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J Biol Chem, Vol. 274, Issue 38, 26912-26916, September 17, 1999
From the Department of Physiology, Emory University School of
Medicine, Center for Cellular and Molecular Signaling, Atlanta, Georgia
30322, § Department of Medicine, University of Pittsburgh,
Laboratory of Epithelial Cell Biology, Pittsburgh, Pennsylvania, 15213 and ¶ Laboratoire de Physiologie et Physiopatologie, Universite'
Libre de Bruxelles, 1070 Bruxelles, Belgium
The Xenopus laevis distal tubule
epithelial cell line A6 was used as a model epithelia to study the role
of isoprenylcysteine-O-carboxyl methyltransferase
(pcMTase) in aldosterone-mediated stimulation of Na+
transport. Polyclonal antibodies raised against X. laevis
pcMTase were immunoreactive with a 33-kDa protein in whole cell lysate. These antibodies were also reactive with a 33-kDa product from in
vitro translation of the pcMTase cDNA. Aldosterone
application increased pcMTase activity resulting in elevation of total
protein methyl esterification in vivo, but pcMTase protein
levels were not affected by steroid, suggesting that aldosterone
increased activity independent of enzyme number. Inhibition of pcMTase
resulted in a reduction of aldosterone-induced Na+
transport demonstrating the necessity of pcMTase-mediated
transmethylation for steroid induced Na+ reabsorption.
Transfection with an eukaryotic expression construct containing pcMTase
cDNA increased pcMTase protein level and activity. This resulted in
potentiation of the natriferic actions of aldosterone. However,
overexpression did not change Na+ reabsorption in the
absence of steroid, suggesting that pcMTase activity is not limiting
Na+ transport in the absence of steroid, but that
subsequent to aldosterone addition, pcMTase activity becomes limiting.
These results suggest that a critical transmethylation is necessary for
aldosterone-induction of Na+ transport. It is likely that
the protein catalyzing this methylation is
isoprenylcysteine-O-carboxyl methyltransferase and
that aldosterone activates pcMTase without affecting transferase expression.
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