Rattlesnake Phospholipase A(2) Increases CFTR-Chloride Channel Current and Corrects Delta F508CFTR Dysfunction: Impact in Cystic Fibrosis

摘要

Deletion of Phe508 in the nucleotide binding domain (Delta F508-NBD1) of the cystic fibrosis transmembrane regulator (CFTR; a cyclic AMP-regulated chloride channel) is the most frequent mutation associated with cystic fibrosis. This mutation affects the maturation and gating of CFTR protein. The search for new high-affinity ligands of CFTR acting as dual modulators (correctors/activators) presents a major challenge in the pharmacology of cystic fibrosis.