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Vol. 9, Issue 12, 3417-3427, December 1998
and
Institutes of
*Physiology and
The small G protein K-Ras2A is rapidly induced by aldosterone in A6
epithelia. In these Xenopus sodium reabsorbing cells, aldosterone rapidly activates preexisting epithelial Na+
channels (XENaC) via a transcriptionally mediated
mechanism. In the Xenopus oocytes expression system, we
tested whether the K-Ras2A pathway impacts on XENaC
activity by expressing XENaC alone or together with
XK-Ras2A rendered constitutively active (XK-Ras2AG12V). As a second control,
XENaC-expressing oocytes were treated with progesterone,
a sex steroid that induces maturation of the oocytes similarly to
activated Ras. Progesterone or XK-Ras2AG12V
led to oocyte maturation characterized by a decrease in surface area
and endogenous Na+ pump function. In both conditions, the
surface expression of exogenous XENaC's was also
decreased; however, in comparison with progesterone-treated oocytes,
XK-ras2AG12V-coinjected
oocytes expressed a fivefold higher XENaC-mediated macroscopic Na+ current that was as high as that of control
oocytes. Thus, the Na+ current per surface-expressed
XENaC was increased by
XK-Ras2AG12V. The chemical driving force for
Na+ influx was not changed, suggesting that
XK-Ras2AG12V increased the mean activity of
XENaCs at the oocyte surface. These observations raise
the possibility that XK-Ras2A, which is the first
regulatory protein known to be transcriptionally induced by
aldosterone, could play a role in the control of XENaC function in aldosterone target cells.
Anatomy, University of
Zurich, CH-8057 Zurich, Switzerland; and
Institute of
Pharmacology and Toxicology, University of Lausanne, CH-1005 Lausanne,
Switzerland
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