial epithelial cells; cystic fibrosis; SLC6A14

SLC6A14-mediated l-arginine transport has been shown to augment the residual anion channel activity of the major mutant, F508del-CFTR, in the murine gastrointestinal tract. It is not yet known if this transporter augments residual and pharmacological corrected F508del-CFTR in primary airway epitheli...