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M513231200v1
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Papers In Press, published online ahead of print January 17, 2006
J. Biol. Chem, 10.1074/jbc.M513231200
Submitted on December 12, 2005
Revised on January 13, 2006
Accepted on January 17, 2006

Mechanisms of CFTR activation by S-nitrosoglutathione

Lan Chen, Rakesh P. Patel, Xinjun Teng, Charles A. Bosworth, Jack R. Lancaster Jr, and Sadis Matalon

Dept. of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL 35294-2172

Corresponding Author: sadis{at}uab.edu

We investigated the mechanisms by which S-nitrosoglutathione (GSNO) alters CFTR mediated chloride (Cl-) secretion across Calu-3 cells, an extensively used model of human airway gland serous cells. Confluent monolayers of Calu-3 cells, grown under an air-liquid interface, were mounted in Ussing chambers for the measurements of chloride short circuit current (Isc) and trans-epithelial resistance (Rt). Addition of GSNO into the apical compartment of these chambers resulted in significant and sustained increase of Isc with a IC50 3.2 ± 1 mu M (mean ± 1 SEM; n=6). Addition of either glibenclamide or pre-treatment of Calu-3 cells with the soluble guanylate cyclase inhibitor ODQ totally prevented the GSNO-induced increase of Isc. Conversely, BAY 41-2272, a sGC stimulator, increased Isc in a dose-response fashion. The GSNO increase of Isc was reversed by addition of two phosphatases (PPA1 and PPA2) into the apical compartment of Ussing chambers containing Calu-3 monolayers. Oxy-myoglobin (oxy-Mb, 300 mu M) added into the apical compartment of Ussing chambers either prior or after GSNO either completely prevented or immediately reversed the increase of Isc. However, smaller concentrations of oxy-Mb (1-10 mu M), sufficient to scavenge NO in the medium (as assessed by direct measurement of NO in the Ussing chamber using an ISO-NO meter) decreased Isc partially. Addition of cysteine (50 mu M) following GSNO resulted in an additional increase of Isc which was not reversed by oxy-Mb. These findings indicate that GSNO stimulates Cl- secretion via both cGMP dependent and cGMP-independent mechanisms.


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