CFTR as a cAMP-dependent regulator of sodium channels.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Stutts, MJ; Canessa, CM; Olsen, JC; Hamrick, M; Cohn, JA; Rossier, BC; Boucher, RC

Published Date

  • August 1995

Published In

Volume / Issue

  • 269 / 5225

Start / End Page

  • 847 - 850

PubMed ID

  • 7543698

Pubmed Central ID

  • 7543698

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.7543698

Language

  • eng