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Cloning and characterization of a novel human pH‐dependent organic cation transporter, OCTN1

Tamai, Ikumi, Yabuuchi, Hikaru, Nezu, Jun-ichi, Sai, Yoshimichi, Oku, Asuka, Shimane, Miyuki, Tsuji, Akira·1997·FEBS Letters

Abstract

cDNA for a novel proton/organic cation transporter, OCTN1, was cloned from human fetal liver and its transport activity was investigated. OCTN1 encodes a 551‐amino acid protein with 11 transmembrane domains and one nucleotide binding site motif. It is strongly expressed in kidney, trachea, bone marrow and fetal liver and in several human cancer cell lines, but not in adult liver. When expressed in HEK293 cells, OCTN1 exhibited saturable and pH‐dependent [3 H]tetraethyl ammonium uptake with higher activity at neutral and alkaline pH than at acidic pH. Furthermore, treatment with metabolic inhibitors reduced the uptake, which is consistent with the presence of the nucleotide binding site sequence motif. Although its subcellular localization and detailed functional characteristics are not clear at present, OCTN1 appears to be a novel proton antiporter that functions for active secretion of cationic compounds across the renal epithelial brush‐border membrane. It may play a role in the renal excretion of xenobiotics and their metabolites.

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Metadata

Authors
Tamai, I., Yabuuchi, H., Nezu, J.-I., Sai, Y., Oku, A., Shimane, M., & Tsuji, A.
Venue
FEBS Letters
Publisher
Wiley
Published
1997-12-08
Volume
419
Issue
1
Pages
107-111
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1977244805
Cited by
458
References
0
FWCI
7.88
Type
journal article
Language
en
Open access
closed

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