| Literature DB >> 25661196 |
Réginald Philippe1, Fabrice Antigny2, Paul Buscaglia1, Caroline Norez3, Frédéric Becq3, Maud Frieden4, Olivier Mignen5.
Abstract
Cystic Fibrosis (CF) disease is caused by mutations in the CFTR gene (CF transmembrane conductance regulator). F508 deletion is the most represented mutation, and F508del-CFTR is absent of plasma membrane and accumulates into the endoplasmic reticulum (ER) compartment. Using specific Ca2+ genetics cameleon probes, we showed in the human bronchial CF epithelial cell line CFBE that ER Ca2+ concentration was strongly increased compared to non-CF (16HBE) cells, and normalized by the F508del-CFTR corrector agent, VX-809. We also showed that ER F508del-CFTR retention increases SERCA (Sarcoplasmic/Reticulum Ca2+ ATPase) pump activity whereas PMCA (Plasma Membrane Ca2+ ATPase) activities were reduced in these CF cells compared to corrected CF cells (VX-809) and non-CF cells. We are showing for the first time CFTR/SERCA and CFTR/PMCA interactions that are modulated in CF cells and could explain part of Ca2+ homeostasis deregulation due to mislocalization of F508del-CFTR. Using ER or mitochondria genetics Ca2+ probes, we are showing that ER Ca2+ content, mitochondrial Ca2+ uptake, SERCA and PMCA pump, activities are strongly affected by the localization of F508del-CFTR protein.Entities:
Keywords: Calcium signaling; Cystic fibrosis; F508del-CFTR; PMCA; SERCA
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Year: 2015 PMID: 25661196 DOI: 10.1016/j.bbamcr.2015.01.010
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002