AdipoR2 is transcriptionally regulated by ER
stress-inducible ATF3 in HepG2 human hepatocyte cells
In-uk Koh
1,2
, Joo H. Lim
1
, Myung K. Joe
1
, Won H. Kim
1
, Myeong H. Jung
3
, Jong B. Yoon
2
and
Jihyun Song
1
1 Division of Metabolic Disease, Department of Biomedical Science, National Institutes of Health, Seoul, South Korea
2 Department of Biochemistry, College of Science, Yonsei University, Seodaemoon-Gu, Seoul, South Korea
3 School of Korean Medicine, Pusan National University, Yangsan-si, Gyeongnam, South Korea
Introduction
Obesity and/or obesity-linked insulin resistance, one of
the key features of type 2 diabetes, are regarded as risk
factors for metabolic syndrome and atherosclerosis [1].
Adiponectin, which is abundantly expressed in adipose
tissue, is a circulating peptide hormone with direct
insulin-sensitizing activity. This adipokine has amelio-
rative effects on insulin resistance in peripheral tissues,
and plays a central role in the regulation of energy
Keywords
AdipoR2; ATF3; ER stress; insulin

the hepatic expression of adiponectin receptor 2 (AdipoR2) was lower, but
the expression of markers of the ER stress pathway, 78 kDa glucose-regu-
lated protein (GRP78) and activating transcription factor 3 (ATF3), was
higher in the liver of ob/ob mice compared with control mice. To investi-
gate the regulation of AdipoR2 by ER stress, we added thapsigargin, an
ER stress inducer, to a human hepatocyte cell line, HepG2. Addition of
the ER stress inducer increased the levels of GRP78 and ATF3, and
decreased that of AdipoR2, whereas addition of a chemical chaperone, 4-
phenyl butyric acid (PBA), could reverse them. Up- or down-regulation of
ATF3 modulated the AdipoR2 protein levels and AdipoR2 promoter activ-
ities. Reporter gene assays using a series of 5¢-deleted AdipoR2 promoter
constructs revealed the location of the repressor element responding to ER
stress and ATF3. In addition, using electrophoretic mobility shift and chro-
matin immunoprecipitation assays, we identified a region between nucleo-
tides )94 and )86 of the AdipoR2 promoter that functions as a putative
ATF3-binding site in vitro and in vivo. Thus, our findings suggest that the
ER stress-induced decrease in both protein and RNA of AdipoR2 results
from a concomitant increase in expression of ATF3, which may play a role
in the development of obesity-induced insulin resistance and related ER
stress in hepatocytes.
Abbreviations
AdipoR2, adiponection receptor 2; ATF3, activating transcription factor 3; GRP78, 78 kDa glucose-regulated protein; PBA, 4-phenyl butyric
acid.
2304 FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS
homeostasis [2–4]. In obesity, adiponectin activity
declines as a result of decreased adiponectin expression
and/or a defect in downstream adiponectin signalling.
The combined actions of genetic factors such as single-
nucleotide polymorphisms in the adiponectin gene
and environmental factors such as a high-fat diet and

ine phosphorylation of insulin receptor substrate 1
[9,15]. We recently demonstrated that an agent causing
ER stress activated JNK and consequently induced
ATF3, with a reduction in adiponectin transcription [8].
Nakatani et al. [16] identified a molecular chaperone
that protects cells from ER stress and its effect on
insulin sensitivity in the liver. The chemical chaperones
4-phenyl butyric acid (PBA) and tauroursodeoxycholic
acid, which have the ability to decrease ER stress, act
as potent anti-diabetic agents [10]. Because ER is
abundant in hepatocytes, and the liver is a primary
target organ of insulin and adiponectin [3,14,17], we
focused on regulation of the adiponectin receptor
under ER stress-induced conditions in liver cells.
In humans, adiponectin receptors 1 and 2 (AdipoR1
and AdipoR2, respectively) serve as receptors for globu-
lar and/or full-length adiponectin. AdipoR1 is ubiqui-
tously expressed and is particularly abundant in skeletal
muscle, whereas AdipoR2 is expressed primarily in liver
[17]. These receptors have seven transmembrane
domains, and share 67% amino acid homology. In con-
trast to G protein-coupled receptors, their N-terminus is
intracellular [5]. Although the intracellular adaptor pro-
tein APPL1 (adaptor protein, phosphotyrosine interac-
tion, PH domain and leucine zipper containing 1) has
recently been proposed as a modulator of insulin action
by binding to adiponectin receptors [18], the overall
mechanism of adiponectin signaling is largely unknown.
As expression of adiponectin receptors, as well as adipo-
nectin itself, is known to be decreased in obesity-related

the AdipoR2 level, and thus we studied the effect of
ER stress on the AdipoR2 level in human hepatocytes.
When HepG2 cells were exposed to 1.0 lm thapsi-
gargin, a well-known inducer of ER stress, for 24 h,
both the ER molecular chaperone GRP78 and also
ATF3, which has been shown to repress transcription
of the adiponectin gene in adipocytes [8], were induced.
In-uk Koh et al. Transcriptional regulation of AdipoR2 by ATF3
FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS 2305
Interestingly, the level of AdipoR2 protein was
decreased coincidentally with the increase of ATF3
(Fig. 1B and Table S1).
To determine whether the observed changes in
protein expression were caused by thapsigargin-induced
ER stress, cells were pre-incubated with 20 mm PBA
for 24 h prior to thapsigargin exposure. In cells
pre-incubated with PBA, thapsigargin-induced increases
in GRP78 and ATF3 protein levels did not occur, and
the ER stress-induced decrease in AdipoR2 level was
C57BL6/J
ob/ob
1.5
2
2.5 C57BL6/J ob/ob
C57BL6/J
ob/ob
ATF3
GRP78
A
BC

2
Arbitrary units
AdipoR2
ATF3
Actin
(AU)
*
**
*
0
+–
+
+
Ad YFP
Adv-ATF3
–
(MOI)
siATF3
Thap
123123
GRP78 ATF3 AdipoR2
––+
–+
GRP78 ATF3 AdipoR2
atf3 adipor2
Control Thap Thap/PBA
Control Thap
Thap + siATF3 Thap + Neg.RNAi
––
Adv-YFP

after infection with ATF3-expressing adenovirus. HepG2 cells were infected with an adenoviral vector expressing human ATF3 (Adv-ATF3) at
a multiplicity of infection of 2–10 and incubated for 48 h. HepG2 cells infected with Adv-YFP at a multiplicity of infection of 5 were used as
control. (E) Changes in expression of endogenous AdipoR2 upon thapsigargin-induced ER stress with or without silencing of ATF3. siATF3
or Neg.RNAi was introduced to the cells 24 h prior to treatment with 1.0 l
M thapsigargin. For western blot analysis, b-actin was used as a
protein loading control. The asterisks indicate a P value < 0.05 for the bracketed comparisons.
Transcriptional regulation of AdipoR2 by ATF3 In-uk Koh et al.
2306 FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS
specifically rescued (Fig. 1B, lane 3). In addition, we
measured the mRNA levels for ATF3 and AdipoR2
in HepG2 cells with or without thapsigargin or PBA
treatment, and the results showed a trend similar to the
protein level changes (Fig. 1C).
We next examined the effect of ATF3 over-expres-
sion in hepatocytes on changes in the AdipoR2 protein
level. We introduced an adenoviral vector carrying
recombinant ATF3 (Adv-ATF3) into HepG2 cells,
and analyzed the resulting protein expression
using western blotting. As expected, transduction of
Adv-ATF3 resulted in a dose-dependent increase in
the ATF3 protein level. The increase in ATF3 protein
level resulted in a decrease in the AdipoR2 protein
level, but in a non-dose-dependent way (Fig. 1D).
The absence of dose dependence for the reduction of
AdipoR2 may be due to cellular systemic utilization of
the proteins.
In order to further investigate whether ATF3 plays
an important role in ER stress-induced down-regula-
tion of AdipoR2, we assessed the effect of knocking
down ATF3 on the AdipoR2 level. Within 48 h after

treatment, silencing of ATF3 reduced the repressive
effect of thapsigargin on the promoter activity of
AdipoR2 (Fig. 2C). To investigate whether ATF3 affects
AdipoR2 expression directly, in other words to locate
the repressor element in the AR2P()1974) promoter
region, as suggested by the above results, we analyzed
the promoter activity of 5¢ serially deleted human
AdipoR2 promoter constructs in pGL3-Basic vector
(Fig. 2D,E). Four plasmid constructs containing
portions of the promoter region of various lengths were
transfected into HepG2 cells with or without co-trans-
fection of the ATF3-expressing vector (ATF3/
pcDNA3.1). As shown in Fig. 2D, ATF3 co-transfec-
tion repressed the promoter activities of the transfected
AdipoR2 reporter constructs AR2P()1974), AR2P
()870) and AR2P()343). However, the activity of the
shortest construct AR2P() 72) was as low as that in the
control (pGL3) group. In another experiment, various
amounts of ATF3/pcDNA3.1 (0, 0.2 and 0.4 lg) were
co-transfected with AR2P()343) or AR2P()72), and
significant dose-dependent repression by ATF3 was
observed in cells transfected with AR2P()343) but not
in those transfected with AR2P()72) (Fig. 2E). ATF3
co-transfection with this shortest construct AR2P()72)
showed a tendency to decrease the reporter activity
(approximately 50%) but without statistical significance
(P = 0.15) (Table S3 and Fig. S1).
Given that AR2P()72) was not responsive to ATF3,
we presume that more than 72 nucleotides of promoter
region are required for the expression of AdipoR2,

was confirmed by competition with unlabeled oligonu-
cleotides (Fig. 3C) and by dose-dependent inhibition
by antibody against ATF3 (Fig. 3D). As a negative con-
trol for binding of the bZIP (basic leucine zipper) tran-
scription factor ATF3 to the putative binding site, we
used probe ‘X’, containing a sequence that recruits one
of the zinc-finger DNA-binding transcription factor,
also known to interact with the CREB-binding
protein. In the competition EMSA shown in Fig. 3C, a
100 x excess of non-specific probe ‘X’ did not showed
100
120
A
DE
BC
*
100
120
**
*
100
120
*
*
*
20
40
60
80
20

AR2P(–1974)
0
ATF3
0
–
–
+
–
+
+
+
++
AR2P(–1974)
60
80
100
120
75
100
125
150
* * *
**
*
0
20
40
60
AR2P(–1974)
0

––++
–+–+
+++––
–––++
–
+
0 0.4 0 0.4
Fig. 2. Changes in the promoter activity of AdipoR2 under conditions of ER stress and ATF3 over-expression. (A) Activity of the AdipoR2 pro-
moter in HepG2 human liver cells with ER stress induction by 1.0 l
M thapsigargin for 24 h. The pGL3-Basic-derived reporter construct compris-
ing nucleotides ) 1974 to +0 of the AdipoR2 promoter [AR2P(–1974)] was transfected into HepG2 cells, followed by treatment with
thapsigargin. (B) Activity of the AdipoR2 promoter in HepG2 cells with ATF3 over-expression by co-transfection of 0.2 or 0.4 lg of ATF3 expres-
sion vector. (C) Activity of the AdipoR2 promoter in HepG2 cells upon thapsigargin-induced ER stress with or without silencing of ATF3. siATF3
or Neg.RNAi was introduced to the cells 24 h prior to treatment with 1.0 l
M thapsigargin. Luciferase activity values were measured in triplicate
and expressed as arbitrary units. (D) Promoter activities of reporter gene constructs containing 0.6 lg of various lengths of 5¢ deleted fragments
of the promoter region subcloned into the pGL3-Basic plasmid vector and transfected with or without 0.4 lg of ATF3-expressing vector. (E)
ATF3-dose-dependent repression of the promoter activity upon co-transfection of 0, 0.2 or 0.4 lg of ATF3-expressing plasmids with 0.6 lgof
reporter plasmid into HepG2 cells. The asterisks indicate a P value < 0.05 for the bracketed comparisons. NS, not significant.
Transcriptional regulation of AdipoR2 by ATF3 In-uk Koh et al.
2308 FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS
competition in binding to ATF3, but assays using a
100 x excess of cold/unlabeled )94/)86 or the ATF/
CRE positive control probe did show competition with
tested probes containing the putative )94/)86 site, indi-
cating the specificity of this binding assay.
To determine the physiological relevance of ER
stress and/or stress-related expression of ATF3 on
formation of the protein–DNA complex in vitro,we
increased the expression of ATF3 in HepG2 cells by

c
NE: HepG2 cells
–94/–86 of promoter
Consensus ATF/CRE
No Ext.
No Comp.
x10
x100
Competitor
NE: HepG2 cells
o Ext.
o Comp.
x100 Cold
x
100 ATF/CRE
x100 Non-specific
ATF3
N
on-specific Ab
o
Ext.
w/o Ab
1μ
μ
g
2
μ
g
4
μ

type nucleotide )94/)86 probe, a 100-fold excess of the consensus ATF/CRE-binding site sequence, or a 100-fold excess of the non-specific
probe (B,C). Competition assays with ATF-specific antibody (1–4 lg) were also performed (D).
In-uk Koh et al. Transcriptional regulation of AdipoR2 by ATF3
FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS 2309
binding ability in EMSA and ChIP experiments, we
generated a mutant promoter construct lacking a
22 bp fragment of the promoter between nucleotides
)94 and )86 (Fig. 5A), to investigate whether this
region responds to ATF3 and ER stress and plays a
role in the transcriptional regulation of AdipoR2.
The activity of this construct, AR2P()343D), was
then analyzed with or without co-transfection of
ATF3/pcDNA3.1 (Fig. 5B). Co-transfection with
ATF3 dramatically decreased the promoter activity of
the wild-type promoter construct [AR2P()343)] to
one-tenth that of untreated cells, but attenuated the
Thap (1.0 µM)
AB
Adv-ATF3 Mock
ATF3
β
β
-Actin
β
-Actin
ATF3
Ext.
a
p
a

Adv-
Mock
No E
Adv-
Mock
ATF/CRE
–94 / –86
*
*
*
*
Labeled probes
Labeled probes
+–
Exon1
(–94/–86)
Thapsigargin (1.0
μ
M)
IgG
12 h
––
2 h 4 h 6 h
2 h 4 h 6 h
12 h
Input
Promoter, 323 bp Exon1, 328 bp
ATF3
Input
C

to the putative binding element as a result
of ER stress.
Transcriptional regulation of AdipoR2 by ATF3 In-uk Koh et al.
2310 FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS
activity of the mutant construct without the )94/)86
putative binding element [AR2P()343D)] to only half
that of untreated cells (Fig. 5B). As shown in Fig. 5C,
the ER stress inducer thapsigargin had less of a repres-
sor effect on the mutant reporter construct ()56%)
than on the wild-type construct ()85%).
Discussion
Many groups have confirmed the anti-diabetic/insulin-
sensitizing effect of adiponectin, and thus plasma
adiponectin and its receptors in peripheral organs have
been proposed as therapeutic targets for the treatment
of diabetes and obesity-linked insulin resistance
[2,28,29]. The action of adiponectin is known to be
transduced via regulation of AMP-activated protein
kinase (AMPK) function, and, given the report of a
putative adaptor protein that interacts with adiponectin
receptors, insulin and adiponectin signaling are now
considered to be linked in the peripheral organs of
insulin action, such as the liver and skeletal muscle
[16,30,31]. Despite the fact that the action and plasma
level of adiponectin have been reported to be reduced
in diseases associated with obesity, including peripheral
insulin resistance and related ER stress cascades
[2,3,8,9], the relationship between obesity-related ER
stress and the consequent reduction in adiponectin
action is obscure. We found that hepatic expression of

AR2P(–343Δ)
Luc
Luc
(–72 bp)
(–94/–86)
AR2P(–343)
AR2P(–72)
120
A
BC
120
**
* *
40
60
80
100
40
60
80
100
0
20
0
20
AR2P(–343Δ)
AR2P(–343)
ATF3
pGL3
Luciferase activity (%)

AdipoR2 level showed strong support for an ER
stress-based mechanism of AdipoR2 decrease in
human hepatocytes (Fig. 1B). To determine the mecha-
nism of changes in AdipoR2 expression resulting from
ER stress and ATF3 over-expression or silencing in
the liver (Fig. 1B–E), we measured the promoter acti-
vity of the AdipoR2 gene. Up- or down-regulation of
ATF3 modulated the AdipoR2 promoter activity
(Fig. 2B,C). By analysing the promoter region of the
AdipoR2 gene, we identified a putative ATF3-binding
sequence (Fig. 3). As shown in Figs 3 and 4, the
decrease in AdipoR2 expression by ATF3 in ER stress
was mediated by this putative sequence which recruited
ATF3 in vitro and in vivo. This result provides an
explanation for the role of ER stress and induced
ATF3 in obesity-linked insulin resistance through regu-
lation of adiponectin action.
These transcription-repressing mechanisms of ER
stress-induced ATF3 have been shown to contribute to
the development of insulin resistance and type 2 diabe-
tes. Insulin receptor substrates 1 and 2 were found to be
repressed by ATF3 in myocytes [35] and pancreatic b-
cells [11], respectively. The level of the insulin-sensitizing
hormone adiponectin was decreased by ATF3 in adipo-
cytes [8], and the major receptor in hepatocytes, Adi-
poR2, was also negatively regulated. The above effects
of ATF3 on insulin signaling and glucose homeostasis
involve the action of adiponectin in peripheral tissues.
In particular, given that the cause and effect relationship
between adiponectin and insulin action is not fully

of ATF3 on the promoter region of AdipoR2 may
exist through an unidentified binding site. In addition,
this putative ATF3-binding site could recruit the
transcription factor complex for dichotomous actions,
possibly through the action of uncharacterized dimer-
ization partner(s) of ATF3, such as ATF2, c-Jun,
JunB, JunD, etc. [43]. Given the nature of the deleted
‘semi-palindromic’ sequence )94/)86 (TGCGCGTCA)
and bZip transcription factors including ATF3 [27],
these dimerization partner(s) of ATF3 may have very
complicated transcription factor/co-factor relation-
ships. These possibilities must be studied further to
clarify the ATF3-mediated negative effect on transcrip-
tion of AdipoR2 under ER stress in the liver.
In this study, exposure to the ER stress inducer
thapsigargin and the accompanying induction of ATF3
were inversely correlated with changes in the expression
level of AdipoR2 in human HepG2 cells, and this corre-
lation was the result of direct transcriptional regulation
of AdipoR2 by the repressor ATF3 via the putative bind-
ing site between nucleotides )94 and )86 of the pro-
moter region. This finding of decreased AdipoR2 levels
as a result of the regulation by ATF3 is noteworthy, and
suggests that obesity-related ER stress may affect the
development of hepatic insulin resistance, at least in part
by transcriptional repressing activity of ATF3.
Experimental procedures
Animals and materials
To compare the expression levels of ER stress markers and
the adiponectin receptor in animals of various genetic back-

ER stress, cells were pre-incubated for 24 h in culture med-
ium containing 20 mm 4-phenyl butyric acid (PBA) (Calbio-
chem, San Diego, CA, USA) prior to treatment with
1.0 lm thapsigargin.
Over-expression of adenoviral ATF3
After PCR amplification, the ATF3 gene was ligated into
the adenovirus shuttle vector pShuttle-CMV (Stratagene,
La Jolla, CA, USA), which includes GFP (green fluorescent
protein) tagged to the C-terminus of the ATF3 protein.
Recombinant adenoviral genomes were produced by recom-
bination between the shuttle vector constructed above and
the pAdEasy vector (Stratagene), according to the manufac-
turer’s protocol [44]. The genomes were subsequently trans-
fected into HEK 293 cells using Lipofectamine reagent
(Invitrogen). ATF3-expressing adenovirus particles (Adv-
ATF3) were obtained as a viral mixture in culture medium
7–9 days after transfection, with the viral particle number
of the adenoviral mixture ranging between 1.0 and
2.0 · 10
10
IFU (inclusion-forming units)ÆmL
)1
depending
on the sample. The recombinant virus was propagated in
HEK 293 cells before transduction into HepG2 cells. Con-
trol adenovirus (mock, Adv-YFP) was generated by the
same method using an empty adenoviral shuttle plasmid.
HepG2 cells were infected with the adenoviral mixture at a
multiplicity of infection between 2 and 10 for over-expres-
sion of recombinant ATF3, while Adv-YFP was infected

using the KpnI and XhoI restriction sites. AR2P()343D),
a deletion mutant lacking the putative ATF3-binding site,
was PCR-generated from the AR2P()343) plasmid using
the additional internal primers 5¢-GAGGCGGTTCGAG
CCAATA-3¢ and 5¢-CGTGCGGTCGTGGGGG-3¢, which
hybridized upstream and downstream, respectively, of the
22 bp promoter region containing the putative ATF3-bind-
ing site at nucleotide positions )94 to )86.
Luciferase activity assay
HepG2 cells were grown in six-well plates to 70% conflu-
ence and then transfected with pGL3-Basic-derived reporter
constructs containing the AdipoR2 promoter region and a
pcDNA3.1-derived ATF3 expression plasmid using Lipofec-
tAMINE reagent (Invitrogen) according to the manufac-
turer’s instructions [45]. b-galactosidase (CMV-b-gal)
expression vectors were used to correct differences in trans-
fection efficiency. The cells were lysed 24 h after transfec-
tion, and their luciferase activity was measured using a
luciferase assay system (Promega).
Semi-quantitative RT-PCR
We used the following primers for RT-PCR: atf3-sense,
5¢-GGTTTGCCATCCAGAACAAG-3¢; atf3-antisense, 5¢-CC
TCCCAGGAGAAGGTAAGC-3¢; adipor2-sense, 5¢-TAGC
CTTTGGTTTGCTTTGG-3¢; adipor2-antisense, 5 ¢-CATAT
CTCCAGGCGTCAACC-3¢; gapdh-sense, 5¢-ATGACATC
AAGAAGGTGGTG-3¢; gapdh-antisense, 5¢-CCAAATTC
GTTGTCATACCA-3¢. Total RNA was obtained from
HepG2 cells using an RNeasy kit (Qiagen GmbH, Hilden,
Germany) according to the manufacturer’s instructions.
In-uk Koh et al. Transcriptional regulation of AdipoR2 by ATF3

b-actin. Then the protein level for ob/ob mice was com-
pared with that of C57BL6/J mice to obtain the relative
ratio value versus the mean of the control group.
Electrophoretic mobility shift assay (EMSA)
Nuclear extracts of HepG2 cell were prepared as described
previously [46]. Probes corresponding to the putative ATF3/
CRE-binding site on the AdipoR2 promoter region were syn-
thesized and radiolabeled with [c-
32
P]dATP (sense 5¢-
GTGCGATGCGCGTCACGGCGA-3¢; antisense 5¢-TC
GCCGTGACGCGCATCGCAC-3¢). Labeled probes were
then incubated with 5 mg of nuclear extract protein in the
presence or absence of competitor DNA or antibodies. The
resulting complexes were electrophoresed on a 5% non-dena-
turing polyacrylamide gel in 0.5· Tris borate/EDTA electro-
phoresis buffer (45 mm Tris borate, 1 mm EDTA, pH 8.0).
After drying, gels were visualized using autoradiography.
Chromatin immunoprecipitation
Chromatin immunoprecipitation (ChIP) was performed
with a ChIP assay kit (Upstate Biotechnology, Lake Placid,
NY, USA) according to the manufacturer’s protocol, modi-
fied as previously described [47]. After 0–12 h of thapsigar-
gin-induced ER stress, 1 · 10
6
HepG2 cells in a 100 mm
plate were cross-linked with 1% formaldehyde in
Dulbecco’s modified Eagle’s medium for 10 min at room
temperature. The cells were collected, and the chromatin
was sheared into fragments averaging 300–500 bp. The

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Table S3. Statistical analysis of arbitrary values corre-
sponding to the luciferase activities of AR2P(–72) with
or without ATF3 induction.
Table S4. Arbitrary values of the reporter activities of
WT AR2P(-343) and its mutant and the changes by
ATF3 co-transfection.
Table S5. Arbitrary values for the reporter activity of
pGL3-basic vector with or without ATF3 co-transfec-
tion.
Transcriptional regulation of AdipoR2 by ATF3 In-uk Koh et al.
2316 FEBS Journal 277 (2010) 2304–2317 ª 2010 The Authors Journal compilation ª 2010 FEBS
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In-uk Koh et al. Transcriptional regulation of AdipoR2 by ATF3
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