Cm. Fuller et Dj. Benos, Electrophysiological characteristics of the Ca2+-activated Cl- channel family of anion transport proteins, CLIN EXP PH, 27(11), 2000, pp. 906-910
Citations number
30
Categorie Soggetti
Pharmacology & Toxicology
Journal title
CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY
1. A protein isolated from the bovine tracheal epithelium behaves as a Ca2-activated Cl- channel (CaCC) when incorporated into planar lipid bilayers.
2. An antibody raised against this protein was used to screen a cDNA expres
sion library and resulted in the isolation of a cDNA clone that exhibited n
early identical electrophysiological characteristics to the isolated endoge
nous protein when expressed.
3. Recent cloning of several related proteins has revealed that the cloned
bovine CaCC is one of a large and growing family. All new family members so
far examined are associated with the appearance of a novel Ca2+-mediated C
l- conductance when heterologously expressed.
4. This new group of proteins may underlie the Ca2+-mediated Cl- conductanc
e upregulated in the cystic fibrosis (CF) knockout mouse and thought to be
responsible for the escape from the significant airway pathology associated
with CF.