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J Biol Chem, Vol. 275, Issue 6, 4507-4512, February 11, 2000
From the A cDNA encoding a novel multispecific organic
anion transporter, OAT4, was isolated from a human kidney cDNA
library. The OAT4 cDNA consisted of 2210 base pairs that encoded a
550-amino acid residue protein with 12 putative membrane-spanning
domains. The amino acid sequence of OAT4 showed 38 to 44% identity to
those of other members of the OAT family. Northern blot analysis
revealed that OAT4 mRNA is abundantly expressed in the placenta as
well as in the kidney. When expressed in Xenopus oocytes,
OAT4 mediated the high affinity transport of estrone sulfate
(Km = 1.01 µM) and
dehydroepiandrosterone sulfate (Km = 0.63 µM) in a sodium-independent manner. OAT4 also mediated
the transport of ochratoxin A. OAT4-mediated transport of estrone
sulfate was inhibited by several sulfate conjugates, such as
p-nitrophenyl sulfate, Organic anions include a variety of drugs and xenobiotics, many of
which are harmful to the body. In addition, most lipophilic compounds
of both endogenous and exogenous origin are metabolized to organic
anions, e.g. sulfate and glucuronide conjugates. The kidney
and the liver play a central role in the elimination of these toxic
anionic compounds from the body (1-5). In the kidney, proximal tubular
cells take up organic anions from the blood via multispecific organic
anion transport pathway(s) in the basolateral membrane (1-3). In 1997, the multispecific organic anion transporter, organic anion transporter
1 (OAT1),1 was first isolated
from rat kidney cDNA library by the expression cloning method (6,
7). Human (8, 9) and mouse (10, 11) homolog have been also cloned and
characterized. Rat OAT1 is localized at the basolateral membrane of the
middle proximal tubule (S2) (12) and mediates the uptake of a variety
of organic anions into the proximal tubular cells (6, 13-15). To date, two other isoforms, i.e. OAT2 (16) and OAT3 (17, 36), have been identified.
The transcellular transport of organic anions has been demonstrated in
other tissues where the tissue-specific barrier system exists. In the
brain, blood-brain barrier and blood-cerebrospinal fluid barrier
protect the brain from the invasion of xenobiotics (18-20). Recently,
two isoforms of the oatp (organic anion-transporting polypeptide)
family, i.e. oatp1 (21) and oatp2 (22), were shown to be
expressed in the brain, and oatp1 was localized to blood-cerebrospinal
fluid barrier (23). We also suggested the existence of OAT3 in
blood-cerebrospinal fluid barrier (17). P-glycoprotein, a member of the
ABC (ATP binding cassette) family of transporters, was shown to be
expressed in blood-brain barrier (24, 25). Thus, the transporter
molecules, which are likely to act as efflux system of xenobiotics in
blood-brain barrier and blood-cerebrospinal fluid barrier, have just
begun to be identified.
In the placenta, the presence of a tissue-barrier system has been also
predicted. However, little is known as to the mechanisms by which the
placenta carries out this barrier function. The fetus is very
vulnerable to foreign substances that enter the fetal circulation, and
numerous drugs have been known to cause developmental defects in the
fetus. Moreover, the fetus generates harmful metabolites, such as
organic anions. Since the fetal kidney and liver possess limited
capacity for the secretion, it is probable that the placenta plays the
primary role in the excretion of these toxic compounds from the fetus.
In the present study, we report the isolation of a novel member of the
multispecific organic anion transporter family, OAT4. A high level of
mRNA expression of OAT4 was detected in the placenta as well as in
the kidney.
Isolation of OAT4--
EST (expressed sequence tag) data base
were searched for "query OAT1," and an EST clone (H12876) was
identified. The [32P]dCTP-labeled probe was synthesized
from the clone H12876 and used for the screening of a human kidney
cDNA library. A nondirectional cDNA library was prepared from
human kidney poly(A)+ RNA (CLONTECH)
using the Superscript Choice system (Life Technologies, Inc.). The
screening of the cDNA library by H12876 was performed as
described elsewhere (17).
Sequence Determination--
Specially synthesized
oligonucleotide primers were used for the sequencing of the OAT4
cDNA by the dye-termination method using ABI Prism TM 310.
cRNA Synthesis and Uptake Experiments Using Xenopus laevis
Oocytes--
cRNA synthesis and uptake measurements were performed as
described previously (17). The capped cRNA was synthesized in
vitro using T7 RNA polymerase from the plasmid DNA linearized with
HindIII. Defolliculated oocytes were injected with 10 ng of
the capped OAT4 cRNA and incubated in Barth's solution (88 mM NaCl, 1 mM KCl, 0.33 mM
Ca(NO3)2, 0.4 mM CaCl2,
0.8 mM MgSO4, 2.4 mM
NaHCO3, and 10 mM HEPES) containing 50 µg/ml
gentamicin at 18 °C. After 2 to 3 days of incubation, uptake and
efflux experiments were performed at room temperature in ND96 solution
(96 mM NaCl, 2 mM KCl, 1.8 mM
CaCl2, 1 mM MgCl2, and 5 mM HEPES, pH 7.4) as described elsewhere (17). We repeated
each experiment more than two times to confirm the results. The
representative results are shown in Figs. 3 to 7. The kinetic
parameters were obtained by an iterative nonlinear least squares method
using a MULTI program (26).
Northern Blot Analysis--
A commercially available
hybridization blot containing poly(A)+ RNA from various
human tissues (human 12-lane multiple tissue Northern
(MTN)TM blot, CLONTECH) was used for
the Northern blot analysis for OAT4. We used an OAT4 cDNA fragment
(position numbers 1355-1758) as a probe, whose nucleotide sequence
showed 60% identity to the corresponding region of human OAT1 and less
than 60% identity to those of rat OAT1, rat OAT2, and rat OAT3. The
master blot filter was hybridized with the probe overnight at 42 °C
according to the manufacturer's instructions. The filter was washed
finally in a high stringency condition (0.1 × SSC (1 × SSC = 0.15 M NaCl and 0.015 M sodium
citrate) and 0.1% SDS at 65 °C).
An EST data base search identified an EST clone, H12876, which
showed significant identity to OAT1, OAT2, and OAT3. A human kidney
cDNA library was screened using H12876 as a probe, and a cDNA
encoding a novel membrane protein (OAT4) was isolated. OAT4 cDNA
consisted of 2210 base pairs encoding a 550-amino acid residue protein.
Fig. 1 shows the deduced amino acid
sequence of human OAT4 in the alignment with those of human OAT1, rat
OAT2, and rat OAT3. The amino acid sequence of OAT4 showed 44, 43, 38, and 43% identity to those of human OAT1, rat OAT1, rat OAT2, and rat
OAT3, respectively. OAT4 also showed significant identity to rat OCT1
(35%) (27), rat OCT2 (33%) (28), and rat OCT3 (36%) (29).
Kyte-Doolittle hydropathy plot analysis (30) predicted 12 membrane-spanning domains in OAT4 (hydropathy plot not shown). As is
the case in the members of the OAT and OCT families,
N-glycosylation sites (residues 39, 56, 99, 310, 353) and
protein kinase C-dependent phosphorylation sites (residue
65, 164, 224, 225, 279, 319, 326, 428, 529) were predicted in the
sequence of OAT4 (Fig. 1).
The expression of OAT4 mRNA in human tissues was investigated (Fig.
2). A strong mRNA band was detected
only in the kidney (2.7 kilobases) and placenta (2.4 kilobases). No
hybridization signals were detected with mRNAs isolated from other
tissues, including the brain, heart, skeletal muscle, thymus, spleen,
liver, small intestine, lung, and peripheral blood leukocytes. Since the size of mRNA bands detected in the kidney and the placenta were
different, we screened a human placenta cDNA library using H12876
as a probe and isolated a positive full-length cDNA clone. The
sequencing of this clone revealed that the cDNAs isolated from the
kidney (the present OAT4 cDNA clone) and the placenta were
identical, except that the placenta clone possessed a shorter untranslated 5' region.
Molecular Cloning and Characterization of Multispecific
Organic Anion Transporter 4 Expressed in the Placenta*
,,§,,,,, and¶
Department of Pharmacology and Toxicology,
Kyorin University School of Medicine, 6-20-2 Shinkawa, Mitaka,
Tokyo, 181-8611 and § Department of Biopharmaceutics,
Graduate School of Pharmaceutical Sciences, University of Tokyo,
7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan
ABSTRACT
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INTRODUCTION
EXPERIMENTAL PROCEDURES
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DISCUSSION
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-naphthyl sulfate, 
-estradiol
sulfate, and 4-methylumbelliferyl sulfate. By contrast, glucuronide
conjugates showed little or no inhibitory effect on the OAT4-mediated
transport of estrone sulfate. OAT4 interacted with chemically
heterogeneous anionic compounds, such as nonsteroidal anti-inflammatory
drugs, diuretics, sulfobromophthalein, penicillin G, and bile salts,
whereas tetraethylammonium, an organic cation, did not. OAT4 is the
first member of the multispecific organic anion transporter family,
which is expressed abundantly in the placenta. OAT4 might be
responsible for the elimination and detoxification of harmful anionic
substances from the fetus.
INTRODUCTION
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ABSTRACT
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EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
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EXPERIMENTAL PROCEDURES
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View larger version (80K):
[in a new window]
Fig. 1.
The amino acid sequence of OAT4 aligned with
those of human OAT1, rat OAT2, and rat OAT3. Shaded
residues indicate conserved residues in at least two transporters.
Putative N-linked glycosylation sites in OAT4 are indicated
by stars, and putative protein kinase C phosphorylation
sites are indicated by closed circles. The probe (H12876)
that we used for the screening of OAT4 corresponds to the amino acid
residues 437-550 of OAT4 with partial 3'-untranslated regions, which
is indicated by the line over the alignment. The same region
was used for the Northern blot analysis shown in Fig. 2. r,
rat; h, human.
View larger version (64K):
[in a new window]
Fig. 2.
Northern blot analysis of OAT4. Human
multiple tissue blot (CLONTECH) that contains 1 µg of poly(A)+ RNAs from 12 human tissues in each of the
lanes was probed with a 32P-labeled OAT4
cDNA fragment and was washed in a high stringent condition.
kb, kilobases.
Using the Xenopus oocytes expression system, we investigated
transport of organic anions by OAT4 (Fig.
3). The uptake rates of
[3H]estrone sulfate,
[3H]dehydroepiandrosterone sulfate (DHEA-s), and
[3H]ochratoxin A in oocytes expressing OAT4 were much
higher than those of control oocytes. A very low rate of uptake of
p-aminohippurate (a prototypical substrate of OAT1) via OAT4
was also demonstrated.
|
Fig. 4 shows the transport properties of
estrone sulfate via OAT4. The cell-associated count of
[3H]estrone sulfate increased linearly until 2.5 h
of incubation in OAT4-expressing oocytes. This result indicates that
OAT4 not only binds but also translocates estrone sulfate into
cytoplasm (Fig. 4A). The uptake rate of estrone sulfate via
OAT4 was not affected by replacement of the extracellular sodium with
lithium or choline (Fig. 4B). In the experiment shown in
Fig. 4C, the trans-stimulatory effect of estrone
sulfate on OAT4-mediated efflux of estrone sulfate was examined. The
efflux of estrone sulfate was not trans-stimulated in the
presence of extracellular estrone sulfate (0.2 and 2 µM).
|
The concentration dependence of OAT4-mediated uptake of
[3H]estrone sulfate and [3H]DHEA-s was
examined (Fig. 5). OAT4-mediated uptake
of these two compounds showed saturable kinetics and followed the
Michaelis-Menten equation. Nonlinear regression analyses yielded
Km values of 1.01 ± 0.15 µM and
0.63 ± 0.04 µM and Vmax
values of 1.78 ± 0.16 pmol/h/oocyte and 1.26 ± 0.04 pmol/h/oocyte for estrone sulfate and DHEA-s, respectively.
|
To investigate the substrate selectivity of OAT4, inhibition study was
performed. cis-Inhibitory effect of 5, 50, and 500 µM concentrations of various compounds on OAT4-mediated
[3H]estrone sulfate (50 nM) uptake was
investigated (Fig. 6). Because of its
cytotoxic effect, 100 µM sulfobromophthalein was used
instead of 500 µM. Five µM of unlabeled
estrone sulfate and sulfobromophthalein showed definite inhibitory
potency. Probenecid, indomethacin, ibuprofen, diclofenac, furosemide,
bumetanide, and corticosterone (a neutral steroid hormone) exhibited
modest but dose-dependent inhibitory activity at 5 and 50 µM. Penicillin-G, cholic acid, and taurocholic acid
showed much weaker inhibition. In contrast, 500 µM
p-aminohippuric acid (PAH), glutaric acid, salicylic
acid, and azidothymidine did not show inhibitory activity.
-Estradiol, tetraethylammonium (an organic cation), and
Na2SO4 (an inorganic sulfate) also did not show
any inhibitory effect on OAT4-mediated [3H]estrone
sulfate uptake. Since in the result shown in Fig. 3, a very low rate of
uptake of PAH via OAT4 was demonstrated, we examined the inhibitory
potency of PAH at higher concentrations. The result indicated that high
concentrations of PAH (more than several mM) inhibited
OAT4-mediated uptake of estrone sulfate (data not shown).
|
Interaction of OAT4 with several sulfate conjugates and
glucuronide conjugates was also examined (Fig.
7). Five µM sulfate conjugates (estrone-s, DHEA-s, p-nitrophenyl-s,
-naphthyl-s, 4-methylumbelliferyl-s, and -estradiol-s)
showed inhibitory potency on OAT4-mediated uptake of
[3H]estrone sulfate. At 100 µM, all of the
sulfate conjugates except minoxidil sulfate potently inhibited OAT4
(data not shown). In contrast, all of the glucuronide conjugates with
similar side chains showed no inhibition at 5 µM. Even at
500 µM, only chloramphenicol glucuronide and
-naphthyl--glucuronide showed inhibitory potency (data not
shown).
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In the present study, we reported the isolation of OAT4. OAT4 mRNA was abundantly expressed in the placenta as well as in the kidney and mediated the transport of anionic compounds, including sulfate conjugates.
Fetal blood is separated from the maternal blood circulation by the polarized cells, i.e. syncytiotrophoblast, which possess carrier-mediated transport pathways similar to those in the renal proximal tubules and intestinal epithelial cells. Substantive knowledge on the placental transfer of essential compounds from the maternal body to the fetus has been gained, and the expressions of nutrient transporters such as glucose transporters (31), amino acid transporters (32), a vitamin transporter (33), and nucleoside transporters (34) have been identified in the placenta. These carrier proteins facilitate the supply of essential compounds to the developing fetus. In contrast, little is known regarding the elimination pathways for toxic compounds from the fetus. Since the fetal kidney and liver possess a limited capacity for excretion (35), the placenta probably plays the primary role in the elimination of the toxic compounds from the fetus. The present study demonstrated a high level of expression of OAT4 in the placenta and the multiple substrate recognition by OAT4. Rat OAT2 (16) and human OAT3 (36)2 are not expressed in the placenta. The expression of human OAT1 in the placenta was extremely weak or none. Thus, OAT4 is predominantly expressed in the placenta among OAT isoforms and is likely to mediate the excretion of toxic anionic substances from the fetal body. Recently, two candidate excretory pathways have been identified in the placenta. ABCP (37), a member of the ABC superfamily, and OCT3 (29) were demonstrated to be expressed in the placenta. Both of the members of the ABC transporter superfamily and OCT family mediate the elimination of xenobiotics from the body. The entity "placental barrier" may be composed of these xenobiotics transporters, including OAT4.
The placenta is a unique endocrine organ producing peptide hormones and
steroid hormones. The placenta synthesizes a large amount of steroid
hormones, especially estrogens (38). In the placenta, estrogens
(estrone, estradiol, and estriol) are synthesized from DHEA-s or
16-OH DHEA-s, both of which are derived from the fetal adrenal
gland. Thus, the fetus and placenta function together as an endocrine
unit for the production of estrogen, which is important for
continuation of the pregnancy. DHEA-s, however, shows undesirable
effects (e.g. intrauterine growth retardation) on the fetus,
at high blood concentrations (39). Efficient uptake of DHEA-s by the
placenta, therefore, is required not only for the production of
estrogen but also for the protection of fetus from the cytotoxicity of
DHEA-s. Among OAT isoforms, OAT3 also mediates the high affinity
transport of estrone sulfate (17). However, as stated above, the
expression of OAT3 in the human placenta is little or none. It is
probable that OAT4 is localized in the trophoblast membrane facing the
fetal blood and mediates the placental uptake of DHEA-s, although the
localization of OAT4 in the placenta has not yet been identified.
OAT1 shows affinity for compounds possessing negative or partial
negative charge(s) and an appropriately sized hydrophobic core (3, 6,
13). The finding that -estradiol showed no inhibitory effect on the
OAT4-mediated uptake of estrone sulfate whereas -estradiol sulfate
showed a strong inhibitory effect suggests that the anionic moiety is
essential for substrate recognition by OAT4. p-Nitrophenyl
sulfate and -naphthyl sulfate were shown to interact with OAT4.
Thus, the binding site of OAT4 can accept variable sizes of the
hydrophobic side chain (from the phenyl moiety to the steroid core) of
the sulfate conjugates. In contrast, glucuronide conjugates with
similar hydrophobic side chains showed no or little inhibitory effect
on OAT4-mediated transport. The glucuronide moiety might be too large
to be accepted by OAT4. Thus, the interaction of OAT4 with the
hydrophilic part (negatively charged site) of the substrate seems
rather stringent. The molecular mechanism underlying the multispecific
substrate recognition by OAT4 is considered to depend largely on the
nonspecific hydrophobic interaction between the heterogeneous and
variably sized hydrophobic structures of the substrates and OAT4.
The present study showed that OAT4 is expressed in the kidney as well as in the placenta. The other OAT isoforms, OAT1 (6-11), OAT2 (6, 40), and OAT3 (17, 36) have been shown to be expressed in the kidney. RST1 (41) and UST1 (42), candidate members of the OAT family, are exclusively expressed in the kidney. Thus, OAT isoforms are commonly expressed in the kidney. Previously, it had been suggested that a single multispecific organic anion transporter (the PAH transporter) is responsible for the basolateral uptake of a number of anionic substances (1-4). However, the renal organic anion transport system is more complex than has been predicted, and the renal proximal tubules are equipped with an array of OAT isoforms. Five hundred µM PAH and glutaric acid, high affinity substrates of OAT1 (6), showed no or very little inhibitory activity on OAT4-mediated estrone sulfate transport. Salicylate, a good substrate of OAT2 (16), also showed weak inhibitory effect on OAT4-mediated transport. Azidothymidine and penicillin G, both of which potently inhibited OAT3-mediated transport (17), showed minimal effect on OAT4. Thus, OAT4 shows a distinct substrate selectivity, and the isoforms of the OAT family cover a large variety of anionic substances and execute the efficient tubular secretion of organic anions.
The transport mechanism of OAT4 (in other words, the driving force of OAT4) is an important issue that should be clarified. OAT1 is a tertiary active organic anion/dicarboxylate exchanger in physiological condition, and OAT1-mediated transport of organic anions is indirectly coupled to the Na+ ion in the extracellular medium (2, 43). The energetically uphill transport of organic anions via OAT1 is accelerated by outwardly directed dicarboxylate gradient (6, 7), which is maintained by sodium dicarboxylate cotransporter (2, 43). Transport activity via OAT4 did not directly depend on the extracellular sodium ion. trans-Stimulatory effect was not demonstrated in the present study. Thus, the driving force of OAT4-mediated transport still remains to be elucidated. Likewise, the driving forces of OAT2 and OAT3 also have not been clarified yet. Recently, a distinct organic anion transporter, oatp1, was revealed to be an organic anion/glutathione exchanger (44). Unspecified endogenous substances might be the counterion in the transport of OAT4. Further studies are required to address this issue.
In conclusion, we report the molecular cloning of OAT4. OAT4 is
exclusively expressed in the placenta and the kidney. OAT4 mediates the
high affinity transport of estrone sulfate and DHEA-s and shows
affinity for a variety of anionic substances. OAT4 is likely to mediate
the placental uptake of DHEA-s, a precursor of estrogen. Furthermore,
OAT4 may play the major role in the excretion of toxic anionic
substances from the fetal body.
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FOOTNOTES |
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* This work was supported in part by grants from the Japanese Ministry of Education Science, Sports, and Culture, (grants-in-aid for scientific research and High Tech Research Center), the Science Research Promotion Fund of the Japan Private School Promotion Foundation, the Uehara Memorial Foundation, and 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) AB026198.
¶ To whom correspondence should be addressed. Tel.: 81-422-47-5511 (ext. 3451); Fax: 81-422-79-1321.
2 S. H. Cha, T. Sekine, Y. Kanai, and H. Endou, unpublished observation.
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ABBREVIATIONS |
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The abbreviations used are: OAT, organic anion transporter; oatp, organic anion-transporting polypeptide; PAH, p-aminohippuric acid; DHEA-s, dehydroepiandrosterone sulfate.
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ABSTRACT
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DISCUSSION
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C. Sauvant, H. Holzinger, and M. Gekle Short-Term Regulation of Basolateral Organic Anion Uptake in Proximal Tubular OK cells: EGF Acts via MAPK, PLA2, and COX1 J. Am. Soc. Nephrol., August 1, 2002; 13(8): 1981 - 1991. [Abstract] [Full Text] [PDF]
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D. H. Sweet, D. S. Miller, J. B. Pritchard, Y. Fujiwara, D. R. Beier, and S. K. Nigam Impaired Organic Anion Transport in Kidney and Choroid Plexus of Organic Anion Transporter 3 (Oat3 (Slc22a8)) Knockout Mice J. Biol. Chem., July 19, 2002; 277(30): 26934 - 26943. [Abstract] [Full Text] [PDF]
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Y. Kobayashi, N. Ohshiro, A. Shibusawa, T. Sasaki, S. Tokuyama, T. Sekine, H. Endou, and T. Yamamoto Isolation, Characterization and Differential Gene Expression of Multispecific Organic Anion Transporter 2 in Mice Mol. Pharmacol., July 1, 2002; 62(1): 7 - 14. [Abstract] [Full Text] [PDF]
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A. Enomoto, M. Takeda, A. Tojo, T. Sekine, S. H. Cha, S. Khamdang, F. Takayama, I. Aoyama, S. Nakamura, H. Endou, et al. Role of Organic Anion Transporters in the Tubular Transport of Indoxyl Sulfate and the Induction of its Nephrotoxicity J. Am. Soc. Nephrol., July 1, 2002; 13(7): 1711 - 1720. [Abstract] [Full Text] [PDF]
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A. Enomoto, M. Takeda, M. Shimoda, S. Narikawa, Y. Kobayashi, Y. Kobayashi, T. Yamamoto, T. Sekine, S. H. Cha, T. Niwa, et al. Interaction of Human Organic Anion Transporters 2 and 4 with Organic Anion Transport Inhibitors J. Pharmacol. Exp. Ther., June 1, 2002; 301(3): 797 - 802. [Abstract] [Full Text] [PDF]
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M. V. St-Pierre, B. Hagenbuch, B. Ugele, P. J. Meier, and T. Stallmach Characterization of an Organic Anion-Transporting Polypeptide (OATP-B) in Human Placenta J. Clin. Endocrinol. Metab., April 1, 2002; 87(4): 1856 - 1863. [Abstract] [Full Text] [PDF]
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S. C. N. Buist, N. J. Cherrington, S. Choudhuri, D. P. Hartley, and C. D. Klaassen Gender-Specific and Developmental Influences on the Expression of Rat Organic Anion Transporters J. Pharmacol. Exp. Ther., April 1, 2002; 301(1): 145 - 151. [Abstract] [Full Text] [PDF]
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H. Kimura, M. Takeda, S. Narikawa, A. Enomoto, K. Ichida, and H. Endou Human Organic Anion Transporters and Human Organic Cation Transporters Mediate Renal Transport of Prostaglandins J. Pharmacol. Exp. Ther., April 1, 2002; 301(1): 293 - 298. [Abstract] [Full Text] [PDF]
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R. Kojima, T. Sekine, M. Kawachi, S. H. Cha, Y. Suzuki, and H. Endou Immunolocalization of Multispecific Organic Anion Transporters, OAT1, OAT2, and OAT3, in Rat Kidney J. Am. Soc. Nephrol., April 1, 2002; 13(4): 848 - 857. [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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G. Hill, T. Cihlar, C. Oo, E. S. Ho, K. Prior, H. Wiltshire, J. Barrett, B. Liu, and P. Ward The Anti-Influenza Drug Oseltamivir Exhibits Low Potential to Induce Pharmacokinetic Drug Interactions via Renal Secretion---Correlation of in Vivo and in Vitro Studies Drug Metab. Dispos., January 1, 2002; 30(1): 13 - 19. [Abstract] [Full Text] [PDF]
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 G. Lee, S. Dallas, M. Hong, and R. Bendayan Drug Transporters in the Central Nervous System: Brain Barriers and Brain Parenchyma Considerations Pharmacol. Rev., December 1, 2001; 53(4): 569 - 596. [Abstract] [Full Text] [PDF]
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N. A. WOLFF, B. GRUNWALD, B. FRIEDRICH, F. LANG, S. GODEHARDT, and G. BURCKHARDT Cationic Amino Acids Involved in Dicarboxylate Binding of the Flounder Renal Organic Anion Transporter J. Am. Soc. Nephrol., October 1, 2001; 12(10): 2012 - 2018. [Abstract] [Full Text] [PDF]
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D. H. Sweet, K. T. Bush, and S. K. Nigam The organic anion transporter family: from physiology to ontogeny and the clinic Am J Physiol Renal Physiol, August 1, 2001; 281(2): F197 - F205. [Abstract] [Full Text] [PDF]
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S. H. Cha, T. Sekine, J.-i. Fukushima, Y. Kanai, Y. Kobayashi, T. Goya, and H. Endou Identification and Characterization of Human Organic Anion Transporter 3 Expressing Predominantly in the Kidney Mol. Pharmacol., April 16, 2001; 59(5): 1277 - 1286. [Abstract] [Full Text]
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A. S. Mulato, E. S. Ho, and T. Cihlar Nonsteroidal Anti-Inflammatory Drugs Efficiently Reduce the Transport and Cytotoxicity of Adefovir Mediated by the Human Renal Organic Anion Transporter 1 J. Pharmacol. Exp. Ther., October 1, 2000; 295(1): 10 - 15. [Abstract] [Full Text]
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S. Wada, M. Tsuda, T. Sekine, S. H. Cha, M. Kimura, Y. Kanai, and H. Endou Rat Multispecific Organic Anion Transporter 1 (rOAT1) Transports Zidovudine, Acyclovir, and Other Antiviral Nucleoside Analogs J. Pharmacol. Exp. Ther., September 1, 2000; 294(3): 844 - 849. [Abstract] [Full Text]
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D. Chamoun, M. D. DeMoura, E. Levitas, C. E. Resnick, S. E. Gargosky, R. G. Rosenfeld, T. Matsumoto, and E. Y. Adashi Transcriptional and Posttranscriptional Regulation of Intraovarian Insulin-Like Growth Factor-Binding Proteins by Interleukin-1{beta} (IL-1{beta}): Evidence for IL-1{beta} as an Antiatretic Principal Endocrinology, August 1, 1999; 140(8): 3488 - 3495. [Abstract] [Full Text]
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Y.-M. Qian, W.-C. Song, H. Cui, S. P. C. Cole, and R. G. Deeley Glutathione Stimulates Sulfated Estrogen Transport by Multidrug Resistance Protein 1 J. Biol. Chem., February 23, 2001; 276(9): 6404 - 6411. [Abstract] [Full Text] [PDF]
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 A. Emoto, F. Ushigome, N. Koyabu, H. Kajiya, K. Okabe, S. Satoh, K. Tsukimori, H. Nakano, H. Ohtani, and Y. Sawada H+-linked transport of salicylic acid, an NSAID, in the human trophoblast cell line BeWo Am J Physiol Cell Physiol, May 1, 2002; 282(5): C1064 - C1075. [Abstract] [Full Text] [PDF]
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