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Papers In Press, published online ahead of print March 5, 2003
J. Biol. Chem, 10.1074/jbc.M212227200
Submitted on December 2, 2002
Revised on February 28, 2003
Accepted on March 5, 2003

Stimulation of beta 2 adrenergic receptor increases CFTR expression in human airway epithelial cells through a c-AMP/protein kinase A-independent pathway

Karima Taouil, Jocelyne Hinnrasky, Coralie Hologne, Pascal Corlieu, Jean-Michel Klossek, and Edith Puchelle

UMRS INSERM 514, Reims 51092

Corresponding Author: epuche{at}worldnet.fr

PSD-95/Dlg-A/ZO-1 (PDZ) domains play an essential role in determining cell polarity. The Na+/H+ exchanger regulatory factor (NHERF), also known as EBP50 contains two PDZ domains that mediate the assembly of transmembrane and cytosolic proteins into functional signal transduction complexes. Moreover, it has been shown that cystic fibrosis transmembrane conductance regulator (CFTR) and beta 2 adrenergic receptor (beta 2AR) bind equally well to the PDZ1 domain of EBP50. We hypothesized that beta 2AR activation may regulate CFTR protein expression. To verify this hypothesis, we evaluated the effects of a pharmacologically relevant concentration of salmeterol (2.10-7M), a long acting beta 2AR agonist, on CFTR expression in primary human airway epithelial cells (HAEC). beta 2AR stimulation induced a time-dependent increase in apical CFTR protein expression, with a maximal response reached after treatment for 24 hours. This effect was post-transcriptional, dependent upon beta 2AR agonist binding to the beta 2AR and independent of the known beta 2AR agonist-mediated c-AMP/PKA pathway. We demonstrated, by immunohistochemistry, that CFTR, beta 2and EBP50 localize to the apical membrane of HAEC. Analyses of anti-EBP50 proteins immunoprecipitate showed that salmeterol induced an increase in the amount of CFTR that binds to EBP50. These data suggests that beta 2AR activation regulates CFTR association with EBP50 in polarized HAEC.


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