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In 1995 research conducted by the team of scientists comprising of M. Jackson Stutts, Cecilia M. Canessa, John C. Olsen, Maura Hamrick, Jonathan A. Cohn, Bernard C. Rossier and Richard C. Boucher illucidated a key relationship between CFTR protein and the functionality of sodium pumps within an epithelial membrane. Their work was published in the August 11, 1995 edition of Science, vol. 269, pages 847-850 and contains the following 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 epithelia 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."
