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Departments of
Biopharmaceutical Sciences (L.Z., M.J.D., S.T.,
K.M.G.) and
Anesthesia (A.T.G., S.C.Y.), University of California San
Francisco, San Francisco, California 94143
Polyspecific organic cation transporters in the liver mediate the
elimination of a wide array of endogenous amines and xenobiotics. In
contrast to our understanding of the mechanisms of organic cation
transport in rat liver, little is known about the mechanisms of organic
cation transport in the human liver. We report the cloning, sequencing,
and functional characterization of the first human polyspecific organic
cation transporter from liver (hOCT1). hOCT1 (554 amino acids) is 78%
identical to the previously cloned organic cation transporter from rat,
rOCT1 [Nature (Lond.) 372:549-552 (1994)]. In
Xenopus laevis oocytes injected with the cRNA of hOCT1, the specific uptake of the organic cation
3H-1-methyl-4-phenylpyridinium
(3H-MPP+) was significantly enhanced (8-fold)
over that in water-injected oocytes. Uptake of
3H-MPP+ was saturable
(Km = 14.6 ± 4.39 µM) and sensitive to membrane potential. Both small
monovalent organic cations such as tetraethylammonium and
N1-methylnicotinamide and bulkier organic
cations (e.g., vecuronium and decynium-22) inhibited the uptake of
3H-MPP+. In addition, the bile acid
taurocholate inhibited the uptake of 3H-MPP+ in
oocytes expressing hOCT1. Northern analysis demonstrated that the mRNA
transcript of hOCT1 is expressed primarily in the human liver, whereas
the mRNA transcript of rOCT1 is found in rat kidney, liver, intestine,
and colon [Nature (Lond.) 372:549-552 (1994)].
In comparison to rOCT1, hOCT1 exhibits notable differences in its
kinetic characteristics and tissue distribution. The functional expression of hOCT1 will provide a powerful tool for elucidation of the
mechanisms of organic cation transport in the human liver and
understanding of the mechanisms involved in the disposition and
hepatotoxicity of drugs.
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