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PMID: 9632645 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta.

The Journal of biological chemistry ·Vol. 273 ·No. 26 ·1998-06-26 ·Pages 15971-9

Kekuda R, Prasad PD, Wu X, Wang H, Fei YJ, Leibach FH, Ganapathy V

Abstract

We have isolated a cDNA from rat placenta which, when expressed heterologously, mediates the transport of a wide spectrum of organic cations. The cDNA codes for a protein of 551 amino acids containing 12 putative transmembrane domains. Northern blot analysis indicates that this transporter is expressed most abundantly in the placenta and moderately in the intestine, heart, and brain. The expression is comparatively low in the kidney and lung and is undetectable in the liver. This transporter is distinct from the previously cloned organic cation transporters (OCT1, OCT2, NKT, NLT, RST, and OCTN1). When expressed in HeLa cells, the cDNA induces the transport of tetraethylammonium and guanidine. Competition experiments indicate that this transport process recognizes a large number of organic cations, including the neurotoxin 1-methyl-4-phenylpyridinium, as substrates. The cDNA-induced transport is markedly influenced by extracellular pH. However, when expressed in Xenopus laevis oocytes, the cDNA-induced transport is electrogenic, associated with the transfer of positive charge into the oocytes. Under voltage clamp conditions, tetraethylammonium evokes inward currents that are concentration- and potential-dependent. This potential-sensitive organic cation transporter, designated as OCT3, represents a new member of the OCT gene family.

MeSH Terms
Amino Acid Sequence Animals Cloning, Molecular DNA-Binding Proteins/chemistry,genetics HeLa Cells Humans Hydrogen-Ion Concentration Molecular Sequence Data Octamer Transcription Factor-3 Oocytes/metabolism Placenta/metabolism Protein Conformation Rats Transcription Factors/chemistry,genetics Xenopus laevis
Chemicals
DNA-Binding Proteins Octamer Transcription Factor-3 POU5F1 protein, human Transcription Factors
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Kekuda R
Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, Georgia 30912, USA.
Prasad P D
Wu X
Wang H
Fei Y J
Leibach F H
Ganapathy V
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1998-06-26
Pages
15971-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NICHD NIH HHS · HD 10045 · United States
Databases
GENBANK
AF055286
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