Annexin A5 increases the cell surface expression and the chloride channel function of the DeltaF508-cystic fibrosis transmembrane regulator.

Cystic fibrosis (CF) is caused by a mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. In CF, the most common mutant DeltaF508-CFTR is misfolded, is retained in the ER and is rapidly degraded. If conditions could allow DeltaF508-CFTR to reach and to stabilize in the plasma membrane, it could partially correct the CF defect.

Coupling cystic fibrosis to endoplasmic reticulum stress: Differential role of Grp78 and ATF6.

Cystic fibrosis (CF) is the most common Caucasian autosomal recessive disease. It is due to mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene encoding the CFTR protein, which is a chloride (Cl(-)) channel. The most common mutation leads to a missing phenylalanine at position 508 (DeltaF508).

Annexin V is directly involved in cystic fibrosis transmembrane conductance regulator's chloride channel function.

The cystic fibrosis transmembrane conductance regulator (CFTR) functions as a cAMP-activated chloride channel, which is regulated by protein-protein interactions. The extent to which CFTR is regulated by these interactions remains unknown. Annexin V is overexpressed in cystic fibrosis (CF), and given the functional properties of annexin V and CFTR we considered whether they are associated and if so whether this has implications for CFTR function.