Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) was expressed in cultured cystic fibrosis airway epithelial cells and Cl- channel activation assessed in single cells using a fluorescence microscopic assay and the patch-clamp technique. Expression of CFTR, but not of a mutant form of CFTR (delta F508), corrected the Cl- channel defect. Correction of the phenotypic defect demonstrates a causal relationship between mutations in the CFTR gene and defective Cl- transport which is the hallmark of the disease.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Cell Membrane Permeability
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Cells, Cultured
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Chloride Channels
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Chlorides / metabolism
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Cyclic AMP / pharmacology
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Cystic Fibrosis / genetics
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Cystic Fibrosis / metabolism*
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Cystic Fibrosis Transmembrane Conductance Regulator
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Electric Conductivity
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Epithelium / drug effects
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Epithelium / metabolism
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Gene Expression*
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Humans
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Kinetics
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Membrane Proteins / genetics*
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Membrane Proteins / metabolism*
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Membrane Proteins / physiology
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Microscopy, Fluorescence
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Mutation
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Respiratory System / metabolism
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Transfection
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Vaccinia virus / genetics
Substances
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CFTR protein, human
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Chloride Channels
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Chlorides
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Membrane Proteins
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Cystic Fibrosis Transmembrane Conductance Regulator
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Cyclic AMP