Article
Processing and function of CFTR-DeltaF508 are species-dependent.
Proceedings of the National Academy of Sciences of the United States of America - 25 Sept 2007
Ostedgaard Lynda S, Rogers Christopher S, Dong Qian, Randak Christoph O, Vermeer Daniel W, Rokhlina Tatiana, Karp Philip H, Welsh Michael J
Abstract excerpt
Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) cause cystic fibrosis. The most common mutation, a deletion of the phenylalanine at position 508 (DeltaF508), disrupts processing of the protein. Nearly all human CFTR-DeltaF508 is retained in the endoplasmic reticulum and degraded, preventing maturation to the plasma membrane. In addition, the F508 deletion reduces the activity of single...
Topics
- Animals
- Biological Transport
- COS Cells
- Chlorine
- Chlorocebus aethiops
- Cystic Fibrosis
- Cystic Fibrosis Transmembrane Conductance Regulator
- Electrophysiology
- Endoplasmic Reticulum
- Humans
- Mice
- Mutation
- Phenylalanine