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(Received for publication, July 30, 1996, and in revised form, October 2, 1996)
From the Institut für Physiologie der
Eberhard-Karls-Universität, 72076 Tübingen, Germany and the
§ Anatomisches Institut der Bayerischen
Julius-Maximilians-Universität,
97070 Würzburg, Germany
The previously cloned rat cation transporter
rOCT1 detected in renal proximal tubules and hepatocytes
(Gründemann, D., Gorboulev, V., Gambaryan, S., Veyhl, M., and
Koepsell, H. (1994) Nature 372, 549-552) was expressed in
Xenopus oocytes, and transport properties were analyzed
using tracer uptake studies and electrophysiological measurements.
rOCT1 induced highly active transport of a variety of
cations, including the classical substrates for cation transport, such
as N-1-methylnicotinamide,
1-methyl-4-phenylpyridinium (MPP), and tetraethylammonium (TEA), but
also the physiologically important choline. In oocytes rOCT1
also mediated efflux of MPP, which could be trans-stimulated by MPP and
TEA. Cation transport via rOCT1 was electrogenic. In
voltage-clamped oocytes, transport of TEA and choline via
rOCT1 produced inwardly directed currents, which were
independent of extracellular ion composition or pH. The choline- and
TEA-induced currents were voltage-dependent at
nonsaturating concentrations, and the apparent affinity of these
cations was decreased at depolarized voltages. Other substrates
transported by rOCT1 were the polyamines spermine and
spermidine. Interestingly, the previously described potent inhibitors
of rOCT1, cyanine 863, quinine, and D-tubocurarine
were substrates themselves. The data indicate that rOCT1 is an
effective transport system that is responsible for electrogenic uptake
of a wide variety of organic cations into epithelial cells of renal
proximal tubules and hepatocytes.
Volume 271, Number 51,
Issue of December 20, 1996
pp. 32599-32604
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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