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J. Biol. Chem., Vol. 277, Issue 14, 11965-11969, April 5, 2002
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From the Center for Cell and Molecular Signaling and Department of
Physiology, Emory University School of Medicine,
Atlanta, Georgia 30322
Phosphatidylinositol 4,5-bisphosphate
(PIP2) is a membrane lipid found in all eukaryotic
cells, which regulates many important cellular processes, including ion
channel activity. In this study, we used inside-out patch clamp
technique, immunoprecipitation, and Western blot analysis to
investigate the effect of PIP2 on epithelial sodium channel
activity in A6 cells. A6 cells were cultured in media supplemented with
1.5 µM aldosterone. Single sodium channel activity in
excised, inside-out patches was increased by perfusion of the bath
solution with 30 µM PIP2 plus 100 µM GTP (NPo = 1.34 ± 0.14)
compared with the paired control (NPo = 0.09 ± 0.02). However, neither 30 µM
PIP2 (NPo = 0.11 ± 0.02) nor
100 µM GTP (NPo = 0.10 ± 0.02) alone stimulated the sodium channels. The
PIP2-stimulated channel activity was abolished by application of 10 nM G protein
Phosphatidylinositol 4,5-Bisphosphate (PIP2)
Stimulates Epithelial Sodium Channel Activity in A6 Cells*
subunits
(NPo = 0.14 ± 0.05). However, 10 nM G
i-3 + 30 µM
PIP2 increased both NPo and
Po. The stimulating effect of 10 nM
Gi-3 + 30 µM PIP2 is similar
to that of 30 µM PIP2 plus 100 µM GTP. Immunoprecipitation and Western blot analysis
show that both Gi
-3 and PIP2 bind and
epithelial Na+ channels (ENaC), but not ENaC. These results indicate that PIP2 increases ENaC
activity by direct interaction with or xENaC in the presence of
Gi-3.
*
This work was supported by National Institutes of Health
Grant DK37963 (to D. C. E.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Center for Cell and
Molecular Signaling, Emory University School of Medicine, 1648 Pierce
Dr., Atlanta, GA 30322. Tel.: 404-727-7421; Fax: 404-727-0329; E-mail:
deaton@emory.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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