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Volume 272, Number 51, Issue of December 19, 1997 pp. 31953-31956
(Received for publication, September 22, 1997, and in revised form, October 31, 1997)
§
,
,
,
,§
and
From the The substrate specificity of the previously
cloned rat cation transporter rOCT1, which is expressed in
kidney, liver, and small intestine, was reevaluated. rOCT1 is
the first member of a new protein family comprising electrogenic and
polyspecific cation transporters that transport hydrophilic cations
like tetraethylammonium, choline, and monoamine neurotransmitters.
Previous electrical measurements suggested that cations like quinine,
quinidine, and cyanine 863, which have been classified as type 2 cations in the liver, are also transported by rOCT1, since
they may induce inward currents in rOCT1 expressing
Xenopus oocytes (Busch, A. E., Quester, S., Ulzheimer,
J. C., Waldegger, S., Gorboulev, V., Arndt, P., Lang, F., and
Koepsell, H. (1996) J. Biol. Chem. 271, 32599-32604). Tracer flux measurements with oocytes and with stably transfected human
embryonic kidney cells showed that [3H]quinine
and [3H]quinidine are not transported by rOCT1.
The voltage dependence observed for the quinine- or quinidine-induced
inward currents in rOCT1-expressing oocytes, and tracer efflux
measurements indicate that the inward currents by type 2 cations are
generated by the inhibition of electrogenic efflux of transported type
1 cations. Therefore, rOCT1 cannot contribute to transport of
type 2 cations in the liver and the hepatic transporter for type 2 cations remains to be identified.
Max-Planck-Insitiut für Biophysik,
Anatomisches Institut der
Bayerischen Julius-Maximilians-Universität,
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