CFTR as a cAMP-dependent regulator of sodium channels

Details

Serval ID
serval:BIB_0398072AC9E1
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
CFTR as a cAMP-dependent regulator of sodium channels
Journal
Science
Author(s)
Stutts  M. J., Canessa  C. M., Olsen  J. C., Hamrick  M., Cohn  J. A., Rossier  B. C., Boucher  R. C.
ISSN
0036-8075
Publication state
Published
Issued date
08/1995
Peer-reviewed
Oui
Volume
269
Number
5225
Pages
847-50
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Aug 11
Abstract
Cystic fibrosis transmembrane regulator (CFTR), the gene product that is mutated in cystic fibrosis (CF) patients, has a well-recognized function as a cyclic adenosine 3',5'-monophosphate (cAMP)-regulated chloride channel, but this property does not account for the abnormally high basal rate and cAMP sensitivity of sodium ion absorption in CF airway epithelia. Expression of complementary DNAs for rat epithelial Na+ channel (rENaC) alone in Madin Darby canine kidney (MDCK) epithelial cells generated large amiloride-sensitive sodium currents that were stimulated by cAMP, whereas coexpression of human CFTR with rENaC generated smaller basal sodium currents that were inhibited by cAMP. Parallel studies that measured regulation of sodium permeability in fibroblasts showed similar results. In CF airway epithelia, the absence of this second function of CFTR as a cAMP-dependent regulator likely accounts for abnormal sodium transport.
Keywords
3T3 Cells Absorption Amiloride/pharmacology Animals Cell Line Cell Membrane Permeability Chloride Channels/metabolism Cyclic AMP/*metabolism Cystic Fibrosis/*metabolism Cystic Fibrosis Transmembrane Conductance Regulator DNA, Complementary Dogs Humans Membrane Proteins/*metabolism Mice Patch-Clamp Techniques Rats Sodium/metabolism Sodium Channels/*metabolism Transfection
Pubmed
Web of science
Create date
24/01/2008 13:01
Last modification date
20/08/2019 12:25
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