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

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 [3H]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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Tamai I,Yabuuchi H,Nezu J,Sai Y,Oku A,Shimane M,Tsuji A

doi

10.1016/s0014-5793(97)01441-5

subject

Has Abstract

pub_date

1997-12-08 00:00:00

pages

107-11

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014579397014415

journal_volume

419

pub_type

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