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J Biol Chem, Vol. 274, Issue 24, 17159-17163, June 11, 1999
From the We have isolated a novel liver-specific organic
anion transporter, LST-1, that is expressed exclusively in the human,
rat, and mouse liver. LST-1 is a new gene family located between the organic anion transporter family and prostaglandin transporter. LST-1
transports taurocholate (Km = 13.6 µM) in a sodium-independent manner. LST-1 also shows
broad substrate specificity. It transports conjugated steroids
(dehydroepiandrosterone sulfate, estradiol-17 LST-1 is probably the most important transporter in human liver
for clearance of bile acids and organic anions because hepatic levels
of another organic anion transporter, OATP, is very low. This is also
the first report of the human molecule that transports thyroid hormones.
One of the major function of the liver is the removal of various
endogenous and exogenous compounds from the circulation (1, 2). This
clearance process involves basolateral membrane transport systems that
mediate the hepatocellular uptake of bile acids, organic anions, and
organic cations (3, 4). One well studied class of substrates are the
bile acids. The uptake of taurocholate is mainly mediated by the
Na+/taurocholate cotransporting polypeptide (ntcp) in a
Na+-dependent manner (5). The uptake of other
bile acids (e.g. cholate) occurs predominantly via a
Na+-independent mechanism (2, 4). Some amount of
taurocholate is also transported by the Na+-independent
mechanism. This Na+-independent carrier system further
shows a broad substrate specificity transporting conjugated steroids,
cardiac glycosides, and other xenobiotics (4).
Initially, the organic anion transporter
(oatp)1 family (oatp1, oatp2,
oatp3) was considered to represent the Na+-independent
transporting mechanisms in the liver (6-8). Subsequently, a human
cDNA, termed OATP, was isolated (9). However, significant differences were found between human OATP and rat oatp family. First,
although the substrate specificities were qualitatively similar,
significant differences were found between human OATP- and rat oatp
family-mediated initial uptake rates and apparent Km
values (10, 11). Second, Northern blot analysis of the human OATP
showed considerably high expression in the brain, a pattern that is
different from any of the oatp family members. These findings strongly
suggest the existence of a different group of organic anion
transporters in human liver.
Here we report the isolation of a novel human organic anion
transporter, termed LST-1, which is expressed exclusively in the liver.
When expressed in Xenopus oocytes, many of the functional characteristics of LST-1 were identical to the multispecific
transporting mechanisms of human liver. These results suggest that
LST-1 is the predominant clearance mechanism of several endogenous and exogenous substrates in human liver.
Isolation of the Human LST-1 cDNA--
The
GenBankTM data base dbEST was searched with all known
mammalian oatp family and the prostaglandin (PG) transporters (6-9, 12-14) using the TBLASTN algorithm. As a result, three independent clones that have weak to moderate similarity to both the oatp family
and the PG transporter were identified (GenBankTM accession
numbers H62893, T73863, and R29414). Polymerase chain reaction primers
were designed from each EST sequence, and the amplified products were
subcloned into pBluescript. A human liver cDNA library was
constructed by the Homology Analysis--
Multiple sequence alignments of amino
acid sequences and phylogenetic tree construction were carried out
using Clustal W (16). The phylogenetic trees were described by TreeView
(17).
Northern Blot Analysis--
Multiple tissue
NorthernTM blots containing 2 µg of human, rat, and mouse
mRNAs were purchased (CLONTECH). Filters were
hybridized with the 32P-labeled fragment of the
3'-untranslated region of pH1 (EcoRI-EcoRI, 838 base pairs) for human and with full-length cDNA of pH1 for rat and
mouse Northern blot analyses. For human OATP analysis, the
3'-untranslated region (HindIII-EcoRI, 830 base
pairs) was used to discriminate the cross-hybridization. In human
Northern blot analyses, filters were hybridized in a buffer containing 50% formamide, 5 × SSC (1× SSC = 0.15 M NaCl
and 0.015 M sodium citrate), 5 × Denhardt's
solution, and 1% SDS at 42 °C overnight, washed in 0.2× SSC, 1%
SDS at 65 °C for 1 h, and exposed to a film at Expression of LST-1 in Xenopus Oocytes--
The isolated clone
pH1 was linearized, and the capped cRNA was transcribed in
vitro with T7 RNA polymerase (Stratagene). Xenopus laevis oocytes were prepared as described previously (7). Briefly, defolliculated oocytes were microinjected with 10 ng of transcribed cRNA and were cultured for 72 h in a modified Barth's medium (88 mM NaCl, 1 mM KCl, 2.4 mM
NaHCO3, 0.3 mM
Ca(NO3)2, 0.41 mM
CaCl2, 0.82 mM MgSO4, 15 mM Hepes, pH 7.6) at 18 °C. Uptake of radiolabeled chemicals was measured in a medium containing 100 mM NaCl,
2 mM KCl, 1 mM CaCl2, 1 mM MgCl2, 10 mM Hepes, pH 7.5. Oocytes were incubated in 100 µl of the same medium containing
radiolabeled substrate at room temperature. Uptake was terminated by
the addition of 3 ml of ice-cold uptake buffer, and the oocytes were
washed 3 times. The water-injected oocytes were used as controls. The statistical significance was tested by unpaired t test.
Isolation and Structural Analysis of LST-1--
The isolated
cDNA encoding human LST-1 consisted of 691 amino acids
(Mr 78.912), and the hydrophobicity analysis
(18) suggested the presence of 12 transmembrane domains (Fig.
1a). There are seven putative
N-glycosylation sites in the predicted extracellular loops,
one potential phosphorylation site for cAMP-dependent
protein kinase, and one potential phosphorylation site for protein
kinase C in the third cytosolic hydrophilic loop (19, 20). The sequence homology analysis revealed a moderate sequence similarity to both the
oatp family and the PG transporter, which is moderately related to the
oatp family. The overall amino acid sequence identities were 42.2% for
human OATP (9), 42.9% for rat oatp1 (6), 43.6% for rat oatp2 (7, 8),
43.9% for rat oatp3(7), 42.0% for rat OAT-K1 (12), 33.0% for rat PG
transporter (13), and 34.9% for human PG transporter (14). The
phylogenetic tree analysis by using the neighbor-joining and the
maximum-likelihood methods showed that LST-1 is positioned between the
oatp family and the PG transporter (Fig. 1b).
Northern Blot Analyses--
Northern blot analysis of the LST-1
showed two bands (one major band at 3.0 kilonucleotides and one minor
band at 4.8 kilonucleotides) exclusively in the liver (Fig.
2a). No significant expression was detectable in any of the other tissues examined. The rat and mouse
Northern blot analyses with the human LST-1 probe also detected a
single band only in the liver (Fig. 2, b and c),
suggesting that LST-1 and the rat and mouse homologues are
liver-specific.
Because Kullak-Ublick et al. (9) reported the presence of
human OATP transcript in the liver, Northern blot analysis for the
human OATP was further performed. The signals were detected only in the
brain at 8.0 and 2.8 kilonucleotides (Fig. 2d), indicating that the expression of OATP is negligible in human liver.
To confirm this, we re-screened the human liver cDNA library
filters that were used for isolating LST-1 with the human OATP probe.
All the signals detected with the human OATP probe were completely
overlapped with the positive signals detected by the LST-1 probe. To
further characterize the OATP-positive signals, we designed the
polymerase chain reaction primers at the 3'-noncoding region of human
OATP, and amplification was performed. Among 52 LST-1-positive signals,
no polymerase chain reaction positive band was detected. Because the
human liver library used was not amplified, each positive signal was
independent and tentatively represented the population of the original
human liver mRNA. These data revealed that LST-1 is exclusively
expressed in the human, rat, and mouse liver, whereas OATP is expressed
in the human brain.
Pharmacological Characterizations--
Based on the structural
similarities observed between the oatp family and the PG transporter,
we assumed that LST-1 can transport both organic anions
(i.e. taurocholate and conjugated steroids) and eicosanoids.
In the oocytes injected with LST-1 cRNA, [3H]taurocholate
was transported according to the saturation kinetics with an apparent
Km of 13.6 ± 5.6 µM (Fig.
3). This LST-1-mediated [3H]taurocholate uptake was not inhibited by replacing
the extracellular Na+ with choline (p > 0.1), reflecting the Na+-independent fraction in human
liver. The LST-1-expressing oocytes also significantly transported
conjugated steroids dehydroepiandrosterone sulfate,
estradiol-17
Moreover, the oocytes injected with LST-1 cRNA transported PG
E2, thromboxane B2, leukotriene C4,
and leukotriene E4 (Table I). On the other hand, no
arachidonic acid uptake was detected.
We have previously reported that oatp2 and oatp3 transport both
thyroxine (T4) and triiodothyronine (T3) (7). The LST-1 cRNA-injected
oocytes significantly transported [125I]T4 and
[125I]T3 in a saturable manner. The apparent
Km values for [125I]T4 and
[125I]T3 were 3.0 ± 1.3 µM and
2.7 ± 1.1 µM, respectively (Fig.
4, a and b). These
LST-1-mediated T4 and T3 uptakes were also Na+-independent
(data not shown). Thus, these data demonstrated that LST-1 encodes a
human liver-specific multifunctional transporter that transports
taurocholate, conjugated steroids, eicosanoids, and thyroid hormones in
accordance with the structural characteristics.
The present study describes the isolation of a new gene family
encoding human liver-specific organic anion transporter, LST-1. LST-1
appears to be an essential transporter in human liver for the following reasons.
LST-1 Is a Member of a Novel Super Gene Family Expressed in the
Liver--
A comparison of the LST-1 amino acid sequence to that of
human OATP and PG transporter revealed that, although the transmembrane regions and its surrounded area are moderately conserved, the N- and
C-terminal cytoplasmic regions are completely different (Fig.
1a). The phylogenetic tree analysis also revealed that LST-1 is branched between human OATP and PG transporter (Fig. 1b).
Therefore, we propose LST-1 as a novel gene family.
Northern blot analysis showed that the LST-1 mRNA is exclusively
expressed in human liver (Fig. 2a). The rat and mouse
Northern blot analyses with LST-1 as a probe also detected a single
band only in the liver (Fig. 2, b and c). In rat,
four oatp family members have been reported (6-8, 12). Among these,
oatp1, oatp2, and oatp3 are expressed in the liver, but their
expressions are not liver-specific. The PG transporter is also widely
distributed (13, 14). These data strongly suggest that human LST-1 is not the counterpart of the oatp family or the PG transporter, but it
belongs to another new super gene family exclusively expressed in the liver.
Human Organic Anion Transporters Distribute in a Organ-specific
Manner--
Northern blot analysis using the 3'-noncoding region of
human OATP detected signals only in the brain (Fig. 2d).
Although a previous study showed a rather broad distribution (9), this discrepancy is probably because of the cross-hybridization of the
less-specific probe. Thus, in human, OATP appears not to be the
principal organic anion transporter in the liver but to be the main
transporter in the brain. These data further suggest that, in human,
the organic anion transporters are assumed to be expressed in an
organ-specific manner.
Pharmacological Properties Are Similar to Human
Liver--
Functional analysis for LST-1 revealed that LST-1
transported taurocholate (Km, 13.6 µM)
in a Na+-independent manner (Fig. 3). This value is
approximately two to four times lower than those of the oatp family and
human OATP (7-9, 21), whereas it is comparable with that of the human hepatocyte when extracellular Na+ was removed (22). These
data suggest that LST-1 is the molecule representing the
Na+-independent bile acid uptake in human liver.
Furthermore, in the liver, interspecies differences of taurocholate
uptake between rat and human liver have been reported (4, 22). These
functional differences can be explained by the difference in the major
organic anion transporter molecule in rat and human liver: LST-1 in
human and oatp family members in rat.
The oatp family transports bile acids but does not transport
eicosanoids (PG E2, PG
F2
Our previous data revealed that both rat oatp2 and oatp3 transport
thyroid hormones (7). LST-1 cRNA-injected oocytes transported T4 and T3
(Fig. 4, a and b). In human liver,
carrier-mediated transport of thyroid hormone has been predicted (25,
26). Thus, this is the first report identifying a human molecule that transports thyroid hormone, and these findings should be a tool for
understanding the delivery of thyroid hormone to tissue in human
(27).
Taken together, it is concluded that in human, LST-1 should be the
essential molecule for transporting bile acids and organic anions in
the liver, reflecting the multispecificity of the
Na+-independent clearance mechanism in vivo.
So far, in human, the Na+-independent fraction of bile acid
and organic anion transport in the liver have been discussed by using
human OATP as a responsible molecule. However, the present study
reveals that LST-1 may actually be the essential molecule in human
liver, and the hepatic expression of human OATP is negligible. Further
studies of LST-1 should provide new insight into bile acid formation
and greater understanding of the pathogenesis of the diseases such as
cholestasis (28), hyperbilirubinemia (29), and thyroid hormone
resistance (Refetoff's syndrome) (30). Our findings may also be a new
guide to develop the liver-specific drug delivery system and
liver-specific chemotherapy (31).
We thank to Dr. Kazuo Nunoki for discussions.
*
This work was supported in part by research grants from the
Ministry of Education, Science, and Culture of Japan, the Yamanouchi Foundation for Research on Metabolic Disorders, the Nishimiya Foundation, the Tokyo Biochemical Research Foundation, the Japan Research Foundation for Clinical Pharmacology, and the Inamori Foundation.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) AF060500.
§
These authors contributed equally to this study.
¶
To whom correspondence should be addressed: Dept. of
Neurophysiology, Tohoku University School of Medicine, 2-1 Seiryo-cho, Aoba-ku, Sendai, 980-8575, Japan. Tel: +81-22-717-8153; Fax:
+81-22-717-8154; E-mail: takaabe{at}mail.cc.tohoku.ac.jp.
The abbreviations used are:
ntcp, Na+/taurocholate cotransporting polypeptide;
oatp, organic
anion-transporting polypeptide;
PG, prostaglandin;
T4, thyroxine;
T3, 3,5,3'- triiodo-L-thyronine.
Identification of a Novel Gene Family Encoding Human
Liver-specific Organic Anion Transporter LST-1*
§¶,§
,,,,,,, and
Department of Neurophysiology, 1st
Department of Surgery, Department of
Pediatrics,
ABSTRACT
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
-glucuronide, and
estrone-3-sulfate), eicosanoids (prostaglandin E2,
thromboxane B2, leukotriene C4, leukotriene
E4), and thyroid hormones (thyroxine, Km = 3.0 µM and triiodothyronine,
Km = 2.7 µM), reflecting hepatic multispecificity.
INTRODUCTION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
MATERIALS AND METHODS
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
ZAPII vector (Stratagene) (15). 5 × 105 independent clones were screened with each EST clone
under high stringency. As a result, the signals hybridized with each
EST clone were identical with each other. In a series of screenings, 52 hybridization-positive clones were isolated, and the clone that had the
largest insert (pH1) was chosen for further analysis. The sequences
were determined using ABI PrismTM 377 DNA sequencer
(Perkin-Elmer).
80 °C for
3 h (human LST-1) or 3 days (human OATP). For rat and mouse
Northern blot analyses, filters were hybridized in a buffer containing
25% formamide, 5× SSC, 5× Denhardt's solution, and 1% SDS at
42 °C overnight, washed in 2× SSC, 1% SDS at 55 °C for 1 h, and exposed to a film at 80 °C for overnight (mouse) or 4 days
(rat). The human -actin probe was used to monitor the quality of the mRNAs.
RESULTS
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ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
View larger version (46K):
[in a new window]
Fig. 1.
a, alignment of the deduced amino acid
sequence of LST-1 (GenBankTM accession number AF060500),
human OATP, and human PG transporter (PGT). The sequences
are aligned with single-letter notation by inserting gaps (-) to
achieve the maximum homology. The 12 putative transmembrane segments (I
to XII) were assigned on the basis of hydrophobicity analysis. Sequence
motifs for potential N-glycosylation sites
(triangles) and possible phosphorylation sites
(asterisks) are indicated. b, phylogenetic
relationship between LST-1, the oatp family, and PG transporter. The
phylogenetic tree was constructed using CLUSTAL W and TreeView
(http://taxonomy.zoology.gla.ac.uk/rod/treeview.html) using ungapped
regions and distance correction. Branch lengths are drawn to
scale.
View larger version (38K):
[in a new window]
Fig. 2.
Northern blot analysis of the human LST-1
mRNA. a, human Multiple Tissue
NorthernTM blots (2 µg of Poly(A)+ RNAs) were
hybridized with the 3'-noncoding region (the 838 base pairs
EcoRI-EcoRI fragment) of the human LST-1. Rat
(b) and mouse (c) Multiple Tissue
NorthernTM blots (CLONTECH) were
hybridized with the full length of the human LST-1 under low
stringency. d, human Multiple Tissue NorthernTM
blots were hybridized with the HindIII-EcoRI (830 base pairs) fragment of human OATP, which has less than 45% homology
with both human LST-1 and human PG transporter. In a and
d, hybridization of each blot with -actin has been
further performed to ensure the quality of the mRNA. The size
marker (kilonucleotides) used was the RNA ladder.
-glucuronide, and estrone-3-sulfate (Table I). In contrast, unconjugated steroids
such as aldosterone, estradiol, and testosterone were not
transported.
View larger version (11K):
[in a new window]
Fig. 3.
Transport of taurocholate in LST-1-expressing
oocytes. The transport rates of [3H]taurocholate for
the LST-1 cRNA-injected oocytes were measured (20 min). From all uptake
values, nonspecific uptake into water-injected oocytes was subtracted.
A representative of three experiments is shown. The values indicated
are means ±S.E. of 5~9 oocyte determinations.
Uptake of 3H-labeled various compounds by LST-1-expressing
oocytes
View larger version (9K):
[in a new window]
Fig. 4.
Transport of thyroid hormones in
LST-1-expressing oocytes. The transport rates of T4 (a)
and T3 (b) for the LST-1 cRNA-injected oocytes were measured
(20 min). A representative of three experiments is shown. The values
indicated are means ±S.E. of 8~15 oocyte determinations.
DISCUSSION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
, and thromboxane
B2) (21, 23). On the other hand, the PG transporter
transports PG E1, PG E2, PG
F2, and thromboxane B2 but does
not transport taurocholate (13, 14, 24). Our study shows that the
substrate specificities of the LST-1 are intermediate; it transports
taurocholate, conjugated steroids (dehydroepiandrosterone sulfate,
estradiol-17-glucuronide, and estrone-3-sulfate) and eicosanoids (PG
E2, thromboxane B2, leukotriene C4,
and leukotriene E4) (Figs. 3 and 4; Table I). It is
speculated that this wide substrate specificity would be explained by
the structure of the LST-1, because LST-1 is structurally located
intermediately between the oatp family and the PG transporter.
ACKNOWLEDGEMENT
FOOTNOTES
ABBREVIATIONS
REFERENCES
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ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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H. Tahara, H. Kusuhara, K. Maeda, H. Koepsell, E. Fuse, and Y. Sugiyama INHIBITION OF OAT3-MEDIATED RENAL UPTAKE AS A MECHANISM FOR DRUG-DRUG INTERACTION BETWEEN FEXOFENADINE AND PROBENECID Drug Metab. Dispos., May 1, 2006; 34(5): 743 - 747. [Abstract] [Full Text] [PDF]
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R. Nakagomi-Hagihara, D. Nakai, K. Kawai, Y. Yoshigae, T. Tokui, T. Abe, and T. Ikeda OATP1B1, OATP1B3, AND MRP2 ARE INVOLVED IN HEPATOBILIARY TRANSPORT OF OLMESARTAN, A NOVEL ANGIOTENSIN II BLOCKER Drug Metab. Dispos., May 1, 2006; 34(5): 862 - 869. [Abstract] [Full Text] [PDF]
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K. Letschert, H. Faulstich, D. Keller, and D. Keppler Molecular Characterization and Inhibition of Amanitin Uptake into Human Hepatocytes Toxicol. Sci., May 1, 2006; 91(1): 140 - 149. [Abstract] [Full Text] [PDF]
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X. Wang, A. W. Wolkoff, and M. E. Morris FLAVONOIDS AS A NOVEL CLASS OF HUMAN ORGANIC ANION-TRANSPORTING POLYPEPTIDE OATP1B1 (OATP-C) MODULATORS Drug Metab. Dispos., November 1, 2005; 33(11): 1666 - 1672. [Abstract] [Full Text] [PDF]
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K. Kopplow, K. Letschert, J. Konig, B. Walter, and D. Keppler Human Hepatobiliary Transport of Organic Anions Analyzed by Quadruple-Transfected Cells Mol. Pharmacol., October 1, 2005; 68(4): 1031 - 1038. [Abstract] [Full Text] [PDF]
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S. Matsushima, K. Maeda, C. Kondo, M. Hirano, M. Sasaki, H. Suzuki, and Y. Sugiyama Identification of the Hepatic Efflux Transporters of Organic Anions Using Double-Transfected Madin-Darby Canine Kidney II Cells Expressing Human Organic Anion-Transporting Polypeptide 1B1 (OATP1B1)/Multidrug Resistance-Associated Protein 2, OATP1B1/Multidrug Resistance 1, and OATP1B1/Breast Cancer Resistance Protein J. Pharmacol. Exp. Ther., September 1, 2005; 314(3): 1059 - 1067. [Abstract] [Full Text] [PDF]
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C. Chang, K. S. Pang, P. W. Swaan, and S. Ekins Comparative Pharmacophore Modeling of Organic Anion Transporting Polypeptides: A Meta-Analysis of Rat Oatp1a1 and Human OATP1B1 J. Pharmacol. Exp. Ther., August 1, 2005; 314(2): 533 - 541. [Abstract] [Full Text] [PDF]
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X. Cheng, J. Maher, C. Chen, and C. D. Klaassen TISSUE DISTRIBUTION AND ONTOGENY OF MOUSE ORGANIC ANION TRANSPORTING POLYPEPTIDES (OATPS) Drug Metab. Dispos., July 1, 2005; 33(7): 1062 - 1073. [Abstract] [Full Text] [PDF]
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 P. M Beringer and R. L Slaughter Transporters and Their Impact on Drug Disposition Ann. Pharmacother., June 1, 2005; 39(6): 1097 - 1108. [Abstract] [Full Text] [PDF]
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H. Satoh, F. Yamashita, M. Tsujimoto, H. Murakami, N. Koyabu, H. Ohtani, and Y. Sawada CITRUS JUICES INHIBIT THE FUNCTION OF HUMAN ORGANIC ANION-TRANSPORTING POLYPEPTIDE OATP-B Drug Metab. Dispos., April 1, 2005; 33(4): 518 - 523. [Abstract] [Full Text] [PDF]
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M. Sasaki, H. Suzuki, J. Aoki, K. Ito, P. J. Meier, and Y. Sugiyama Prediction of in Vivo Biliary Clearance from the in Vitro Transcellular Transport of Organic Anions across a Double-Transfected Madin-Darby Canine Kidney II Monolayer Expressing Both Rat Organic Anion Transporting Polypeptide 4 and Multidrug Resistance Associated Protein 2 Mol. Pharmacol., September 1, 2004; 66(3): 450 - 459. [Abstract] [Full Text] [PDF]
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 T. Mikkaichi, T. Suzuki, T. Onogawa, M. Tanemoto, H. Mizutamari, M. Okada, T. Chaki, S. Masuda, T. Tokui, N. Eto, et al. Isolation and characterization of a digoxin transporter and its rat homologue expressed in the kidney PNAS, March 9, 2004; 101(10): 3569 - 3574. [Abstract] [Full Text] [PDF]
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N. Mano, T. Goto, M. Uchida, K. Nishimura, M. Ando, N. Kobayashi, and J. Goto Presence of protein-bound unconjugated bile acids in the cytoplasmic fraction of rat brain J. Lipid Res., February 1, 2004; 45(2): 295 - 300. [Abstract] [Full Text] [PDF]
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 A. Ito, K. Yamaguchi, H. Tomita, T. Suzuki, T. Onogawa, T. Sato, H. Mizutamari, T. Mikkaichi, T. Nishio, T. Suzuki, et al. Distribution of Rat Organic Anion Transporting Polypeptide-E (oatp-E) in the Rat Eye Invest. Ophthalmol. Vis. Sci., November 1, 2003; 44(11): 4877 - 4884. [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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 F. Pizzagalli, Z. Varga, R. D. Huber, G. Folkers, P. J. Meier, and M. V. St-Pierre Identification of Steroid Sulfate Transport Processes in the Human Mammary Gland J. Clin. Endocrinol. Metab., August 1, 2003; 88(8): 3902 - 3912. [Abstract] [Full Text] [PDF]
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 T. Suzuki, T. Onogawa, N. Asano, H. Mizutamari, T. Mikkaichi, M. Tanemoto, M. Abe, F. Satoh, M. Unno, K. Nunoki, et al. Identification and Characterization of Novel Rat and Human Gonad-Specific Organic Anion Transporters Mol. Endocrinol., July 1, 2003; 17(7): 1203 - 1215. [Abstract] [Full Text] [PDF]
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H. H. A. G. M. van der Putten, E. C. H. Friesema, N. A. Abumrad, M. E. Everts, and T. J. Visser Thyroid Hormone Transport by the Rat Fatty Acid Translocase Endocrinology, April 1, 2003; 144(4): 1315 - 1323. [Abstract] [Full Text] [PDF]
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 M. Trauner and J. L. Boyer Bile Salt Transporters: Molecular Characterization, Function, and Regulation Physiol Rev, April 1, 2003; 83(2): 633 - 671. [Abstract] [Full Text] [PDF]
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Y. Shitara, T. Itoh, H. Sato, A. P. Li, and Y. Sugiyama Inhibition of Transporter-Mediated Hepatic Uptake as a Mechanism for Drug-Drug Interaction between Cerivastatin and Cyclosporin A J. Pharmacol. Exp. Ther., February 1, 2003; 304(2): 610 - 616. [Abstract] [Full Text] [PDF]
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 B. Ugele, M. V. St-Pierre, M. Pihusch, A. Bahn, and P. Hantschmann Characterization and identification of steroid sulfate transporters of human placenta Am J Physiol Endocrinol Metab, February 1, 2003; 284(2): E390 - E398. [Abstract] [Full Text] [PDF]
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R. G. Tirona, B. F. Leake, A. W. Wolkoff, and R. B. Kim Human Organic Anion Transporting Polypeptide-C (SLC21A6) Is a Major Determinant of Rifampin-Mediated Pregnane X Receptor Activation J. Pharmacol. Exp. Ther., January 1, 2003; 304(1): 223 - 228. [Abstract] [Full Text] [PDF]
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Y. Miki, T. Nakata, T. Suzuki, A. D. Darnel, T. Moriya, C. Kaneko, K. Hidaka, Y. Shiotsu, H. Kusaka, and H. Sasano Systemic Distribution of Steroid Sulfatase and Estrogen Sulfotransferase in Human Adult and Fetal Tissues J. Clin. Endocrinol. Metab., December 1, 2002; 87(12): 5760 - 5768. [Abstract] [Full Text] [PDF]
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 C. Michalski, Y. Cui, A. T. Nies, A. K. Nuessler, P. Neuhaus, U. M. Zanger, K. Klein, M. Eichelbaum, D. Keppler, and J. Konig A Naturally Occurring Mutation in the SLC21A6 Gene Causing Impaired Membrane Localization of the Hepatocyte Uptake Transporter J. Biol. Chem., November 1, 2002; 277(45): 43058 - 43063. [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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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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Y. Kawabata, S. Furuta, Y. Shinozaki, T. Kurimoto, and R. Nishigaki Carrier-Mediated Active Transport of a Novel Thromboxane A2 Receptor Antagonist [2-(4-Chlorophenylsulfonylaminomethyl)indan-5-yl]acetate (Z-335) into Rat Liver Drug Metab. Dispos., May 1, 2002; 30(5): 498 - 504. [Abstract] [Full Text] [PDF]
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N. Li, D. P. Hartley, N. J. Cherrington, and C. D. Klaassen Tissue Expression, Ontogeny, and Inducibility of Rat Organic Anion Transporting Polypeptide 4 J. Pharmacol. Exp. Ther., May 1, 2002; 301(2): 551 - 560. [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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G. L. Guo, J. Staudinger, K. Ogura, and C. D. Klaassen Induction of Rat Organic Anion Transporting Polypeptide 2 by Pregnenolone-16alpha -carbonitrile Is via Interaction with Pregnane X Receptor Mol. Pharmacol., April 1, 2002; 61(4): 832 - 839. [Abstract] [Full Text] [PDF]
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O. Briz, M. A. Serrano, N. Rebollo, B. Hagenbuch, P. J. Meier, H. Koepsell, and J. J.G. Marin Carriers Involved in Targeting the Cytostatic Bile Acid-Cisplatin Derivatives cis-Diammine-chloro-cholylglycinate-platinum(II) and cis-Diammine-bisursodeoxycholate-platinum(II) toward Liver Cells Mol. Pharmacol., April 1, 2002; 61(4): 853 - 860. [Abstract] [Full Text] [PDF]
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S.-Y. Cai, W. Wang, C. J. Soroka, N. Ballatori, and J. L. Boyer An evolutionarily ancient Oatp: insights into conserved functional domains of these proteins Am J Physiol Gastrointest Liver Physiol, April 1, 2002; 282(4): G702 - G710. [Abstract] [Full Text] [PDF]
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G. L. Guo, D. R. Johnson, and C. D. Klaassen Postnatal Expression and Induction by Pregnenolone-16alpha -Carbonitrile of the Organic Anion-Transporting Polypeptide 2 in Rat Liver Drug Metab. Dispos., March 1, 2002; 30(3): 283 - 288. [Abstract] [Full Text] [PDF]
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T. Yamada, M. Yoshikawa, S. Kanda, Y. Kato, Y. Nakajima, S. Ishizaka, and Y. Tsunoda In Vitro Differentiation of Embryonic Stem Cells into Hepatocyte-Like Cells Identified by Cellular Uptake of Indocyanine Green Stem Cells, March 1, 2002; 20(2): 146 - 154. [Abstract] [Full Text] [PDF]
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M. Sasaki, H. Suzuki, K. Ito, T. Abe, and Y. Sugiyama Transcellular Transport of Organic Anions Across a Double-transfected Madin-Darby Canine Kidney II Cell Monolayer Expressing Both Human Organic Anion-transporting Polypeptide (OATP2/SLC21A6) and Multidrug Resistance-associated Protein 2 (MRP2/ABCC2) J. Biol. Chem., February 15, 2002; 277(8): 6497 - 6503. [Abstract] [Full Text] [PDF]
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D. Sugiyama, H. Kusuhara, Y. Shitara, T. Abe, and Y. Sugiyama Effect of 17beta -Estradiol-D-17beta -Glucuronide on the Rat Organic Anion Transporting Polypeptide 2-Mediated Transport Differs Depending on Substrates Drug Metab. Dispos., February 1, 2002; 30(2): 220 - 223. [Abstract] [Full Text] [PDF]
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Y. Cui, J. Konig, and D. Keppler Vectorial Transport by Double-Transfected Cells Expressing the Human Uptake Transporter SLC21A8 and the Apical Export Pump ABCC2 Mol. Pharmacol., November 1, 2001; 60(5): 934 - 943. [Abstract] [Full Text] [PDF]
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E. C. H. Friesema, R. Docter, E. P. C. M. Moerings, F. Verrey, E. P. Krenning, G. Hennemann, and T. J. Visser Thyroid Hormone Transport by the Heterodimeric Human System L Amino Acid Transporter Endocrinology, October 1, 2001; 142(10): 4339 - 4348. [Abstract] [Full Text] [PDF]
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 G. Hennemann, R. Docter, E. C. H. Friesema, M. de Jong, E. P. Krenning, and T. J. Visser Plasma Membrane Transport of Thyroid Hormones and Its Role in Thyroid Hormone Metabolism and Bioavailability Endocr. Rev., August 1, 2001; 22(4): 451 - 476. [Abstract] [Full Text] [PDF]
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P. M. Yen Physiological and Molecular Basis of Thyroid Hormone Action Physiol Rev, July 1, 2001; 81(3): 1097 - 1142. [Abstract] [Full Text] [PDF]
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D. Nakai, R. Nakagomi, Y. Furuta, T. Tokui, T. Abe, T. Ikeda, and K. Nishimura Human Liver-Specific Organic Anion Transporter, LST-1, Mediates Uptake of Pravastatin by Human Hepatocytes J. Pharmacol. Exp. Ther., June 1, 2001; 297(3): 861 - 867. [Abstract] [Full Text]
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K. Fujiwara, H. Adachi, T. Nishio, M. Unno, T. Tokui, M. Okabe, T. Onogawa, T. Suzuki, N. Asano, M. Tanemoto, et al. Identification of Thyroid Hormone Transporters in Humans: Different Molecules Are Involved in a Tissue-Specific Manner Endocrinology, May 1, 2001; 142(5): 2005 - 2012. [Abstract] [Full Text]
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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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C. Buettner, J. W. Harney, and P. R. Larsen The Role of Selenocysteine 133 in Catalysis by the Human Type 2 Iodothyronine Deiodinase Endocrinology, December 1, 2000; 141(12): 4606 - 4612. [Abstract] [Full Text] [PDF]
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H. C. Walters, A. L. Craddock, H. Fusegawa, M. C. Willingham, and P. A. Dawson Expression, transport properties, and chromosomal location of organic anion transporter subtype 3 Am J Physiol Gastrointest Liver Physiol, December 1, 2000; 279(6): G1188 - G1200. [Abstract] [Full Text] [PDF]
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L. Li, P. J. Meier, and N. Ballatori Oatp2 Mediates Bidirectional Organic Solute Transport: A Role for Intracellular Glutathione Mol. Pharmacol., August 1, 2000; 58(2): 335 - 340. [Abstract] [Full Text]
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B. Gao, B. Hagenbuch, G. A. Kullak-Ublick, D. Benke, A. Aguzzi, and P. J. Meier Organic Anion-Transporting Polypeptides Mediate Transport of Opioid Peptides across Blood-Brain Barrier J. Pharmacol. Exp. Ther., July 1, 2000; 294(1): 73 - 79. [Abstract] [Full Text]
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J. Konig, Y. Cui, A. T. Nies, and D. Keppler A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane Am J Physiol Gastrointest Liver Physiol, January 1, 2000; 278(1): G156 - G164. [Abstract] [Full Text] [PDF]
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B. Hsiang, Y. Zhu, Z. Wang, Y. Wu, V. Sasseville, W.-P. Yang, and T. G. Kirchgessner A Novel Human Hepatic Organic Anion Transporting Polypeptide (OATP2). IDENTIFICATION OF A LIVER-SPECIFIC HUMAN ORGANIC ANION TRANSPORTING POLYPEPTIDE AND IDENTIFICATION OF RAT AND HUMAN HYDROXYMETHYLGLUTARYL-CoA REDUCTASE INHIBITOR TRANSPORTERS J. Biol. Chem., December 24, 1999; 274(52): 37161 - 37168. [Abstract] [Full Text] [PDF]
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J. Konig, Y. Cui, A. T. Nies, and D. Keppler Localization and Genomic Organization of a New Hepatocellular Organic Anion Transporting Polypeptide J. Biol. Chem., July 21, 2000; 275(30): 23161 - 23168. [Abstract] [Full Text] [PDF]
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Y. Cui, J. Konig, I. Leier, U. Buchholz, and D. Keppler Hepatic Uptake of Bilirubin and Its Conjugates by the Human Organic Anion Transporter SLC21A6 J. Biol. Chem., March 23, 2001; 276(13): 9626 - 9630. [Abstract] [Full Text] [PDF]
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E. Battaglia and J. Gollan A Unique Multifunctional Transporter Translocates Estradiol-17beta -Glucuronide in Rat Liver Microsomal Vesicles J. Biol. Chem., June 22, 2001; 276(26): 23492 - 23498. [Abstract] [Full Text] [PDF]
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R. G. Tirona, B. F. Leake, G. Merino, and R. B. Kim Polymorphisms in OATP-C. IDENTIFICATION OF MULTIPLE ALLELIC VARIANTS ASSOCIATED WITH ALTERED TRANSPORT ACTIVITY AMONG EUROPEAN- AND AFRICAN-AMERICANS J. Biol. Chem., September 14, 2001; 276(38): 35669 - 35675. [Abstract] [Full Text] [PDF]
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D. Jung, B. Hagenbuch, L. Gresh, M. Pontoglio, P. J. Meier, and G. A. Kullak-Ublick Characterization of the Human OATP-C (SLC21A6) Gene Promoter and Regulation of Liver-specific OATP Genes by Hepatocyte Nuclear Factor 1alpha J. Biol. Chem., September 28, 2001; 276(40): 37206 - 37214. [Abstract] [Full Text] [PDF]
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