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(Received for publication, April 15, 1997, and in revised form, June 3, 1997)
From the Department of Pharmacology and Toxicology, Kyorin
University School of Medicine, 6-20-2 Shinkawa, Mitaka, Tokyo
181, Japan
ABSTRACT Numerous drugs and endogenous compounds are
efficiently excreted from the renal proximal tubule via
carrier-mediated pathways. Transepithelial excretion of organic anions
occurs via their accumulative transport from the blood into the
proximal tubule cells across the basolateral membrane and subsequent
secretion into the urine through the apical membrane. Here we report on
the isolation of a novel complementary DNA from rat kidney that encodes
a 551-amino acid residue protein (OAT1) with 12 putative
membrane-spanning domains. When expressed in Xenopus laevis
oocytes, OAT1 mediated sodium-independent para-aminohippurate (PAH)
uptake (Km = 14.3 ± 2.9 µM).
The uptake rate of PAH was increased by the outwardly directed
dicarboxylate gradient, consisting with the idea that OAT1 is an
organic anion/dicarboxylate exchanger. OAT1 displayed remarkably wide
substrate selectivity, covering endogenous substrates such as cyclic
nucleotides, a prostaglandin and uric acid, and a variety of drugs
with different structures (e.g. antibiotics, a nonsteroidal
anti-inflammatory drug, diuretics, an antineoplastic drug, and a
uricosuric drug). The Northern blot analysis and in situ
hybridization revealed that OAT1 is exclusively expressed in the
particular segment of the proximal tubule in the kidney. These data
suggest that OAT1 is a multispecific organic anion transporter at the
basolateral membrane of the proximal tubule. Isolation of OAT1 will
facilitate elucidation of the molecular basis of drug kinetics and the
development of new drugs lacking unwanted side effects.
INTRODUCTION The kidney plays an essential role in the elimination of numerous
organic anions including endogenous compounds, xenobiotics, and their
metabolites (1-3). The proximal tubule cells actively secrete them
into the urine. The first step of this secretion is the extraction of
organic anion from the peritubular blood plasma by the proximal tubule
cells through the basolateral membrane. This basolateral uptake of
organic anions has been extensively investigated using
para-aminohippuric acid (PAH)1 as a test
substrate. The most striking feature of this organic anion transport
system is its extremely wide substrate selectivity, covering not only
endogenous anionic substrates but also a number of clinically important
drugs (1, 3). Because of its importance in renal physiology and
pharmacology, cloning of the organic anion transporter has been
attempted by many investigators using different approaches; however,
the molecular structure of the responsible transporter has not yet
determined.
For the last decade it has been proposed that the basolateral uptake of
organic anion is mediated by organic anion/dicarboxylate exchanger (1,
4). According to this model, outwardly directed dicarboxylate gradient
is essential to express the transport activity of this exchanger. In
the present study, we isolated first rat sodium dicarboxylate
transporter (rNaDC-1) and then co-expressed it together with rat kidney
poly(A)+ RNA in Xenopus oocytes to energize
organic anion transport in oocytes. We describe here functional
expression cloning of an organic anion/dicarboxylate exchanger (OAT1)
and its characteristics as a multispecific organic anion
transporter.
EXPERIMENTAL PROCEDURES A
nondirectional cDNA library was prepared from rat kidney
poly(A)+ RNA using Superscript Choice system (Life
Technologies, Inc.) and was ligated to Xenopus laevis oocyte
expression studies and uptake measurements were performed as described
elsewhere (6). Defolliculated oocytes were injected with in
vitro transcribed cRNA and/or rat kidney poly(A)+ RNA
as indicated in each experiment. In vitro transcription was done by using T7 RNA polymerase in the presence of cap analog. After
incubation of oocytes at 18 °C for 2-3 days, uptake studies were
performed in sodium uptake solution (96 mM NaCl, 2 mM KCl, 1.8 mM CaCl2, 1 mM MgCl2, 5 mM HEPES, pH 7.4)
containing radiolabeled substrates as indicated in each experiment.
Four-hundred µg of rat kidney poly(A)+ RNA was
size-fractionated as described elsewhere (6) using preparative gel
electrophoresis (Bio-Rad, model 491 Prep cell). Then we co-injected
poly(A)+ RNAs of each fraction together with rNaDC-1 cRNA
into oocytes. Before the uptake study, the oocytes were routinely
preincubated for 2 h in sodium uptake solution containing 1 mM glutarate. [14C]PAH (50 µM)
uptake was measured in sodium uptake solution without glutarate for
1 h. A directional cDNA library was constructed from fractions
showing the highest rate of [14C]PAH uptake
(1.8-2.4-kilobase (kb) poly(A)+ RNA) using Superscript
Plasmid system (Life Technologies, Inc.) and was ligated into the
SalI and NotI site of pSPORT 1. Recombinants were
electroporated into Electro Max DH10B competent cells (Life Technologies, Inc.). Approximately 500 colonies were grown on nitrocellulose membrane. Plasmid DNA was purified from colonies of each
plate. Capped cRNA was synthesized in vitro after
linearization of each plasmid DNA with NotI. Then we
co-injected cRNA synthesized from each filter together with 2 ng of
rNaDC-1 cRNA into oocytes. When [14C]PAH uptake was
detected on a particular group, it was subdivided into several groups
and further screened. Eight-thousand clones were screened until a
single clone was isolated.
Deleted clones obtained by
Kilo-Sequence deletion kit (Takara, Japan), or specially synthesized
oligonucleotide primers were used for sequencing of rNaDC1 and OAT1
cDNA. rNaDC1 and OAT1 were sequenced by dideoxytermination method
using Sequenase version 2.0 (Amersham Corp.) or dye primer cycle
sequencing kit (Applied Biosystems).
The functional
characterization of OAT1 was analyzed without co-expression of rNaDC-1
except for the experiment of which the results are shown in Fig.
1c. In experiments of Fig. 1, d and e,
and Fig. 4, a and b, oocytes expressed with OAT1
were preincubated with 1 mM glutarate for 2 h before
uptake studies were performed. For the determination of the sodium
dependence of OAT1 transport activity, [14C]PAH uptake
was measured either in sodium uptake solution or in choline chloride
uptake solution (96 mM NaCl of sodium solution was replaced
by 96 mM choline chloride, and pH was adjusted to 7.4 with
Tris). For kinetic analysis, [14C]PAH influx was measured
for 3 min. For inhibition study, 2 µM [14C]PAH uptake via OAT1 was measured in the absence or
presence of 2 mM nonradiolabeled compounds in sodium uptake
solution.
Three µg of poly(A)+
RNA prepared from various rat tissues were electrophoresed on a 1%
agarose/formaldehyde gel and transferred to a nitrocellulose filter.
The filter was hybridized at 42 °C overnight in the hybridization
solution with full-length OAT1 cDNA labeled with
[32P]dCTP. The filter was washed finally in 0.1 × SSC, 0.1% SDS at 65 °C.
In situ hybridization was
performed as described elsewhere (7) with some modifications. Briefly,
after perfusion fixation with 4% paraformaldehyde, rat kidney was
excised and postfixed in 4% paraformaldehyde. Five-µm cryostat
sections of rat kidney were used in situ hybridization.
35S-Labeled sense and antisense cRNA were synthesized from
the full-length OAT1 cDNA (in pBlueScript SK RESULTS Using an approach based on homology to rabbit sodium dicarboxylate
transporter (NaDC-1) (5), we isolated rNaDC-1 (rat
sodium-dependent dicarboxylate transporter-1: accession
number for the nucleotide sequence of cDNA: AB001321; DDBJ, EBI,
and GenBankTM nucleotide sequence data bases). When expressed in
X. laevis oocytes, rNaDC-1 mediates
sodium-dependent [14C]glutarate uptake (Fig.
1a). Then we co-injected X. laevis
oocytes with rat kidney poly(A)+ RNA and cRNA of rNaDC-1
and preincubated them with 1 mM glutarate to induce
generation of an outwardly directed dicarboxylate gradient. These
"co-expressed" oocytes exhibited [14C]PAH uptake,
whereas oocytes injected with only rat kidney poly(A)+ RNA
exhibited no detectable [14C]PAH uptake (Fig.
1b). Using a functional expression method together with this
co-expression system, we isolated a 2294-base pair cDNA encoding an
organic anion/dicarboxylate exchanger (OAT1: organic anion transporter
1).
Fig. 1c shows the dependence of OAT1-mediated
[14C]PAH uptake on the intracellular dicarboxylate
(glutarate) concentration. The rate of [14C]PAH uptake by
oocytes via OAT1 is increased by preincubation of the oocytes with 1 mM glutarate. When oocytes co-expressing rNaDC-1 and OAT1
are preincubated with glutarate, they showed a further increase in the
rate of [14C]PAH uptake. This
trans-stimulative effect of glutarate indicates that OAT1 is
an organic anion/dicarboxylate exchanger. As shown in Fig.
1d, replacement of extracellular sodium with choline had no
effect on the rate of [14C]PAH uptake. Because
[14C]PAH (1 mM) uptake via OAT1 was linearly
increased until 5 min under this condition (data not shown), we
performed the kinetic study for 3 min. [14C]PAH uptake
via OAT1 follows Michaelis-Menten kinetics (Fig. 1e), and
the estimated Km value (14.3 ± 2.9 µM: mean ± S.E., n = 3) is similar
to that previously reported for the basolateral organic anion transport
system (80 µM) (2).
OAT1 cDNA consists of 2294 nucleotides, and contains an open
reading frame encoding a 551-amino acid residue protein (Fig. 2a). Kyte-Doolittle hydropathy analysis (8)
of OAT1 predicts 12 putative membrane-spanning domains (Fig.
2b). Four N-glycosylation sites are predicted in
the first hydrophilic loop. There are four putative protein kinase
C-dependent phosphorylation sites in the hydrophilic loop
between sixth and seventh transmembrane domains.
Under high stringency Northern blot analysis of poly(A)+
RNA from rat various tissues, a strong 2.4-kb mRNA band and two
bands corresponding to longer transcripts (3.9 and 4.2 kb) were
detected predominantly in the kidney (Fig.
3a). Upon longer exposure, a faint 2.4-kb
mRNA band was detected in the brain. No hybridization signals were
obtained with mRNA isolated from other tissues. In the kidney,
expression of OAT1 mRNA is strong in the cortex and outer medulla
(cortex > outer medulla) and very weak in the inner medulla.
In situ hybridization of rat kidney coronal sections (Fig.
3b) revealed that OAT1 mRNA is expressed in renal cortex
and outer medulla, especially in the medullary rays of the cortex.
Expression of OAT-1 was not found in the inner medulla. No significant
hybridization signal was detected in control experiments using sense
OAT1 cRNA as a probe (data not shown). This overall pattern of in
situ hybridization suggests that OAT1 is most strongly expressed
in the middle portion of the proximal tubule (S2). This intrarenal
localization is in good agreement with the previous studies, which
demonstrate that the highest PAH transport activity were seen in S2 of
rat proximal tubule (1).
To evaluate the substrate selectivity of OAT1, we examined the levels
of the inhibition of OAT1-mediated [14C]PAH uptake by
various compounds (Fig. 4a).
cis-Inhibitory effects were observed for structurally
unrelated drugs. Cephaloridine ( DISCUSSION The present study describes the isolation of cDNA encoding a
rat renal organic anion transporter, OAT1. The results indicate that
OAT1 possesses the same characteristics as the predicted organic
anion/dicarboxylate exchanger responsible for multispecific organic
anion transport at the basolateral membrane of renal proximal tubules.
The anion exchange model of the renal organic anion transporter has
been proposed within the last decade (1, 4). According to this model,
organic anions are transported into the cell in exchange for
intracellular dicarboxylates, which are subsequently returned into the
cell via sodium-dependent dicarboxylate transporter. In
the present report, we directly demonstrate the validity of this
exchange model. Accumulated glutarate via sodium-dependent dicarboxylate transporter (rNaDC-1) stimulates [14C]PAH
uptake via anion exchanger (OAT1) in Xenopus oocytes. These data explain indirect sodium coupling of renal organic anion
transporter.
Unexpectedly, a search of EBI/GenBankTM data base (January 31, 1997)
revealed that the amino acid sequence of OAT1 shows weak (38%)
identity to organic "cation" transporter (OCT1) (9). The sequence
of OAT1 shows no significant similarity with the members of the
inorganic anion exchanger (AE) family. OCT1 is considered to be a
facilitated transporter, and substrates transported by OCT1 are
different from those of OAT1. Although OAT1 and OCT1 transport
substrates having opposite charges, there is a common feature in which
these two transporters interact with molecules possessing a certain
size of hydrophobic cores. This common aspect may be relevant to the
weak homology between OAT1 and OCT1. Structure function analysis
of OAT1 and OCT1 may provide some clues as to the sites of
proteins that recognize the charge(s) of the substrates.
To date, at least two multispecific transporter families were
identified. One is the ABC superfamily, which includes P-glycoprotein (10), a multidrug resistance associated protein (11, 12) and a
canalicular multispecific organic anion transporter (cMOAT) (13).
P-glycoprotein and multidrug resistance associated protein extrude a
range of anticancer drugs from cells via ATP hydrolysis and confer
multidrug resistance on cancer cells. cMOAT is considered to mediate
hepatobiliary excretion of organic anions; however, its functional
characteristics have not yet been analyzed in detail. Another is the
oatp (organic anion transporting polypeptide) superfamily, which
includes a Na+-independent oatp isolated from rat liver
(14), prostaglandin transporter (15), and kidney-specific oatp (OAT-K1)
(16). oatp mediates transport of bile acids, bromosulfophthalein,
and conjugated and unconjugated steroid hormones (14, 17). We found no
significant sequence similarity between OAT1 and other multispecific
organic anion transporters, including cMOAT, oatp, and prostaglandin
transporter. The structural and transport characteristics of OAT1 are
distinct from those of the members of these two multispecific transporter superfamilies. Further investigation is required for clarification of the individual roles of the members of these three
multispecific transporter superfamilies in drug delivery to and
elimination from the body.
Similar to the case in the kidney, anionic substrates should be
transported in other organs, including liver and brain. In high
stringency Northern blot analysis, however, no signals were detected
except for the kidney and the brain. The liver plays a key role in the
detoxification of many endogenous and exogenous compounds. Lipophilic
xenobiotics are transported into hepatocytes and extensively
biotransformed by P450- and transferase-mediated reactions. As a
result, negatively charged amphiphilic compounds are produced, which
must be secreted from the hepatocytes. Thus, the liver needs
multispecific transporter(s) of anionic compounds (18, 19). cMOAT and
oatp may play certain roles in organic anion transport in the liver;
however, the multiplicity of drug transport has never been fully
explained (20, 21). Recently, organic anion/dicarboxylate exchange
systems in the liver and brain have been identified (22, 23), and a
search of a data base revealed the existence of a liver protein that is
structurally related to OAT1 but whose function has not been determined
(24). Isoform(s) of OAT1 serving as organic anion transporters possibly exist in several organs. Identification of isoforms of OAT1 in other
organs will facilitate the understanding of drug delivery and excretion
system of the body and should provide useful tools for developing drugs
that show desirable distribution in the body.
The original role of OAT1 is presumed to be mediation of transport of
endogenous anionic compounds, such as cyclic nucleotides, prostaglandin
E2, and uric acid. A variety of anionic xenobiotics, such
as drugs and food additives, are newly synthesized and administered to
the body, which must be excreted. Because of its wide substrate selectivity, OAT1 fits the role of a xenobiotic transporter and can
serve as an essential multispecific anionic drug transporter.
Practically, expression of OAT1 in epithelial cell lines is expected to
be useful for the development of in vitro assay systems for
drug elimination and drug/drug interaction studies. Furthermore, such
systems could be used for screening of drugs for nephrotoxicity, which
is one of the most critical points in drug administration to the body.
Many drugs that can cause acute renal failure, such as FOOTNOTES The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB004559. REFERENCES
Volume 272, Number 30,
Issue of July 25, 1997
pp. 18526-18529
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
ZipLox EcoRI arms
(Life Technologies, Inc.). A polymerase chain reaction product
corresponding to nucleotides 1323-1763 of the rabbit sodium
dicarboxylate transporter (NaDC-1) (5) was labeled with
[32P]dCTP. A rat cDNA library was screened with this
probe at low stringency. Hybridization was done overnight in the
hybridization solution at 37 °C, and filters were washed finally at
37 °C in 0.1 × SSC, 0.1% SDS. The hybridization solution
contains 5 × SSC, 3 × Denhardt's solution, 0.2% SDS, 10%
dextran sulfate, 50% formamide, 0.01% Antifoam B, 0.2 mg/ml denatured
salmon sperm DNA, 2.5 mM sodium pyrophosphate, and 25 mM MES, pH 6.5. cDNA inserts in positive ZipLox
phage were recovered in plasmid pZL1 by in vitro excision and further subcloned into pBluescript II SK
(Stratagene)
for sequencing and in vitro transcription.
Fig. 1.
Co-expression and functional characterization
of OAT1 in X. laevis oocytes. a,
[14C]glutarate (170 µM) uptake into
X. laevis oocytes expressed with rNaDC-1 were measured in
the presence (Na+) or absence (choline+) of
sodium. Glutarate uptake via rNaDC-1 is dependent on extracellular sodium. Values represent the mean ± S.E. (n = 5-8 oocytes). b, [14C]PAH (50 µM) uptakes were determined in oocytes injected with rat
kidney poly (A)+ RNA, rNaDC-1 cRNA, and rat kidney
poly(A)+ RNA and rNaDC-1 cRNA. Oocytes were preincubated in
sodium uptake solution containing 1 mM glutarate for 2 h. c, dependence of OAT1-mediated [14C]PAH
uptake on intracellular glutarate concentration. Oocytes are expressed
with OAT1 or OAT1 and rNaDC-1. Fifty µM
[14C]PAH uptakes were determined after preincubation of
the oocytes in the presence or absence of glutarate (1 mM).
d, dependence of OAT1-mediated [14C]PAH uptake
on extracellular Na+. e, concentration
dependence of OAT1-mediated [14C]PAH uptake.
[View Larger Version of this Image (19K GIF file)]
Fig. 4.
Substrate selectivity of OAT1. a,
inhibition of OAT1-mediated [14C]PAH uptake by various
drugs and endogenous substrates. [14C]PAH (2 µM) uptake in the presence of nonradiolabeled test
substrates (2 mM) is expressed as percent of the control
[14C]PAH uptake in the absence of other substrates
(mean ± S.E.; n = 5-8 oocytes). b,
OAT1-mediated uptake of radiolabeled drugs and endogenous substrates.
The amounts of radiolabeled substrates (2 µM
[3H]methotrexate, 1 µM
[3H]cAMP, 1 µM [3H]cGMP, 60 nM [3H]prostaglandin E2, 100 µM [14C]urate, 5 µM
[14C]
-ketoglutarate) taken up by control (open
column) or OAT1-expressed (closed column) oocytes were
measured for 1 h (mean ± S.E.; n = 5-8).
[View Larger Version of this Image (25K GIF file)]
) using
T7 or T3 RNA polymerase after linearization of plasmid DNA with
SpeI or XhoI, respectively. RNA probe was
degraded by partial hydrolysis for 45 min. The cryosections were
hybridized with the probe overnight in the hybridization solution and
washed to a final stringency of 0.1 × SSC at 37 °C for 30 min.
Fig. 2.
a, amino acid sequence of OAT1.
Potential N-glycosylation sites are indicated by
asterisks and protein kinase C phosphorylation sites by
dots. b, Kyte-Doolittle hydropathy analysis of
OAT1 (window of 11). Predicted membrane-spanning regions of
OAT1 are numbered 1-12.
[View Larger Version of this Image (35K GIF file)]
Fig. 3.
Localization of OAT1 mRNA by Northern
blot analysis and in situ hybridization. a,
high-stringency Northern blot analysis of poly(A)+ RNA from
various rat tissues probed with 32P-labeled OAT1 cDNA.
b, In situ hybridization of rat kidney probed with antisense
cRNA transcribed from full-length OAT1 cDNA. Left and
right panels are low- and high-power field micrographs,
respectively.
[View Larger Version of this Image (58K GIF file)]
-lactam antibiotic), nalidixic acid
("old" quinolone), furosemide and ethacrynic acid (diuretics),
indomethacin (nonsteroidal anti-inflammatory drug), probenecid
(uricosuric drug), and valproic acid (antiepileptic drug) potently
inhibited (>85%) OAT1-mediated [14C]PAH uptake by the
oocytes. An antineoplastic drug, methotrexate, moderately inhibited the
[14C]PAH uptake. Endogenous compounds, such as
prostaglandin E2, cyclic AMP, cyclic GMP, and uric acid
also inhibited [14C]PAH uptake. We examined several
radiolabeled compounds in terms of whether they are taken up into
oocytes via OAT1. As Fig. 4b shows,
[3H]methotrexate, [3H]cAMP,
[3H]cGMP, [3H]prostaglandin E2,
[14C]urate and [14C]-ketoglutarate were
transported into the oocytes. No uptake of
[14C]tetraethylammonium and [3H]taurocholic
acid were detected (data not shown).
-lactam
antibiotics, diuretics, and nonsteroidal anti-inflammatory drugs (25),
are transported by the organic anion transport system. One reason why
such drugs are nephrotoxic may be related to their accumulation via
OAT1. Isolation of OAT1, therefore, will facilitate elucidation of the
molecular basis of pharmacokinetics and toxicokinetics.
To whom correspondence should be addressed: Dept. of Pharmacology
and Toxicology, Kyorin University School of Medicine, 6-20-2 Shinkawa,
Mitaka, Tokyo 181, Japan. Tel.: 81-422-47-5511 (ext. 3451); Fax:
81-422-79-1321.
1
The abbreviations used are: PAH,
para-aminohippuric acid; MES, 4-morpholineethanesulfonic acid; kb,
kilobase(s); oatp, organic anion transporting polypeptide.
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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 A. G. Aslamkhan, D. M. Thompson, J. L. Perry, K. Bleasby, N. A. Wolff, S. Barros, D. S. Miller, and J. B. Pritchard The flounder organic anion transporter fOat has sequence, function, and substrate specificity similarity to both mammalian Oat1 and Oat3 Am J Physiol Regulatory Integrative Comp Physiol, December 1, 2006; 291(6): R1773 - R1780. [Abstract] [Full Text] [PDF]
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Y. Hagos, J. Steffgen, A. N. Rizwan, D. Langheit, A. Knoll, G. Burckhardt, and B. C. Burckhardt Functional roles of cationic amino acid residues in the sodium-dicarboxylate cotransporter 3 (NaDC-3) from winter flounder Am J Physiol Renal Physiol, December 1, 2006; 291(6): F1224 - F1231. [Abstract] [Full Text] [PDF]
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W. Xu, K. Tanaka, A.-q. Sun, and G. You Functional Role of the C Terminus of Human Organic Anion Transporter hOAT1 J. Biol. Chem., October 20, 2006; 281(42): 31178 - 31183. [Abstract] [Full Text] [PDF]
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 M. Hiasa, T. Matsumoto, T. Komatsu, and Y. Moriyama Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations Am J Physiol Cell Physiol, October 1, 2006; 291(4): C678 - C686. [Abstract] [Full Text] [PDF]
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G. W. Schnabolk, G. L. Youngblood, and D. H. Sweet Transport of estrone sulfate by the novel organic anion transporter Oat6 (Slc22a20) Am J Physiol Renal Physiol, August 1, 2006; 291(2): F314 - F321. [Abstract] [Full Text] [PDF]
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 K. L. Price, Y. Y. Sautin, D. A. Long, L. Zhang, H. Miyazaki, W. Mu, H. Endou, and R. J. Johnson Human Vascular Smooth Muscle Cells Express a Urate Transporter J. Am. Soc. Nephrol., July 1, 2006; 17(7): 1791 - 1795. [Abstract] [Full Text] [PDF]
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E. K. Jackson, L. C. Zacharia, M. Zhang, D. G. Gillespie, C. Zhu, and R. K. Dubey cAMP-Adenosine Pathway in the Proximal Tubule J. Pharmacol. Exp. Ther., June 1, 2006; 317(3): 1219 - 1229. [Abstract] [Full Text] [PDF]
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N. Bakhiya, M. Stephani, A. Bahn, B. Ugele, A. Seidel, G. Burckhardt, and H. Glatt Uptake of Chemically Reactive, DNA-Damaging Sulfuric Acid Esters into Renal Cells by Human Organic Anion Transporters J. Am. Soc. Nephrol., May 1, 2006; 17(5): 1414 - 1421. [Abstract] [Full Text] [PDF]
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S. A. Eraly, V. Vallon, D. A. Vaughn, J. A. Gangoiti, K. Richter, M. Nagle, J. C. Monte, T. Rieg, D. M. Truong, J. M. Long, et al. Decreased Renal Organic Anion Secretion and Plasma Accumulation of Endogenous Organic Anions in OAT1 Knock-out Mice J. Biol. Chem., February 24, 2006; 281(8): 5072 - 5083. [Abstract] [Full Text] [PDF]
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T. Sekine, H. Miyazaki, and H. Endou Molecular physiology of renal organic anion transporters Am J Physiol Renal Physiol, February 1, 2006; 290(2): F251 - F261. [Abstract] [Full Text] [PDF]
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 O. Q. P. Yin, B. Tomlinson, and M. S. S. Chow Variability in Renal Clearance of Substrates for Renal Transporters in Chinese Subjects J. Clin. Pharmacol., February 1, 2006; 46(2): 157 - 163. [Abstract] [Full Text] [PDF]
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 A. Clarke, L. A. J. Mur, R. M. Darby, and P. Kenton Harpin modulates the accumulation of salicylic acid by Arabidopsis cells via apoplastic alkalization J. Exp. Bot., December 1, 2005; 56(422): 3129 - 3136. [Abstract] [Full Text] [PDF]
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N. Anzai, P. Jutabha, A. Enomoto, H. Yokoyama, H. Nonoguchi, T. Hirata, K. Shiraya, X. He, S. H. Cha, M. Takeda, et al. Functional Characterization of Rat Organic Anion Transporter 5 (Slc22a19) at the Apical Membrane of Renal Proximal Tubules J. Pharmacol. Exp. Ther., November 1, 2005; 315(2): 534 - 544. [Abstract] [Full Text] [PDF]
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S. Soodvilai, S. H. Wright, W. H. Dantzler, and V. Chatsudthipong Involvement of tyrosine kinase and PI3K in the regulation of OAT3-mediated estrone sulfate transport in isolated rabbit renal proximal tubules Am J Physiol Renal Physiol, November 1, 2005; 289(5): F1057 - F1064. [Abstract] [Full Text] [PDF]
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 C. E. Wood, R. Cousins, D. Zhang, and M. Keller-Wood Ontogeny of Expression of Organic Anion Transporters 1 and 3 in Ovine Fetal and Neonatal Kidney Experimental Biology and Medicine, October 1, 2005; 230(9): 668 - 673. [Abstract] [Full Text] [PDF]
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M. Hong, W. Xu, T. Yoshida, K. Tanaka, D. J. Wolff, F. Zhou, M. Inouye, and G. You Human Organic Anion Transporter hOAT1 Forms Homooligomers J. Biol. Chem., September 16, 2005; 280(37): 32285 - 32290. [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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N. Morita, H. Kusuhara, Y. Nozaki, H. Endou, and Y. Sugiyama FUNCTIONAL INVOLVEMENT OF RAT ORGANIC ANION TRANSPORTER 2 (SLC22A7) IN THE HEPATIC UPTAKE OF THE NONSTEROIDAL ANTI-INFLAMMATORY DRUG KETOPROFEN Drug Metab. Dispos., August 1, 2005; 33(8): 1151 - 1157. [Abstract] [Full Text] [PDF]
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K. Bleasby, L. A. Hall, J. L. Perry, H. W. Mohrenweiser, and J. B. Pritchard Functional Consequences of Single Nucleotide Polymorphisms in the Human Organic Anion Transporter hOAT1 (SLC22A6) J. Pharmacol. Exp. Ther., August 1, 2005; 314(2): 923 - 931. [Abstract] [Full Text] [PDF]
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B. M. Schmitt and H. Koepsell Alkali Cation Binding and Permeation in the Rat Organic Cation Transporter rOCT2 J. Biol. Chem., July 1, 2005; 280(26): 24481 - 24490. [Abstract] [Full Text] [PDF]
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B. C. Burckhardt, J. Lorenz, C. Kobbe, and G. Burckhardt Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions Am J Physiol Renal Physiol, April 1, 2005; 288(4): F792 - F799. [Abstract] [Full Text] [PDF]
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L. M. Augustine, R. J. Markelewicz Jr., K. Boekelheide, and N. J. Cherrington XENOBIOTIC AND ENDOBIOTIC TRANSPORTER MRNA EXPRESSION IN THE BLOOD-TESTIS BARRIER Drug Metab. Dispos., January 1, 2005; 33(1): 182 - 189. [Abstract] [Full Text] [PDF]
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P. H.E. Smeets, R. A.M.H. van Aubel, A. C. Wouterse, J. J.M.W. van den Heuvel, and F. G.M. Russel Contribution of Multidrug Resistance Protein 2 (MRP2/ABCC2) to the Renal Excretion of p-aminohippurate (PAH) and Identification of MRP4 (ABCC4) as a Novel PAH Transporter J. Am. Soc. Nephrol., November 1, 2004; 15(11): 2828 - 2835. [Abstract] [Full Text] [PDF]
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X. Zhang, C. E. Groves, A. Bahn, W. M. Barendt, M. D. Prado, M. Rodiger, V. Chatsudthipong, G. Burckhardt, and S. H. Wright Relative contribution of OAT and OCT transporters to organic electrolyte transport in rabbit proximal tubule Am J Physiol Renal Physiol, November 1, 2004; 287(5): F999 - F1010. [Abstract] [Full Text] [PDF]
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S. Soodvilai, V. Chatsudthipong, K. K. Evans, S. H. Wright, and W. H. Dantzler Acute regulation of OAT3-mediated estrone sulfate transport in isolated rabbit renal proximal tubules Am J Physiol Renal Physiol, November 1, 2004; 287(5): F1021 - F1029. [Abstract] [Full Text] [PDF]
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T. Imaoka, H. Kusuhara, S. Adachi-Akahane, M. Hasegawa, N. Morita, H. Endou, and Y. Sugiyama The Renal-Specific Transporter Mediates Facilitative Transport of Organic Anions at the Brush Border Membrane of Mouse Renal Tubules J. Am. Soc. Nephrol., August 1, 2004; 15(8): 2012 - 2022. [Abstract] [Full Text] [PDF]
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G. L. Youngblood and D. H. Sweet Identification and functional assessment of the novel murine organic anion transporter Oat5 (Slc22a19) expressed in kidney Am J Physiol Renal Physiol, August 1, 2004; 287(2): F236 - F244. [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. Aruga, A. M. Pajor, K. Nakamura, L. Liu, O. W. Moe, P. A. Preisig, and R. J. Alpern OKP cells express the Na-dicarboxylate cotransporter NaDC-1 Am J Physiol Cell Physiol, July 1, 2004; 287(1): C64 - C72. [Abstract] [Full Text] [PDF]
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M. Ljubojevic, C. M. Herak-Kramberger, Y. Hagos, A. Bahn, H. Endou, G. Burckhardt, and I. Sabolic Rat renal cortical OAT1 and OAT3 exhibit gender differences determined by both androgen stimulation and estrogen inhibition Am J Physiol Renal Physiol, July 1, 2004; 287(1): F124 - F138. [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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S. C. N. Buist and C. D. Klaassen RAT AND MOUSE DIFFERENCES IN GENDER-PREDOMINANT EXPRESSION OF ORGANIC ANION TRANSPORTER (OAT1-3; SLC22A6-8) mRNA LEVELS Drug Metab. Dispos., June 1, 2004; 32(6): 620 - 625. [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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A. Bahn, C. Ebbinghaus, D. Ebbinghaus, E. G. Ponimaskin, L. Fuzesi, G. Burckhardt, and Y. Hagos EXPRESSION STUDIES AND FUNCTIONAL CHARACTERIZATION OF RENAL HUMAN ORGANIC ANION TRANSPORTER 1 ISOFORMS Drug Metab. Dispos., April 1, 2004; 32(4): 424 - 430. [Abstract] [Full Text] [PDF]
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Y. Nozaki, H. Kusuhara, H. Endou, and Y. Sugiyama Quantitative Evaluation of the Drug-Drug Interactions between Methotrexate and Nonsteroidal Anti-Inflammatory Drugs in the Renal Uptake Process Based on the Contribution of Organic Anion Transporters and Reduced Folate Carrier J. Pharmacol. Exp. Ther., April 1, 2004; 309(1): 226 - 234. [Abstract] [Full Text]
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C. Sauvant, D. Hesse, H. Holzinger, K. K. Evans, W. H. Dantzler, and M. Gekle Action of EGF and PGE2 on basolateral organic anion uptake in rabbit proximal renal tubules and hOAT1 expressed in human kidney epithelial cells Am J Physiol Renal Physiol, April 1, 2004; 286(4): F774 - F783. [Abstract] [Full Text] [PDF]
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S. A. Eraly, K. T. Bush, R. V. Sampogna, V. Bhatnagar, and S. K. Nigam The Molecular Pharmacology of Organic Anion Transporters: from DNA to FDA? Mol. Pharmacol., March 1, 2004; 65(3): 479 - 487. [Abstract] [Full Text] [PDF]
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C. Kneuer, K. U. Honscha, and W. Honscha Sodium-dependent methotrexate carrier-1 is expressed in rat kidney: cloning and functional characterization Am J Physiol Renal Physiol, March 1, 2004; 286(3): F564 - F571. [Abstract] [Full Text]
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M. Hosoyamada, K. Ichida, A. Enomoto, T. Hosoya, and H. Endou Function and Localization of Urate Transporter 1 in Mouse Kidney J. Am. Soc. Nephrol., February 1, 2004; 15(2): 261 - 268. [Abstract] [Full Text] [PDF]
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 N. Shikano, Y. Kanai, K. Kawai, N. Ishikawa, and H. Endou Transport of 99mTc-MAG3 via Rat Renal Organic Anion Transporter 1 J. Nucl. Med., January 1, 2004; 45(1): 80 - 85. [Abstract] [Full Text] [PDF]
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M. D. Blaufox Transport of 99mTc-MAG3 via Rat Renal Organic Anion J. Nucl. Med., January 1, 2004; 45(1): 86 - 88. [Full Text] [PDF]
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C. Sauvant, H. Holzinger, and M. Gekle Short-Term Regulation of Basolateral Organic Anion Uptake in Proximal Tubular Opossum Kidney Cells: Prostaglandin E2 Acts via Receptor-Mediated Activation of Protein Kinase A J. Am. Soc. Nephrol., December 1, 2003; 14(12): 3017 - 3026. [Abstract] [Full Text] [PDF]
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E. Babu, Y. Kanai, A. Chairoungdua, D. K. Kim, Y. Iribe, S. Tangtrongsup, P. Jutabha, Y. Li, N. Ahmed, S. Sakamoto, et al. Identification of a Novel System L Amino Acid Transporter Structurally Distinct from Heterodimeric Amino Acid Transporters J. Biol. Chem., October 31, 2003; 278(44): 43838 - 43845. [Abstract] [Full Text] [PDF]
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 E. Beery, P. Middel, A. Bahn, H. S. Willenberg, Y. Hagos, H. Koepsell, S. R. Bornstein, G. A. Muller, G. Burckhardt, and J. Steffgen Molecular Evidence of Organic Ion Transporters in the Rat Adrenal Cortex with Adrenocorticotropin-Regulated Zonal Expression Endocrinology, October 1, 2003; 144(10): 4519 - 4526. [Abstract] [Full Text] [PDF]
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A. Aslamkhan, Y.-H. Han, R. Walden, D. H. Sweet, and J. B. Pritchard Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells Am J Physiol Renal Physiol, October 1, 2003; 285(4): F775 - F783. [Abstract] [Full Text] [PDF]
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 N. Mizuno, T. Niwa, Y. Yotsumoto, and Y. Sugiyama Impact of Drug Transporter Studies on Drug Discovery and Development Pharmacol. Rev., September 1, 2003; 55(3): 425 - 461. [Abstract] [Full Text] [PDF]
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 G.-H. Kim, K. Y. Na, S.-Y. Kim, K. W. Joo, Y. K. Oh, S.-W. Chae, H. Endou, and J. S. Han Up-regulation of organic anion transporter 1 protein is induced by chronic furosemide or hydrochlorothiazide infusion in rat kidney Nephrol. Dial. Transplant., August 1, 2003; 18(8): 1505 - 1511. [Abstract] [Full Text] [PDF]
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G.-H. Kim, K. Y. Na, S.-Y. Kim, K. W. Joo, Y. K. Oh, S.-W. Chae, H. Endou, and J. S. Han Up-regulation of organic anion transporter 1 protein is induced by chronic furosemide or hydrochlorothiazide infusion in rat kidney Nephrol. Dial. Transplant., August 1, 2003; 18(88): 1505 - 1511. [Abstract] [Full Text]
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P. Jutabha, Y. Kanai, M. Hosoyamada, A. Chairoungdua, D. K. Kim, Y. Iribe, E. Babu, J. Y. Kim, N. Anzai, V. Chatsudthipong, et al. Identification of a Novel Voltage-driven Organic Anion Transporter Present at Apical Membrane of Renal Proximal Tubule J. Biol. Chem., July 18, 2003; 278(30): 27930 - 27938. [Abstract] [Full Text] [PDF]
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R. Kikuchi, H. Kusuhara, D. Sugiyama, and Y. Sugiyama Contribution of Organic Anion Transporter 3 (Slc22a8) to the Elimination of p-Aminohippuric Acid and Benzylpenicillin across the Blood-Brain Barrier J. Pharmacol. Exp. Ther., July 1, 2003; 306(1): 51 - 58. [Abstract] [Full Text] [PDF]
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M. Hasegawa, H. Kusuhara, H. Endou, and Y. Sugiyama Contribution of Organic Anion Transporters to the Renal Uptake of Anionic Compounds and Nucleoside Derivatives in Rat J. Pharmacol. Exp. Ther., June 1, 2003; 305(3): 1087 - 1097. [Abstract] [Full Text] [PDF]
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S. C. N. Buist, N. J. Cherrington, and C. D. Klaassen Endocrine Regulation of Rat Organic Anion Transporters Drug Metab. Dispos., May 1, 2003; 31(5): 559 - 564. [Abstract] [Full Text] [PDF]
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 F. Van Bambeke, J.-M. Michot, and P. M. Tulkens Antibiotic efflux pumps in eukaryotic cells: occurrence and impact on antibiotic cellular pharmacokinetics, pharmacodynamics and toxicodynamics J. Antimicrob. Chemother., May 1, 2003; 51(5): 1067 - 1077. [Full Text] [PDF]
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D. H. Sweet, L. M. S. Chan, R. Walden, X.-P. Yang, D. S. Miller, and J. B. Pritchard Organic anion transporter 3 (Slc22a8) is a dicarboxylate exchanger indirectly coupled to the Na+ gradient Am J Physiol Renal Physiol, April 1, 2003; 284(4): F763 - F769. [Abstract] [Full Text] [PDF]
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S. Ohtsuki, T. Takizawa, H. Takanaga, N. Terasaki, T. Kitazawa, M. Sasaki, T. Abe, K.-i. Hosoya, and T. Terasaki In Vitro Study of the Functional Expression of Organic Anion Transporting Polypeptide 3 at Rat Choroid Plexus Epithelial Cells and Its Involvement in the Cerebrospinal Fluid-to-Blood Transport of Estrone-3-Sulfate Mol. Pharmacol., March 1, 2003; 63(3): 532 - 537. [Abstract] [Full Text] [PDF]
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A. G. Aslamkhan, Y.-H. Han, X.-P. Yang, R. K. Zalups, and J. B. Pritchard Human Renal Organic Anion Transporter 1-Dependent Uptake and Toxicity of Mercuric-Thiol Conjugates in Madin-Darby Canine Kidney Cells Mol. Pharmacol., March 1, 2003; 63(3): 590 - 596. [Abstract] [Full Text] [PDF]
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C. E. Groves, L. Munoz, A. Bahn, G. Burckhardt, and S. H. Wright Interaction of Cysteine Conjugates with Human and Rabbit Organic Anion Transporter 1 J. Pharmacol. Exp. Ther., February 1, 2003; 304(2): 560 - 566. [Abstract] [Full Text] [PDF]
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 P. T. Ronaldson and R. Bendayan Renal Drug Transport and Drug-Drug Interactions Journal of Pharmacy Practice, December 1, 2002; 15(6): 490 - 503. [Abstract] [PDF]
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Y. Tsutsumi, T. Deguchi, M. Takano, A. Takadate, W. E. Lindup, and M. Otagiri Renal Disposition of a Furan Dicarboxylic Acid and Other Uremic Toxins in the Rat J. Pharmacol. Exp. Ther., November 1, 2002; 303(2): 880 - 887. [Abstract] [Full Text] [PDF]
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A. Bahn, M. Knabe, Y. Hagos, M. Rodiger, S. Godehardt, D. S. Graber-Neufeld, K. K. Evans, G. Burckhardt, and S. H. Wright Interaction of the Metal Chelator 2,3-Dimercapto-1-propanesulfonate with the Rabbit Multispecific Organic Anion Transporter 1 (rbOAT1) Mol. Pharmacol., November 1, 2002; 62(5): 1128 - 1136. [Abstract] [Full Text] [PDF]
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 F. Knauf, B. Rogina, Z. Jiang, P. S. Aronson, and S. L. Helfand Functional characterization and immunolocalization of the transporter encoded by the life-extending gene Indy PNAS, October 29, 2002; 99(22): 14315 - 14319. [Abstract] [Full Text] [PDF]
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A. S. Koh, T. A. Simmons-Willis, J. B. Pritchard, S. M. Grassl, and N. Ballatori Identification of a Mechanism by Which the Methylmercury Antidotes N-Acetylcysteine and Dimercaptopropanesulfonate Enhance Urinary Metal Excretion: Transport by the Renal Organic Anion Transporter-1 Mol. Pharmacol., October 1, 2002; 62(4): 921 - 926. [Abstract] [Full Text] [PDF]
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 F. Pizzagalli, B. Hagenbuch, B. Stieger, U. Klenk, G. Folkers, and P. J. Meier Identification of a Novel Human Organic Anion Transporting Polypeptide as a High Affinity Thyroxine Transporter Mol. Endocrinol., October 1, 2002; 16(10): 2283 - 2296. [Abstract] [Full Text] [PDF]
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S. M. Grassl Urate/alpha -ketoglutarate exchange in avian basolateral membrane vesicles Am J Physiol Cell Physiol, October 1, 2002; 283(4): C1144 - C1154. [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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Y. Kato, K. Kuge, H. Kusuhara, P. J. Meier, and Y. Sugiyama Gender Difference in the Urinary Excretion of Organic Anions in Rats J. Pharmacol. Exp. Ther., August 1, 2002; 302(2): 483 - 489. [Abstract] [Full Text] [PDF]
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M. Takeda, S. Khamdang, S. Narikawa, H. Kimura, M. Hosoyamada, S. H. Cha, T. Sekine, and H. Endou Characterization of Methotrexate Transport and Its Drug Interactions with Human Organic Anion Transporters J. Pharmacol. Exp. Ther., August 1, 2002; 302(2): 666 - 671. [Abstract] [Full Text] [PDF]
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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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 J. Alcorn and P. J. McNamara Acyclovir, Ganciclovir, and Zidovudine Transfer into Rat Milk Antimicrob. Agents Chemother., June 1, 2002; 46(6): 1831 - 1836. [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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Y. L. Zhao, X. B. Cen, M. Ito, K. Yokoyama, K. Takagi, K. Kitaichi, M. Nadai, M. Ohta, K. Takagi, and T. Hasegawa Shiga-Like Toxin II Derived from Escherichia coli O157:H7 Modifies Renal Handling of Levofloxacin in Rats Antimicrob. Agents Chemother., May 1, 2002; 46(5): 1522 - 1528. [Abstract] [Full Text] [PDF]
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Y. Nagata, H. Kusuhara, H. Endou, and Y. Sugiyama Expression and Functional Characterization of Rat Organic Anion Transporter 3 (rOat3) in the Choroid Plexus Mol. Pharmacol., May 1, 2002; 61(5): 982 - 988. [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. Hasegawa, H. Kusuhara, D. Sugiyama, K. Ito, S. Ueda, H. Endou, and Y. Sugiyama Functional Involvement of Rat Organic Anion Transporter 3 (rOat3; Slc22a8) in the Renal Uptake of Organic Anions J. Pharmacol. Exp. Ther., March 1, 2002; 300(3): 746 - 753. [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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R. A. M. H. van Aubel, P. H. E. Smeets, J. G. P. Peters, R. J. M. Bindels, and F. G. M. Russel The MRP4/ABCC4 Gene Encodes a Novel Apical Organic Anion Transporter in Human Kidney Proximal Tubules: Putative Efflux Pump for Urinary cAMP and cGMP J. Am. Soc. Nephrol., March 1, 2002; 13(3): 595 - 603. [Abstract] [Full Text] [PDF]
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C. S. Wilcox New Insights into Diuretic Use in Patients with Chronic Renal Disease J. Am. Soc. Nephrol., March 1, 2002; 13(3): 798 - 805. [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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