Corpus ID: 22281058

Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations.

@article{Yabuuchi1999NovelMT,
  title={Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations.},
  author={H. Yabuuchi and I. Tamai and J. Nezu and K. Sakamoto and A. Oku and M. Shimane and Y. Sai and A. Tsuji},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1999},
  volume={289 2},
  pages={
          768-73
        }
}
In the present study, functional characteristics of organic cation transporter (OCTN)1, which was cloned as the pH-dependent tetraethylammonium (TEA) transporter when expressed in mammalian human embryonic kidney (HEK)293 cells, were further investigated using Xenopus oocytes as well as HEK293 cells as gene expression systems. When OCTN1-derived complementary RNA was injected into Xenopus oocytes, pH-dependent transport of [14C]TEA was observed as the same in HEK293 cells. In contrast, a… Expand
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Na(+)-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney.
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References

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Cloning and characterization of a novel human pH‐dependent organic cation transporter, OCTN1
TLDR
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 and may play a role in the renal excretion of xenobiotics and their metabolites. Expand
Cloning and characterization of two human polyspecific organic cation transporters.
TLDR
Cl cloning and characterization of two homologous transporters from man (hOCT1 and hOCT2) displaying approximately 80% amino acid identity to rOCT 1 and rO CT2 are reported, respectively. Expand
Molecular and Functional Identification of Sodium Ion-dependent, High Affinity Human Carnitine Transporter OCTN2*
TLDR
OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans, and the functional characteristics of OCTN2 coincide with those reported for plasma membrane carnitine transport. Expand
Cloning and Functional Characterization of a Potential-sensitive, Polyspecific Organic Cation Transporter (OCT3) Most Abundantly Expressed in Placenta*
TLDR
A cDNA isolated from rat placenta which, when expressed heterologously, mediates the transport of a wide spectrum of organic cations, represents a new member of the OCT gene family. Expand
Primary Structure and Functional Expression of the Apical Organic Cation Transporter from Kidney Epithelial LLC-PK1Cells*
TLDR
Reverse transcriptase-polymerase chain reaction indicates that mRNA of OCT1r is limited to non-neuronal tissue, whereas OCT2r, the OCT2p homologue from rat, was found in both the kidney and central nervous regions known to be rich in the monoamine transmitter dopamine. Expand
cDNA cloning and functional expression of a novel rat kidney organic cation transporter, OCT2.
TLDR
Findings suggest that OCT2 is responsible for the transport of cationic drugs in the kidney, and that this transcript was not detected in the brain, heart, lung, liver, small intestine or spleen. Expand
Cloning and functional expression of a human liver organic cation transporter.
TLDR
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 mechanism involved in the disposition and hepatotoxicity of drugs. Expand
Drug excretion mediated by a new prototype of polyspecific transporter
TLDR
The isolation of a complementary DNA from rat kidney is reported that encodes a 556-amino-acid membrane protein, OCT1, which has the functional characteristics of organic cation uptake over the basolateral membrane of renal proximal tubules and of organiccation uptake into hepatocytes. Expand
cDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family.
TLDR
Cloned OCTN2, a new member of the organic cation transporter family, from a human placental trophoblast cell line, mediates the transport of tetraethylammonium in a pH-dependent manner and is more closely related to OCTN1 than to OCT1, OCT2 and OCT3. Expand
Transport of tetraethylammonium by rabbit renal brush-border and basolateral membrane vesicles.
Brush-border and basolateral membrane vesicles (BBMV and BLMV, respectively) from rabbit renal cortex were used to study transport of the organic cation, tetraethylammonium (TEA). Outwardly directedExpand
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