|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1995-1-5
|
|
pubmed:abstractText |
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.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1061-4036
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
3
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
311-6
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:7526932-Amino Acid Sequence,
pubmed-meshheading:7526932-Animals,
pubmed-meshheading:7526932-Base Sequence,
pubmed-meshheading:7526932-CHO Cells,
pubmed-meshheading:7526932-Cell Line,
pubmed-meshheading:7526932-Chloride Channels,
pubmed-meshheading:7526932-Cricetinae,
pubmed-meshheading:7526932-Cyclic AMP,
pubmed-meshheading:7526932-Cystic Fibrosis,
pubmed-meshheading:7526932-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:7526932-Humans,
pubmed-meshheading:7526932-Kinetics,
pubmed-meshheading:7526932-Lipid Bilayers,
pubmed-meshheading:7526932-Membrane Potentials,
pubmed-meshheading:7526932-Membrane Proteins,
pubmed-meshheading:7526932-Molecular Sequence Data,
pubmed-meshheading:7526932-Phenylalanine,
pubmed-meshheading:7526932-Phosphorylation,
pubmed-meshheading:7526932-Protein Folding,
pubmed-meshheading:7526932-Recombinant Proteins,
pubmed-meshheading:7526932-Sequence Deletion,
pubmed-meshheading:7526932-Spodoptera,
pubmed-meshheading:7526932-Transfection
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR.
|
|
pubmed:affiliation |
Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
