CFTR as a cAMP-dependent regulator of sodium channels
Détails
ID Serval
serval:BIB_0398072AC9E1
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
CFTR as a cAMP-dependent regulator of sodium channels
Périodique
Science
ISSN
0036-8075
Statut éditorial
Publié
Date de publication
08/1995
Peer-reviewed
Oui
Volume
269
Numéro
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
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Aug 11
Résumé
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.
Mots-clé
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
Création de la notice
24/01/2008 14:01
Dernière modification de la notice
20/08/2019 13:25