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J Biol Chem, Vol. 273, Issue 32, 20378-20382, August 7, 1998
From the Primary carnitine deficiency, because of a defect
of the tissue plasma membrane carnitine transporters, causes critical
symptoms. However, the transporter has not been molecularly identified. In this study, we screened a human kidney cDNA library and
assembled a cDNA-encoding OCTN2 as a homologue of the organic
cation transporter OCTN1, and then we examined the function of
OCTN2 as a carnitine transporter. OCTN2-cDNA encodes a polypeptide
of 557 amino acids with 75.8% similarity to OCTN1. Northern blot
analysis showed that OCTN2 is strongly expressed in kidney, skeletal
muscle, heart, and placenta in adult humans. When OCTN2 was expressed
in HEK293 cells, uptake of
L-[3H]carnitine was strongly enhanced
in a sodium-dependent manner with Km
value of 4.34 µM, whereas typical substrates for
previously known organic cation transporters, tetraethylammonium and
guanidine, were not good substitutes. OCTN2-mediated
L-[3H]carnitine transport was inhibited by
the D-isomer, acetyl-D,L-carnitine, and Carnitine (3-hydroxy-4-N-trimethylaminobutyric acid) is
a small, water soluble molecule that has important physiological roles, including involvement in the Although many membrane-physiological studies of carnitine transport
mechanisms have been reported (3, 5-7,12-16), it is essential for a
clearer understanding of the primary carnitine deficiency to identify
the relevant transporter and to functionally characterize the carnitine
transport in detail. We have recently cloned and characterized a novel
organic cation transporter OCTN1 from human fetal liver (17). OCTN1 was
expressed strongly in adult tissues such as kidney, trachea, and bone
marrow and weakly in other tissues. When expressed in HEK293 cells,
OCTN1 caused significant transport of tetraethylammonium
(TEA),1 a typical organic
cation, in a pH-dependent manner. These characteristics strongly suggested that OCTN1 acts as a proton/organic cation antiporter at the renal epithelial apical membrane (17, 18). In the
present study, we identified a new transporter molecule, OCTN2, with
high homology to OCTN1. We cloned full-length cDNA for this
putative member of the organic cation transporter family, expressed it
in HEK293 cells, and showed that OCTN2 has the characteristics of a
high affinity sodium/carnitine cotransporter.
Materials--
L-[Methyl-3H]carnitine
hydrochloride (85 Ci/mmol) and [14C]guanidine (56 mCi/mmol), [1-14C]-tetraethylammonium bromide (2.4 mCi/mmol), and [ Cloning of OCTN2 cDNA and Northern Blot Analysis--
A data
base search for matches to the cDNA sequence of the OCTN1 gene
revealed several genomic cosmid clones (GenBankTM accession
numbers L43407, L43408, L46907, L81773, and L43409), derived from human
chromosome 5q, that contain sequences highly homologous to OCTN1.
Because these genomic sequences do not cover the entire open reading
frame for this new gene, which we designated OCTN2 on the basis of its
high similarity to OCTN1, we initiated cDNA cloning. From the
genomic sequence, two primers (631RT S4 5'-GTGCTGTTGGGCTCCTTCATTTCA-3'
and 631RT A1 5'-AGCTGCATGAAGAGAAGGACACTG-3') were prepared and used in
reverse transcription-polymerase chain reaction of human kidney-derived cDNA. This afforded a 900-base pair 32 cDNA fragment of OCTN2. Screening of a human kidney cDNA library with this fragment as the
probe yielded overlapping, longer clones that provided additional sequences. A primer (631R S6 5'-AGCATCCTGTCTCCCTACTTCGTT-3') designed from the new sequence was used to amplify the 3' portion of OCTN2 by 3'
rapid amplification of cDNA ends using human kidney
Marathon-ReadyTM cDNA (CLONTECH).
Finally, the full coding sequence of OCTN2 was obtained by assembling
these sequences. To assess OCTN2 expression in human tissues, an OCTN2
cDNA fragment, amplified with the 631RT S4 and 631RT A1 primers,
was labeled with [ Transport Study in HEK293 Cells--
The full-length OCTN2
cDNA was subcloned into the BamHI sites of the
expression vector pcDNA3, and the construct, pcDNA3/OCTN2 was
used to transfect HEK293 cells by means of the calcium phosphate precipitation method as described previously (17). The cells were
cultivated in Dulbecco's modified Eagle's medium containing 10%
fetal calf serum (Life Technologies, Inc., Tokyo, Japan), 100 units/ml
penicillin, and 100 µg/ml streptomycin in tissue culture dishes in a
humidified incubator at 37 °C under 5% CO2 for 24 h and then transfected with pcDNA3 plasmid carrying full-length OCTN2 cDNA or with the pcDNA3 plasmid vector alone. At 48 h after transfection, the cells were harvested by scraping with a
rubber policemen and suspended in the medium for transport study, which consisted of 125 mM NaCl, 4.8 mM KCl, 5.6 mM D-glucose, 1.2 mM CaCl2, 1.2 mM KH2PO4,
1.2 mM MgSO4, and 25 mM HEPES (pH
7.4). The cell suspension and transport medium containing a
radiolabeled test compound were preincubated separately for 20 min and
then mixed to initiate uptake. At appropriate times, 200-µl aliquots of the mixture were withdrawn, and the cells were separated from the
transport medium by centrifugation in a microtube containing a silicon
oil and liquid paraffin mixture with a density of 1.03. The resultant
cell pellets were solubilized in 3 N KOH and then neutralized with HCl, and the associated radioactivity was quantitated in a liquid scintillation counter (Aloka, Tokyo, Japan). Cellular protein content was determined according to the method of Bradford (19)
using a Bio-Rad protein assay kit. When sodium ions were replaced with
other cations, the obtained cells were suspended in sodium-free medium.
The composition of sodium-free medium was the same as that of the above
transport medium except that the sodium chloride was replaced
isotonically with potassium chloride, choline chloride,
N-methylglucamine chloride, or lithium chloride.
Molecular and Functional Identification of Sodium
Ion-dependent, High Affinity Human Carnitine Transporter
OCTN2*
,,,, and¶
Faculty of Pharmaceutical Sciences, Kanazawa
University, 13-1 Takara-machi, Kanazawa 920-0934, Japan and the
§ Chugai Research Institute for Molecular Medicine Inc.,
Ibaraki 300-4101, Japan
ABSTRACT
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Abstract
Introduction
Procedures
Results
Discussion
References
-butyrobetaine with high affinity and by glycinebetaine with lower affinity, whereas choline, 
-hydroxybutyric acid,
-aminobutyric acid, lysine, and taurine were not inhibitory. Because
the observed tissue distribution of OCTN2 is consistent with the
reported distribution of carnitine transport activity and the
functional characteristics of OCTN2 coincide with those reported for
plasma membrane carnitine transport, we conclude that OCTN2 is a
physiologically important, high affinity sodium-carnitine cotransporter
in humans.
INTRODUCTION
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Results
Discussion
References
-oxidation of fatty acids by
facilitating the transport of long chain fatty acids across the
mitochondrial inner membrane as their acylcarnitine esters and
modulation of intracellular CoA homeostasis (1, 2). Carnitine
deficiency causes severe pathological symptoms such as cardiomyopathy
and muscle weakness (3-6). Primary carnitine deficiency is thought to
be because of a defect of active transport of carnitine across plasma
membranes, whereas secondary carnitine deficiency seems to be
associated with an enzymatic defect, resulting in impaired oxidation of
acyl-CoA intermediates in the mitochondria (1-3). Reduced carnitine
concentration in tissue and plasma may be caused by insufficient
carnitine uptake activity from plasma and impaired reabsorption in the
kidney, respectively (3, 5-8). Symptoms related to defective carnitine
transport have been studied in a carnitine-deficient mutant animal
model, juvenile visceral steatosis mouse, which shows several symptoms
of primary and/or secondary carnitine deficiency and lacks in high
affinity transport activity in several tissues (7, 9-12).
EXPERIMENTAL PROCEDURES
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Discussion
References
-32P]dCTP were purchased from Amersham
Pharmacia Biotech (Rockinghamshire, UK), Moravek Biochemicals Inc.
(Brea, CA), and New England Nuclear (Boston, MA), respectively.
pcDNA3 was obtained from Invitrogen (San Diego, CA). Multiple
tissue Northern blots were purchased from CLONTECH.
All other enzymes and reagents were obtained from Takara (Otsu, Japan),
Toyobo (Osaka, Japan), Wako Pure Chemical Industries (Osaka, Japan),
and Sigma Chemical Co. (St. Louis, MO). HEK293 cells were obtained from
Japanese Cancer Research Resources Bank (Tokyo, Japan).
-32P]dCTP and subjected to Northern
blotting with poly(A)+ RNA from a wide range of normal
human tissues and cancer cell lines (CLONTECH).
Hybridization was carried out in ExpressHyb hybridization solution
(CLONTECH) at 68 °C for 1 h. Membranes were
then washed in 2× SSC containing 0.1% SDS at room temperature for 60 min and finally in 0.1× SSC, 0.1% SDS at 50 °C for 20 min twice.
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Amino Acid Sequence and Tissue Distribution of Human OCTN2-- The full-length OCTN2 cDNA appeared to encode a polypeptide of 557 amino acids and have 75.8% similarity with human OCTN1 (17) (Fig. 1A). Human OCTN2 is predicted to have twelve putative membrane-spanning domains by hydropathy analysis according to TopPred 2 (20) as well as three N-glycosylation sites and six protein kinase C phosphorylation sites. The presence of twelve membrane spanning domains agrees with that of previously known membrane transporters (21). Like human OCTN1, OCTN2 has a unique sugar transport protein signature (17). Comparison of the amino acid sequence with those of other organic ion transporters revealed that human OCTN2 has similarity with rat OCT1 (32.5%) (22), rat OCT2 (33.6%) (23), human OCT1 (33.1%) (24), human OCT2 (33.1%) (25), and rat OAT1 (28.4%) (26). No significant similarity was observed with human oatp (27) or monoamine neurotransmitter transporters such as serotonin transporter (28) or monoamine transporter (29). These data indicate that OCTN2 may be a member of the organic cation transporter family.
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Functional Analysis of OCTN2 Expressed in HEK293 Cells-- Because human OCTN1 transported the organic cation TEA in a pH-dependent manner when expressed in HEK293 cells in our previous study (17), we expressed human OCTN2 in the same cells and measured the uptake of cationic compounds for comparison with that of OCTN1. Although TEA is a good substrate of OCTN1 (17), no significant increase of [14C]TEA uptake was observed in human OCTN2-transfected cells (298 ± 60 pmol/mg protein/3 min in OCTN2-transfected HEK293 cells and 263 ± 12 in nontransfected cells at the TEA concentration of 60 µM and at 3 min). Because guanidine was suggested to be transported by a different transporter than that for TEA across the apical membrane of renal tubular epithelial cells (30), we examined the uptake of [14C]guanidine in human OCTN1- or OCTN2-expressing cells. However, neither OCTN1 (106 ± 5.6 pmol/mg protein/3 min at 10 µM guanidine) nor OCTN2 (95.1 ± 11.8 pmol/mg protein/3 min at 10 µM guanidine) exhibited increased guanidine transport activity compared with nontransfected cells (98.4 ± 5.9 pmol/mg protein/3 min at 10 µM guanidine). Zwitterionic carnitine is reabsorbed in the kidney via an active transport mechanism, although the molecular identity of the transporter remains to be established. Accordingly, we examined the transport of carnitine in the present study. Although OCTN1 showed slight but significant uptake of L-[3H]carnitine (2.5-fold increased uptake compared with nontransfected cells), a very large uptake of L-[3H]carnitine was seen with the human OCTN2-expressing HEK293 cells, as described below.
Fig. 3A shows the time course of the uptake of L-[3H]carnitine by HEK293 cells transfected with OCTN2 or with the expression vector pcDNA3 alone, in the presence or absence of sodium ions. Uptake of L-[3H]carnitine was significantly increased by OCTN2 transfection both in the presence and absence of sodium ions in the transport medium. The uptake of L-[3H]carnitine was particularly high in OCTN2-transfected cells in the presence of sodium ions, and it appears that OCTN2 is a sodium ion-dependent carnitine transporter. Because the cells transfected with expression vector alone showed a slight but significant increase of L-[3H]carnitine uptake in the presence of sodium ions compared with that in the absence of sodium ions, HEK293 cells themselves seem to have a weak activity of sodium ion-dependent carnitine transport. This is not surprising considering that HEK293 cells were originally derived from human embryonic kidney. Because sodium ion-dependent and OCTN2-mediated uptake of carnitine increased linearly up to 5 min, initial uptake rate of carnitine was determined at 3 min to characterize the transporter in all subsequent studies.
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-butyrobetaine reduced L-[3H]carnitine
uptake at 5 and 50 µM. Because L-carnitine
demonstrated more potent inhibition than the D-isomer at
low concentration (5 µM) OCTN2 seems to have
stereospecificity. Glycinebetaine less effectively reduced the uptake
of L-[3H]carnitine, and others examined,
including -aminobutyric acid, choline, -hydroxybutyrate, lysine,
and taurine, were not inhibitory. Accordingly, the structural
requirement of OCTN2-mediated carnitine transport is rather strict.
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Carnitine is normally maintained at a steady level in the blood, suggesting its physiological importance (1, 2). Although carnitine is biosynthesized in liver and brain (31), a significant amount of carnitine is also obtained from the diet via carrier-mediated transport across the intestinal epithelial cell membranes (32, 33) and is retained in the body through reabsorption in the kidney via active transport across the renal tubular epithelial cell membrane (1, 7, 14, 15). Furthermore, many studies have demonstrated that the tissues that extensively accumulate carnitine, such as skeletal muscle, heart, liver, and epididymis, take up and/or release carnitine via specialized transport mechanisms to maintain the steady-state tissue concentration (1). Although many of these membrane physiological studies suggested the participation of multiple sodium ion-dependent transporters with high and low affinities in carnitine movement across tissue plasma membranes (1, 13, 15), no such transporter has yet been identified at the molecular level. Accordingly, to achieve a better understanding of the biological and physiological roles of carnitine, as well as carnitine-related pathological states, it is essential to identify the carnitine transporter(s). We have previously cloned the human organic cation transporter OCTN1, which may participate at least partially in proton/organic cation antiport at the renal apical membranes, and characterized it by measuring the uptake of the typical organic cation TEA by OCTN1-transfected HEK293 cells (17). In the present study, we succeeded in obtaining cDNA of a second member of the human OCTN family, OCTN2, which has a high similarity to OCTN1, and found that OCTN2 has many of the characteristics of a high affinity, sodium ion-dependent carnitine transporter.
The idea that human OCTN2 is a sodium ion-dependent carnitine transporter is supported by the specific tissue distribution and the result of functional expression in HEK293 cells. Most adult tissues that highly express OCTN2, including skeletal muscle, kidney, placenta, and heart, have been reported to take up carnitine via a sodium ion-dependent, carrier-mediated transport mechanism (1, 15, 16, 34-36). As regards fetal tissues, we previously found that mouse embryo fibroblasts take up carnitine in a sodium ion-dependent manner with a half-saturation concentration of 5.5 µM, although the distribution of carnitine transport activity in fetal tissues was not established (13). Tissues that have apparently low affinity carnitine transporters, such as liver, brain, and intestine, with apparent half-saturation concentrations between 0.2 mM and 10 mM (1, 33, 37, 38), showed low expression of OCTN2. The distribution of OCTN2 is different from that of OCTN1, which has 75.8% sequence similarity with OCTN2 and coincides well with the functional distribution of sodium ion-dependent, high affinity carnitine transport activity as discussed above. Furthermore, OCTN2 hardly transported TEA, a good substrate of OCTN1, or guanidine, a substrate of the second renal organic cation transporter, which is distinct from that for TEA (30), OCTN2 seems likely to have some physiological role other than the renal excretion of organic cations.
When OCTN2 was expressed in HEK293 cells, a high uptake of L-[3H]carnitine was observed in the presence of sodium ions (Fig. 3, A and B). Because the cellular volume of HEK293 cells obtained from the accumulation of 3H2O is 6.3 µl/mg protein (17), L-[3H]carnitine apparently accumulated to the extent of about 320-fold at the steady-state in the cells by utilizing an inside-directed sodium ion gradient as the driving force. Lithium ions partially retained uphill transport (Fig. 3B) in a manner comparable with the carnitine transport obtained using rat renal brush border membrane vesicles (15) and human placental choriocarcinoma cells (16), which suggests that lithium ions are partially accepted as the cation for cotransport with carnitine. When sodium was replaced with choline, carnitine uptake was specifically eliminated (Fig. 3B). Although 500 µM choline was not inhibitory (Fig. 4B), choline may have a low affinity to compete with carnitine binding to OCTN2.
The half-saturation concentration of L-carnitine uptake by
OCTN2 was estimated to be 4.34 µM, which is very similar
to the values observed for high affinity carnitine transport in
membrane physiological studies in kidney, skeletal muscle, heart,
placenta, and cultured fibroblasts (1, 2, 5, 6, 15, 16, 34-36),
tissues that exhibited high expression of OCTN2 in Northern blot
analysis (Fig. 2). Carnitine transport in these tissues was reported to
be significantly inhibited by the D-isomer of carnitine, acetylcarnitine, and -butyrobetaine in a stereospecific manner (6,
15, 16, 35, 36). Furthermore, glycinebetaine and choline were low
affinity inhibitors and -aminobutyric acid was not inhibitory
(14-16, 36). These previously reported substrate specificity
characteristics exactly coincide with the properties of OCTN2. We
conclude that OCTN2 is a high affinity, sodium
ion-dependent carnitine transporter expressed in several
tissues, including kidney, skeletal muscle, heart, and placenta.
The amino acid sequence of human OCTN2 is very similar to that of human OCTN1, although OCTN1 exhibited only a low carnitine transport activity and had the functional characteristics of a proton/organic cation antiporter (17). Furthermore, TEA, a good substrate for OCTN1, was not transported well by OCTN2. Such significant differences of substrate specificity and driving force for transport despite the similarity in amino acid sequence may suggest that the binding or recognition specificity for substrates and cotransported ions on the transporter proteins is determined in a very limited region and that OCTN proteins have both common structures as membrane transporters and distinct small regions for the recognition of the substrate and cotransported ions. It will be interesting to identify the essential amino acid sequence of the functional binding sites by constructing chimeric proteins of OCTN1 and OCTN2. The strong expression of OCTN2 in human-derived tumor cells is similar to that of OCTN1 (14). This may reflect up-regulation of expression of the gene in malignancy to meet a higher requirement for L-carnitine.
In conclusion, human OCTN2 was cloned as a new member of the family of organic cation transporters. Studies of its tissue distribution and its functional expression in HEK293 cells indicated that OCTN2 is a physiologically important, high affinity carnitine transporter that shows significant sodium ion dependence. The identification of this carnitine transporter should contribute to a better understanding of the physiological and biochemical functions of carnitine, as well as to the development of measures to treat primary carnitine deficiency. In addition, isolation of the counterpart of OCTN2 in mice and comparison with juvenile visceral steatosis mice, which show abnormal carnitine metabolism and related diseases, may help to identify the principal causes of carnitine deficiency syndromes (7, 9-12).
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FOOTNOTES |
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* This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture, Japan and by CREST Core Research for Evolutional Science and Technology of the Japan Science and Technology Corporation (JST).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB015050.
¶ To whom correspondence should be addressed. Fax: 81-76-234-4477; E-mail: tsuji{at}kenroku.ipc.kanazawa-u.ac.jp.
The abbreviation used is: TEA, tetraethylammonium.
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  T. Kano, Y. Kato, K. Ito, T. Ogihara, Y. Kubo, and A. Tsuji Carnitine/Organic Cation Transporter OCTN2 (Slc22a5) Is Responsible for Renal Secretion of Cephaloridine in Mice Drug Metab. Dispos., May 1, 2009; 37(5): 1009 - 1016. [Abstract] [Full Text] [PDF]
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S. Grigat, C. Fork, M. Bach, S. Golz, A. Geerts, E. Schomig, and D. Grundemann The Carnitine Transporter SLC22A5 Is Not a General Drug Transporter, but It Efficiently Translocates Mildronate Drug Metab. Dispos., February 1, 2009; 37(2): 330 - 337. [Abstract] [Full Text] [PDF]
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 Q. Garrett, S. Xu, P. A. Simmons, J. Vehige, J. L. Flanagan, and M. D. Willcox Expression and Localization of Carnitine/Organic Cation Transporter OCTN1 and OCTN2 in Ocular Epithelium Invest. Ophthalmol. Vis. Sci., November 1, 2008; 49(11): 4844 - 4849. [Abstract] [Full Text] [PDF]
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 S. Hu, R. M. Franke, K. K. Filipski, C. Hu, S. J. Orwick, E. A. de Bruijn, H. Burger, S. D. Baker, and A. Sparreboom Interaction of Imatinib with Human Organic Ion Carriers Clin. Cancer Res., May 15, 2008; 14(10): 3141 - 3148. [Abstract] [Full Text] [PDF]
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 A. Koch, B. Konig, G. I. Stangl, and K. Eder PPAR{alpha} Mediates Transcriptional Upregulation of Novel Organic Cation Transporters-2 and -3 and Enzymes Involved in Hepatic Carnitine Synthesis Experimental Biology and Medicine, March 1, 2008; 233(3): 356 - 365. [Abstract] [Full Text] [PDF]
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 D. Kobayashi, I. Tamai, Y. Sai, K. Yoshida, T. Wakayama, Y. Kido, J.-i. Nezu, S. Iseki, and A. Tsuji Transport of carnitine and acetylcarnitine by carnitine/organic cation transporter (OCTN) 2 and OCTN3 into epididymal spermatozoa Reproduction, November 1, 2007; 134(5): 651 - 658. [Abstract] [Full Text] [PDF]
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 F. B. Stephens, D. Constantin-Teodosiu, and P. L. Greenhaff New insights concerning the role of carnitine in the regulation of fuel metabolism in skeletal muscle J. Physiol., June 1, 2007; 581(2): 431 - 444. [Abstract] [Full Text] [PDF]
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 D. B. Carlson, J. C. Woodworth, and J. K. Drackley Effect of L-Carnitine Infusion and Feed Restriction on Carnitine Status in Lactating Holstein Cows J Dairy Sci, May 1, 2007; 90(5): 2367 - 2376. [Abstract] [Full Text] [PDF]
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T. Maeda, M. Hirayama, D. Kobayashi, K. Miyazawa, and I. Tamai Mechanism of the Regulation of Organic Cation/Carnitine Transporter 1 (SLC22A4) by Rheumatoid Arthritis-Associated Transcriptional Factor RUNX1 and Inflammatory Cytokines Drug Metab. Dispos., March 1, 2007; 35(3): 394 - 401. [Abstract] [Full Text] [PDF]
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 F. B. Stephens, C. E. Evans, D. Constantin-Teodosiu, and P. L. Greenhaff Carbohydrate ingestion augments L-carnitine retention in humans J Appl Physiol, March 1, 2007; 102(3): 1065 - 1070. [Abstract] [Full Text] [PDF]
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 F. B. Stephens, D. Constantin-Teodosiu, D. Laithwaite, E. J. Simpson, and P. L. Greenhaff A threshold exists for the stimulatory effect of insulin on plasma L-carnitine clearance in humans Am J Physiol Endocrinol Metab, February 1, 2007; 292(2): E637 - E641. [Abstract] [Full Text] [PDF]
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 G. Horvath, N. Schmid, M. A. Fragoso, A. Schmid, G. E. Conner, M. Salathe, and A. Wanner Epithelial Organic Cation Transporters Ensure pH-Dependent Drug Absorption in the Airway Am. J. Respir. Cell Mol. Biol., January 1, 2007; 36(1): 53 - 60. [Abstract] [Full Text] [PDF]
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 G. D'Argenio, M. Calvani, A. Casamassimi, O. Petillo, S. Margarucci, M. Rienzo, I. Peluso, R. Calvani, A. Ciccodicola, N. Caporaso, et al. Experimental colitis: decreased Octn2 and Atb0+ expression in rat colonocytes induces carnitine depletion that is reversible by carnitine-loaded liposomes FASEB J, December 1, 2006; 20(14): 2544 - 2546. [Abstract] [Full Text] [PDF]
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C. Watanabe, Y. Kato, T. Sugiura, Y. Kubo, T. Wakayama, S. Iseki, and A. Tsuji PDZ Adaptor Protein PDZK2 Stimulates Transport Activity of Organic Cation/Carnitine Transporter OCTN2 by Modulating Cell Surface Expression Drug Metab. Dispos., November 1, 2006; 34(11): 1927 - 1934. [Abstract] [Full Text] [PDF]
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 T. J. Urban, R. C. Gallagher, C. Brown, R. A. Castro, L. L. Lagpacan, C. M. Brett, T. R. Taylor, E. J. Carlson, T. E. Ferrin, E. G. Burchard, et al. Functional Genetic Diversity in the High-Affinity Carnitine Transporter OCTN2 (SLC22A5) Mol. Pharmacol., November 1, 2006; 70(5): 1602 - 1611. [Abstract] [Full Text] [PDF]
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Y. Kato, M. Sugiura, T. Sugiura, T. Wakayama, Y. Kubo, D. Kobayashi, Y. Sai, I. Tamai, S. Iseki, and A. Tsuji Organic Cation/Carnitine Transporter OCTN2 (Slc22a5) Is Responsible for Carnitine Transport across Apical Membranes of Small Intestinal Epithelial Cells in Mouse Mol. Pharmacol., September 1, 2006; 70(3): 829 - 837. [Abstract] [Full Text] [PDF]
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R. Kato, T. Maeda, T. Akaike, and I. Tamai Characterization of novel Na+-dependent nucleobase transport systems at the blood-testis barrier Am J Physiol Endocrinol Metab, May 1, 2006; 290(5): E968 - E975. [Abstract] [Full Text] [PDF]
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 B. Kwok, A. Yamauchi, R. Rajesan, L. Chan, U. Dhillon, W. Gao, H. Xu, B. Wang, S. Takahashi, J. Semple, et al. Carnitine/xenobiotics transporters in the human mammary gland epithelia, MCF12A Am J Physiol Regulatory Integrative Comp Physiol, March 1, 2006; 290(3): R793 - R802. [Abstract] [Full Text] [PDF]
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 M. Grube, H. E.U. Meyer zu Schwabedissen, D. Prager;, J. Haney, K.-U. Moritz, K. Meissner, D. Rosskopf, L. Eckel, M. Bohm, G. Jedlitschky, et al. Uptake of Cardiovascular Drugs Into the Human Heart: Expression, Regulation, and Function of the Carnitine Transporter OCTN2 (SLC22A5) Circulation, February 28, 2006; 113(8): 1114 - 1122. [Abstract] [Full Text] [PDF]
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 L. Vernez, M. Dickenmann, J. Steiger, M. Wenk, and S. Krahenbuhl Effect of L-carnitine on the kinetics of carnitine, acylcarnitines and butyrobetaine in long-term haemodialysis Nephrol. Dial. Transplant., February 1, 2006; 21(2): 450 - 458. [Abstract] [Full Text] [PDF]
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D. Kobayashi, M. Irokawa, T. Maeda, A. Tsuji, and I. Tamai Carnitine/organic cation transporter OCTN2-mediated transport of carnitine in primary-cultured epididymal epithelial cells Reproduction, December 1, 2005; 130(6): 931 - 937. [Abstract] [Full Text] [PDF]
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 A. Mancinelli, A. M. Evans, R. L. Nation, and A. Longo Uptake of L-Carnitine and Its Short-Chain Ester Propionyl-L-carnitine in the Isolated Perfused Rat Liver J. Pharmacol. Exp. Ther., October 1, 2005; 315(1): 118 - 124. [Abstract] [Full Text] [PDF]
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 Y. Kobayashi, A. Shibusawa, H. Saito, N. Ohshiro, M. Ohbayashi, N. Kohyama, and T. Yamamoto Isolation and Functional Characterization of a Novel Organic Solute Carrier Protein, hOSCP1 J. Biol. Chem., September 16, 2005; 280(37): 32332 - 32339. [Abstract] [Full Text] [PDF]
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D. Kobayashi, A. Goto, T. Maeda, J.-i. Nezu, A. Tsuji, and I. Tamai OCTN2-mediated transport of carnitine in isolated Sertoli cells Reproduction, June 1, 2005; 129(6): 729 - 736. [Abstract] [Full Text] [PDF]
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 D. Grundemann, S. Harlfinger, S. Golz, A. Geerts, A. Lazar, R. Berkels, N. Jung, A. Rubbert, and E. Schomig Discovery of the ergothioneine transporter PNAS, April 5, 2005; 102(14): 5256 - 5261. [Abstract] [Full Text] [PDF]
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N. Ishiguro, A. Saito, K. Yokoyama, M. Morikawa, T. Igarashi, and I. Tamai TRANSPORT OF THE DOPAMINE D2 AGONIST PRAMIPEXOLE BY RAT ORGANIC CATION TRANSPORTERS OCT1 AND OCT2 IN KIDNEY Drug Metab. Dispos., April 1, 2005; 33(4): 495 - 499. [Abstract] [Full Text] [PDF]
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Y. Kato, Y. Sai, K. Yoshida, C. Watanabe, T. Hirata, and A. Tsuji PDZK1 Directly Regulates the Function of Organic Cation/Carnitine Transporter OCTN2 Mol. Pharmacol., March 1, 2005; 67(3): 734 - 743. [Abstract] [Full Text] [PDF]
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M. Grube, H. M. z. Schwabedissen, K. Draber, D. Prager, K.-U. Moritz, K. Linnemann, C. Fusch, G. Jedlitschky, and H. K. Kroemer EXPRESSION, LOCALIZATION, AND FUNCTION OF THE CARNITINE TRANSPORTER OCTN2 (SLC22A5) IN HUMAN PLACENTA Drug Metab. Dispos., January 1, 2005; 33(1): 31 - 37. [Abstract] [Full Text] [PDF]
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E. Rytting and K. L. Audus Novel Organic Cation Transporter 2-Mediated Carnitine Uptake in Placental Choriocarcinoma (BeWo) Cells J. Pharmacol. Exp. Ther., January 1, 2005; 312(1): 192 - 198. [Abstract] [Full Text] [PDF]
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A. J. Hirsh, J. R. Sabater, A. Zamurs, R. T. Smith, A. M. Paradiso, S. Hopkins, W. M. Abraham, and R. C. Boucher Evaluation of Second Generation Amiloride Analogs as Therapy for Cystic Fibrosis Lung Disease J. Pharmacol. Exp. Ther., December 1, 2004; 311(3): 929 - 938. [Abstract] [Full Text] [PDF]
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K. C. Cundy, R. Branch, T. Chernov-Rogan, T. Dias, T. Estrada, K. Hold, K. Koller, X. Liu, A. Mann, M. Panuwat, et al. XP13512 [({+/-})-1-([({alpha}-Isobutanoyloxyethoxy)carbonyl] aminomethyl)-1-cyclohexane Acetic Acid], A Novel Gabapentin Prodrug: I. Design, Synthesis, Enzymatic Conversion to Gabapentin, and Transport by Intestinal Solute Transporters J. Pharmacol. Exp. Ther., October 1, 2004; 311(1): 315 - 323. [Abstract] [Full Text] [PDF]
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 K. Lahjouji, I. Elimrani, J. Lafond, L. Leduc, I. A. Qureshi, and G. A. Mitchell L-Carnitine transport in human placental brush-border membranes is mediated by the sodium-dependent organic cation transporter OCTN2 Am J Physiol Cell Physiol, August 1, 2004; 287(2): C263 - C269. [Abstract] [Full Text] [PDF]
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 S. H. Wright and W. H. Dantzler Molecular and Cellular Physiology of Renal Organic Cation and Anion Transport Physiol Rev, July 1, 2004; 84(3): 987 - 1049. [Abstract] [Full Text] [PDF]
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 S. A. Eraly, J. C. Monte, and S. K. Nigam Novel slc22 transporter homologs in fly, worm, and human clarify the phylogeny of organic anion and cation transporters Physiol Genomics, June 17, 2004; 18(1): 12 - 24. [Abstract] [Full Text] [PDF]
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Y. Kobayashi, N. Ohshiro, A. Tsuchiya, N. Kohyama, M. Ohbayashi, and T. Yamamoto RENAL TRANSPORT OF ORGANIC COMPOUNDS MEDIATED BY MOUSE ORGANIC ANION TRANSPORTER 3 (MOAT3): FURTHER SUBSTRATE SPECIFICITY OF MOAT3 Drug Metab. Dispos., May 1, 2004; 32(5): 479 - 483. [Abstract] [Full Text] [PDF]
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C. Amat di San Filippo and N. Longo Tyrosine Residues Affecting Sodium Stimulation of Carnitine Transport in the OCTN2 Carnitine/Organic Cation Transporter J. Biol. Chem., February 20, 2004; 279(8): 7247 - 7253. [Abstract] [Full Text] [PDF]
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 M. Aouida, N. Page, A. Leduc, M. Peter, and D. Ramotar A Genome-Wide Screen in Saccharomyces cerevisiae Reveals Altered Transport As a Mechanism of Resistance to the Anticancer Drug Bleomycin Cancer Res., February 1, 2004; 64(3): 1102 - 1109. [Abstract] [Full Text] [PDF]
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C. A. di San Filippo, Y. Wang, and N. Longo Functional Domains in the Carnitine Transporter OCTN2, Defective in Primary Carnitine Deficiency J. Biol. Chem., November 28, 2003; 278(48): 47776 - 47784. [Abstract] [Full Text] [PDF]
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S. Tanaka, K. Deai, M. Inagaki, and A. Ichikawa Uptake of histamine by mouse peritoneal macrophages and a macrophage cell line, RAW264.7 Am J Physiol Cell Physiol, September 1, 2003; 285(3): C592 - C598. [Abstract] [Full Text] [PDF]
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 I. Elimrani, K. Lahjouji, E. Seidman, M.-J. Roy, G. A. Mitchell, and I. Qureshi Expression and localization of organic cation/carnitine transporter OCTN2 in Caco-2 cells Am J Physiol Gastrointest Liver Physiol, May 1, 2003; 284(5): G863 - G871. [Abstract] [Full Text] [PDF]
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 I. Cetinkaya, G. Ciarimboli, G. Yalcinkaya, T. Mehrens, A. Velic, J. R. Hirsch, V. Gorboulev, H. Koepsell, and E. Schlatter Regulation of human organic cation transporter hOCT2 by PKA, PI3K, and calmodulin-dependent kinases Am J Physiol Renal Physiol, February 1, 2003; 284(2): F293 - F302. [Abstract] [Full Text] [PDF]
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K. B. Goralski, G. Lou, M. T. Prowse, V. Gorboulev, C. Volk, H. Koepsell, and D. S. Sitar The Cation Transporters rOCT1 and rOCT2 Interact with Bicarbonate but Play Only a Minor Role for Amantadine Uptake into Rat Renal Proximal Tubules J. Pharmacol. Exp. Ther., December 1, 2002; 303(3): 959 - 968. [Abstract] [Full Text] [PDF]
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K. Lee, C. Ng, K. L. R. Brouwer, and D. R. Thakker Secretory Transport of Ranitidine and Famotidine across Caco-2 Cell Monolayers J. Pharmacol. Exp. Ther., November 1, 2002; 303(2): 574 - 580. [Abstract] [Full Text] [PDF]
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A. Enomoto, M. F. Wempe, H. Tsuchida, H. J. Shin, S. H. Cha, N. Anzai, A. Goto, A. Sakamoto, T. Niwa, Y. Kanai, et al. Molecular Identification of a Novel Carnitine Transporter Specific to Human Testis. INSIGHTS INTO THE MECHANISM OF CARNITINE RECOGNITION J. Biol. Chem., September 20, 2002; 277(39): 36262 - 36271. [Abstract] [Full Text] [PDF]
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R. Ohashi, I. Tamai, A. Inano, M. Katsura, Y. Sai, J.-i. Nezu, and A. Tsuji Studies on Functional Sites of Organic Cation/Carnitine Transporter OCTN2 (SLC22A5) Using a Ser467Cys Mutant Protein J. Pharmacol. Exp. Ther., September 1, 2002; 302(3): 1286 - 1294. [Abstract] [Full Text] [PDF]
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D. Kristufek, W. Rudorfer, C. Pifl, and S. Huck Organic cation transporter mRNA and function in the rat superior cervical ganglion J. Physiol., August 15, 2002; 543(1): 117 - 134. [Abstract] [Full Text] [PDF]
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T. Nozawa, M. Nakajima, I. Tamai, K. Noda, J.-i. Nezu, Y. Sai, A. Tsuji, and T. Yokoi Genetic Polymorphisms of Human Organic Anion Transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): Allele Frequencies in the Japanese Population and Functional Analysis J. Pharmacol. Exp. Ther., August 1, 2002; 302(2): 804 - 813. [Abstract] [Full Text] [PDF]
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 E Xiaofei, Y. Wada, M. Dakeishi, F. Hirasawa, K. Murata, H. Masuda, T. Sugiyama, H. Nikaido, and A. Koizumi Age-Associated Cardiomyopathy in Heterozygous Carrier Mice of a Pathological Mutation of Carnitine Transporter Gene, OCTN2 J. Gerontol. A Biol. Sci. Med. Sci., July 1, 2002; 57(7): B270 - 278. [Abstract] [Full Text]
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 Y. Urakami, M. Akazawa, H. Saito, M. Okuda, and K.-i. Inui cDNA Cloning, Functional Characterization, and Tissue Distribution of an Alternatively Spliced Variant of Organic Cation Transporter hOCT2 Predominantly Expressed in the Human Kidney J. Am. Soc. Nephrol., July 1, 2002; 13(7): 1703 - 1710. [Abstract] [Full Text] [PDF]
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 C. M. Rodriguez, J. C. Labus, and B. T. Hinton Organic Cation/Carnitine Transporter, OCTN2, Is Differentially Expressed in the Adult Rat Epididymis Biol Reprod, July 1, 2002; 67(1): 314 - 319. [Abstract] [Full Text] [PDF]
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 E. Cova, U. Laforenza, G. Gastaldi, Y. Sambuy, S. Tritto, A. Faelli, and U. Ventura Guanidine Transport across the Apical and Basolateral Membranes of Human Intestinal Caco-2 Cells Is Mediated by Two Different Mechanisms J. Nutr., July 1, 2002; 132(7): 1995 - 2003. [Abstract] [Full Text] [PDF]
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H. Motohashi, Y. Sakurai, H. Saito, S. Masuda, Y. Urakami, M. Goto, A. Fukatsu, O. Ogawa, and K.-i. Inui Gene Expression Levels and Immunolocalization of Organic Ion Transporters in the Human Kidney J. Am. Soc. Nephrol., April 1, 2002; 13(4): 866 - 874. [Abstract] [Full Text] [PDF]
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M. Takeda, S. Khamdang, S. Narikawa, H. Kimura, Y. Kobayashi, T. Yamamoto, S. H. Cha, T. Sekine, and H. Endou Human Organic Anion Transporters and Human Organic Cation Transporters Mediate Renal Antiviral Transport J. Pharmacol. Exp. Ther., March 1, 2002; 300(3): 918 - 924. [Abstract] [Full Text] [PDF]
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D. H. Sweet, D. S. Miller, and J. B. Pritchard Ventricular Choline Transport. A ROLE FOR ORGANIC CATION TRANSPORTER 2 EXPRESSED IN CHOROID PLEXUS J. Biol. Chem., November 2, 2001; 276(45): 41611 - 41619. [Abstract] [Full Text] [PDF]
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S. Ohnishi, H. Saito, A. Fukada, and K.-I. Inui Independent organic cation transport activity of Na+-L-carnitine cotransport system in LLC-PK1 cells Am J Physiol Renal Physiol, August 1, 2001; 281(2): F273 - F279. [Abstract] [Full Text] [PDF]
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T. Nakanishi, T. Hatanaka, W. Huang, P. D Prasad, F. H Leibach, M. E Ganapathy, and V. Ganapathy Na+- and Cl--coupled active transport of carnitine by the amino acid transporter ATB0,+ from mouse colon expressed in HRPE cells and Xenopus oocytes J. Physiol., April 15, 2001; 532(2): 297 - 304. [Abstract] [Full Text] [PDF]
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Y.-H. Han, D. H. Sweet, D.-N. Hu, and J. B. Pritchard Characterization of a Novel Cationic Drug Transporter in Human Retinal Pigment Epithelial Cells J. Pharmacol. Exp. Ther., April 13, 2001; 296(2): 450 - 457. [Abstract] [Full Text]
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R. Ohashi, I. Tamai, J.-i. Nezu, H. Nikaido, N. Hashimoto, A. Oku, Y. Sai, M. Shimane, and A. Tsuji Molecular and Physiological Evidence for Multifunctionality of Carnitine/Organic Cation Transporter OCTN2 Mol. Pharmacol., February 1, 2001; 59(2): 358 - 366. [Abstract] [Full Text]
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C. A. Wagner, U. Lukewille, S. Kaltenbach, I. Moschen, A. Broer, T. Risler, S. Broer, and F. Lang Functional and pharmacological characterization of human Na+-carnitine cotransporter hOCTN2 Am J Physiol Renal Physiol, September 1, 2000; 279(3): F584 - F591. [Abstract] [Full Text] [PDF]
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V. Ganapathy, P. D. Prasad, M. E. Ganapathy, and F. H. Leibach Placental Transporters Relevant to Drug Distribution across the Maternal-Fetal Interface J. Pharmacol. Exp. Ther., August 1, 2000; 294(2): 413 - 420. [Full Text]
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G. Burckhardt and N. A. Wolff Structure of renal organic anion and cation transporters Am J Physiol Renal Physiol, June 1, 2000; 278(6): F853 - F866. [Abstract] [Full Text] [PDF]
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H. Ueda, Y. Horibe, K.-J. Kim, and V. H. L. Lee Functional Characterization of Organic Cation Drug Transport in the Pigmented Rabbit Conjunctiva Invest. Ophthalmol. Vis. Sci., March 1, 2000; 41(3): 870 - 876. [Abstract] [Full Text]
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Y. Zhu, M. C. Jong, K. A. Frazer, E. Gong, R. M. Krauss, J.-F. Cheng, D. Boffelli, and E. M. Rubin Genomic interval engineering of mice identifies a novel modulator of triglyceride production PNAS, February 1, 2000; 97(3): 1137 - 1142. [Abstract] [Full Text] [PDF]
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M. E. Ganapathy, W. Huang, D. P. Rajan, A. L. Carter, M. Sugawara, K. Iseki, F. H. Leibach, and V. Ganapathy beta -Lactam Antibiotics as Substrates for OCTN2, an Organic Cation/Carnitine Transporter J. Biol. Chem., January 21, 2000; 275(3): 1699 - 1707. [Abstract] [Full Text] [PDF]
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V. Gorboulev, C. Volk, P. Arndt, A. Akhoundova, and H. Koepsell Selectivity of the Polyspecific Cation Transporter rOCT1 Is Changed by Mutation of Aspartate 475 to Glutamate Mol. Pharmacol., December 1, 1999; 56(6): 1254 - 1261. [Abstract] [Full Text]
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P. Seth, X. Wu, W. Huang, F. H. Leibach, and V. Ganapathy Mutations in Novel Organic Cation Transporter (OCTN2), an Organic Cation/Carnitine Transporter, with Differential Effects on the Organic Cation Transport Function and the Carnitine Transport Function J. Biol. Chem., November 19, 1999; 274(47): 33388 - 33392. [Abstract] [Full Text] [PDF]
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R. Ohashi, I. Tamai, H. Yabuuchi, J.-I. Nezu, A. Oku, Y. Sai, M. Shimane, and A. Tsuji Na+-Dependent Carnitine Transport by Organic Cation Transporter (OCTN2): Its Pharmacological and Toxicological Relevance J. Pharmacol. Exp. Ther., November 1, 1999; 291(2): 778 - 784. [Abstract] [Full Text]
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X. Wu, W. Huang, P. D. Prasad, P. Seth, D. P. Rajan, F. H. Leibach, J. Chen, S. J. Conway, and V. Ganapathy Functional Characteristics and Tissue Distribution Pattern of Organic Cation Transporter 2 (OCTN2), an Organic Cation/Carnitine Transporter J. Pharmacol. Exp. Ther., September 1, 1999; 290(3): 1482 - 1492. [Abstract] [Full Text]
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D. Gründemann, G. Liebich, N. Kiefer, S. Köster, and E. Schömig Selective Substrates for Non-Neuronal Monoamine Transporters Mol. Pharmacol., July 1, 1999; 56(1): 1 - 10. [Abstract] [Full Text]
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H. Yabuuchi, I. Tamai, J.-I. Nezu, K. Sakamoto, A. Oku, M. Shimane, Y. Sai, and A. Tsuji Novel Membrane Transporter OCTN1 Mediates Multispecific, Bidirectional, and pH-Dependent Transport of Organic Cations J. Pharmacol. Exp. Ther., May 1, 1999; 289(2): 768 - 773. [Abstract] [Full Text]
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Y. Wang, J. Ye, V. Ganapathy, and N. Longo Mutations in the organic cation/carnitine transporter OCTN2 in primary carnitine deficiency PNAS, March 2, 1999; 96(5): 2356 - 2360. [Abstract] [Full Text] [PDF]
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X. Wu, R. Kekuda, W. Huang, Y.-J. Fei, F. H. Leibach, J. Chen, S. J. Conway, and V. Ganapathy Identity of the Organic Cation Transporter OCT3 as the Extraneuronal Monoamine Transporter (uptake2) and Evidence for the Expression of the Transporter in the Brain J. Biol. Chem., December 4, 1998; 273(49): 32776 - 32786. [Abstract] [Full Text] [PDF]
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Y. Wang, T. A. Meadows, and N. Longo Abnormal Sodium Stimulation of Carnitine Transport in Primary Carnitine Deficiency J. Biol. Chem., June 30, 2000; 275(27): 20782 - 20786. [Abstract] [Full Text] [PDF]
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I. Tamai, R. Ohashi, J.-i. Nezu, Y. Sai, D. Kobayashi, A. Oku, M. Shimane, and A. Tsuji Molecular and Functional Characterization of Organic Cation/Carnitine Transporter Family in Mice J. Biol. Chem., December 15, 2000; 275(51): 40064 - 40072. [Abstract] [Full Text] [PDF]
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