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Am J Physiol Renal Physiol (June 15, 2004). doi:10.1152/ajprenal.00078.2004
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Submitted on March 10, 2004
Accepted on June 8, 2004

Modulation of epithelial Na+ channel activity by long chain n-3 fatty acids

Frederique Mies1, Vadim Shlyonsky1, Arnaud Goolaerts1, and Sarah Sariban-Sohraby1*

1 From the Physiology Department, Universite Libre de Bruxelles, Brussels, Brabant, Belgium

* To whom correspondence should be addressed. E-mail: sohraby{at}ulb.ac.be.

The epithelial sodium channel is found in apical membranes of a variety of native epithelial tissues where it regulates sodium and fluid balance. In vivo, a number of hormones and other endogenous factors including polyunsaturated fatty acids (PUFAs) regulate these channels. We tested the effects of essential n-3 and n-6 PUFAs on amiloride-sensitive sodium transport in A6 epithelial cells. Eicosapentaenoic acid (EPA, C20:5, n-3) transiently stimulated amiloride-sensitive open-circuit current (INa) from 4.0 ± 0.3 to 7.7 ± 0.3 µA/cm2 within 30 min (p<0.001). No activation was seen in the presence of 10 µM amiloride. In cellattached but not in cell-excised patches, EPA acutely increased open probability (NPo) of sodium channels from 0.45 ± 0.08 to 0.63 ± 0.10 (p=0.02, paired t-test). n-6 PUFAs, including linoleic acid (C18:2,), eicosatetraynoic acid (C20:4) and docosapentanoic acid (C22:5) had no effect, while n-3 docosahexanoic acid (C22:6,) activated amiloride-sensitive INa similar to EPA. Activation of INa by EPA was prevented by H89, a PKA inhibitor. Likewise, PKA activity was stimulated by EPA. Non specific stimulation of phosphodiesterase activity by CoCl2 completely prevented the effect of EPA on sodium transport. We conclude that n-3 PUFAs activate epithelial sodium channels downstream of cAMP in a cAMP dependent pathway also involving PKA.




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