Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) is a phosphorylation-regulated Cl- channel. In most mammalian cells, the functional consequences of the most common CF mutation, delta F508-CFTR, cannot be assessed as the mutant protein undergoes biosynthetic arrest. However, function can be studied in the baculovirus-insect cell expression system where delta F508-CFTR does not appear to undergo such arrest. Our results show that phosphorylation-regulated Cl- channel activity of delta F508-CFTR is similar to that of wild-type CFTR. This observation was confirmed in comparative studies of purified delta F508-CFTR and CFTR reconstituted in planar lipid bilayers. Therefore, we suggest that this common mutation does not result in a significant alteration in CFTR function.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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CHO Cells
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Cell Line
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Chloride Channels / chemistry
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Chloride Channels / genetics*
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Chloride Channels / metabolism
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Cricetinae
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Cyclic AMP / pharmacology
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Cystic Fibrosis / genetics*
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Cystic Fibrosis Transmembrane Conductance Regulator
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Humans
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Kinetics
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Lipid Bilayers
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Membrane Potentials / drug effects
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Membrane Potentials / physiology
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Membrane Proteins / chemistry
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Membrane Proteins / genetics*
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Phenylalanine*
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Phosphorylation
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Protein Folding
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Deletion*
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Spodoptera
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Transfection
Substances
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CFTR protein, human
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Chloride Channels
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Lipid Bilayers
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Membrane Proteins
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Recombinant Proteins
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Cystic Fibrosis Transmembrane Conductance Regulator
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Phenylalanine
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Cyclic AMP