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• W1874417194 endingPage "C1099" @default.
• W1874417194 startingPage "C1088" @default.
• W1874417194 abstract "The pleiotropic effects of cystic fibrosis (CF) result from the mislocalization or inactivity of an apical membrane chloride channel, the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR may also modulate intracellular chloride conductances and thus affect organelle pH. To test the role of CFTR in organelle pH regulation, we developed a model system to selectively perturb the pH of a subset of acidified compartments in polarized cells and determined the effects on various protein trafficking steps. We then tested whether these effects were observed in cells lacking wild-type CFTR and whether reintroduction of CFTR affected trafficking in these cells. Our model system involves adenovirus-mediated expression of the influenza virus M2 protein, an acid-activated ion channel. M2 expression selectively slows traffic through the trans-Golgi network (TGN) and apical endocytic compartments in polarized Madin-Darby canine kidney (MDCK) cells. Expression of M2 or treatment with other pH perturbants also slowed protein traffic in the CF cell line CFPAC, suggesting that the TGN in this cell line is normally acidified. Expression of functional CFTR had no effect on traffic and failed to rescue the effect of M2. Our results argue against a role for CFTR in the regulation of organelle pH and protein trafficking in epithelial cells." @default.
• W1874417194 created "2016-06-24" @default.
• W1874417194 creator A5026814916 @default.
• W1874417194 creator A5062551240 @default.
• W1874417194 creator A5087929660 @default.
• W1874417194 date "2000-10-01" @default.
• W1874417194 modified "2023-10-14" @default.
• W1874417194 title "Evidence against the acidification hypothesis in cystic fibrosis" @default.
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• W1874417194 doi "https://doi.org/10.1152/ajpcell.2000.279.4.c1088" @default.
• W1874417194 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11003589" @default.
• W1874417194 hasPublicationYear "2000" @default.
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