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Departments of Biochemistry (T.S.), Pediatrics (S.A.), and Obstetrics and Gynecology (N.S., Y.F., E.N., S.F.), Hokkaido University School of Medicine, Sapporo, Hokkaido 060-8638, Japan; Department of Pediatrics, Asahikawa Medical College (K.F.), Asahikawa, Hokkaido 078-8510, Japan; and Division of Virology of the National Cancer Center Research Institute (M.S.), Tukiji, Tokyou 104-8638, Japan
Address all correspondence and requests for reprints to: Dr. Teruo Sugawara, Department of Biochemistry, Hokkaido University School of Medicine, Kita-ku, Kita 15, Nishi 7, Sapporo 060-8638, Japan. E-mail: terusuga{at}med.hokudai.ac.jp
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Introduction |
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SF-1 is an orphan nuclear receptor (8) and plays a major role in regulation of the expression of steroidogenic P450 enzymes and the steroidogenic acute regulatory protein (StAR) gene, which plays a key role in the intramitochondrial movement of cholesterol to P450scc (9, 10, 11, 12). The transport of cholesterol from the outer mitochondrial membrane to the inner membrane is the rate-limiting process of steroidogenesis. The StAR gene is mutated in subjects with congenital lipoid adrenal hyperplasia (13), resulting in marked impairment of adrenal gonadal steroid synthesis. The promoters of the human, mouse and porcine StAR genes each contain SF-1 binding sites (14, 15, 16, 17), and SF-1 has been shown to be important for basal and cAMP-stimulated activity of the human StAR promoter (16).
DAX-1 has been identified as the gene responsible for adrenal hypoplasia congenita (18, 19). Human DAX-1 protein consists of 470 amino acids (aa), and half of the 225 aa of the C-terminal region have high homology to the ligand-binding domain of some members of the nuclear hormone receptor superfamily (20, 21, 22, 23). DAX-1 is expressed in a tissue-specific manner, and it is found in the adrenal cortex, testis, ovary, anterior pituitary gonadotropes, and ventral medial hypothalamus (21, 24, 25). In steroidogenic tissues, DAX-1 blocks steroid biosynthesis by impairing the expression of the StAR gene (26, 27), which is also restricted to steroid-producing cells of the adrenal gland, testis, and ovary (28). Thus, the orphan receptors SF-1 and DAX-1 play key roles in the control of StAR gene expression and, hence, steroid hormone production.
We have demonstrated an interaction between Sp1 and SF-1 on the human StAR promoter (29). Although Sp1 and SF-1 interact with each other and cooperate to regulate the basal activity of the human StAR promoter, these interactions have only a small influence on cAMP-stimulated promoter activity. Other factors, coactivators or corepressors, may combine with SF-1 and DAX-1 to control the human StAR gene. In the present study we examined the role of a comodulator in SF-1 and DAX-1 actions on human StAR gene transcription.
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Materials and Methods |
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Cell culture and antibodies
Mouse Y-1 adrenal tumor cells and COS-1 cells were obtained from
RIKEN Cell Bank (Tsukuba, Japan). Human granulosa-like tumor KGN cells
were a gift from Dr. Yoshihiro Nishi (Graduate School of Medical
Sciences, Kyushu University, Kyushu, Japan) (31). The Y-1
cells and COS-1 cells were grown in 35-mm plastic dishes. The Y-1 cells
and COS-1 cells were cultured in DMEM supplemented with 10% FCS and 50
µg/ml gentamicin. The KGN cells were grown in DMEM/Ham’s F-12
containing 10% FCS and 50 µg/ml gentamicin. A polyclonal antibody
against DAX-1 was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA). A polyclonal antibody against SF-1 was
provided by Dr. Kenichiro Morohashi.
Luciferase assays
Mouse Y-1 adrenal tumor cells and COS-1 cells were grown in
35-mm plastic dishes in DMEM supplemented with 10% FCS, as previously
described (29). Cells were transfected with
pGL2 plasmids and pCH110 with 4.5 µl Tfx-50
(Promega Corp.)/1 µg DNA with DAX-1 or RIP 140
expression plasmids. Cells were harvested 48 h after transfection.
Some cultures were treated with 8-bromo-cAMP (1 mM) during
the final 24 h of culture. Cell extracts were made in 400 µl
lysis buffer (Promega Corp.). One hundred microliters were
used for the luciferase assay, and 150 µl were used for the
ß-galactosidase assay. The luciferase assay results were normalized
to ß-galactosidase activity to compensate for variations in
transfection efficiency, as previously described (29).
GST pull-down experiment
The RIP 140 coding sequence was prepared by PCR and cloned into
a PCR II vector (Invitrogen, Carlsbad, CA). RIP 140
protein was synthesized in vitro using a T7 RNA
polymerase-based TNT-coupled reticulocyte lysate system
(Promega Corp.). The murine SF-1-GST fusion protein
construct, provided by Dr. Keith Parker, was expressed in bacteria
(32) and was used for pull-down assays and
coimmunoprecipitation. SF-1-GST fusion protein bound to
glutathione-Sepharose-4B beads was incubated for 3 h with 50 µl
in vitro-translated
[35S]methionine-labeled RIP 140 in a total
volume of 250 µl incubation buffer [50 mM
potassium phosphate (pH 7.4), 150 mM KCl, 1
mM MgCl2, 10% glycerol,
and 1% Triton-X]. Beads were collected by microcentrifugation and
washed three times. Washed beads were resuspended in 20 µl 2 x
SDS sample buffer, heated for 5 min, and pelleted in a microfuge, and
the supernatant was subjected to SDS-PAGE.
Cross-linking experiment and coimmunoprecipitation
Coimmunoprecipitations were performed using in
vitro-translated protein, as previous described (29).
The pBK SF-1 plasmid was used to generate radiolabeled SF-1 in a TNT
T7-coupled reticulocyte lysate system (Promega Corp.)
(29). 35S-Labeled SF-1 was incubated
with recombinant human DAX-1. RIP 140 protein was synthesized in
vitro using a T7 RNA polymerase-based TNT-coupled reticulocyte
lysate system described previously (Promega Corp.).
35S-Labeled RIP 140 was incubated with
recombinant GST-SF-1 or recombinant human DAX-1. The human DAX-1
protein was expressed in bacteria according to the instructions in the
supplier’s manual (Novagen, San Diego, CA). The reaction mixture was
diluted with binding buffer (20 mM HEPES, 5%
glycerol, 100 mM KCl, 5 mM
MgCl2, 0.5 mM
dithiothreitol, and 1 mM EDTA, in a final volume
of 25 µl) and cross-linked with a reversible cross-linking agent (5
mM dithiobis[succinimidyl propionate]) for
1 h at 25 C, then quenched with 0.22 M
lysine. Radioimmunoprecipitation was carried out by adding 500 µl
RIPA buffer (PBS, 1% Nonidet P-40, 0.5% sodium deoxycholate, 0.1%
SDS, 10 mg/ml phenylmethylsulfonylfluoride, 30 µg/ml aprotinin, and
10 µg/ml sodium orthovanadate) and 1 µl antiserum. After incubating
for 1 h at 4 C, 20 µl protein G-Sepharose 4FF (Amersham Pharmacia Biotech) were added, and the mixture was incubated for
1 h at 4 C. The bound complex was then washed four times with RIPA
buffer containing 2 M urea. The precipitated
proteins were eluted with 20 µl 2 x SDS sample buffer to
reverse the cross-links, resolved on a 12% SDS polyacrylamide gel,
dried, and visualized by autoradiography.
Coprecipitation with fusion protein
For coprecipitation, Y-1 cells or KGN whole cell extracts (1 mg)
in buffer [10 mM Tris-HCl (pH 8.0), 100 mM
NaCl, 0.5% Nonidet P-40, 1 mM dithiothreitol, 1
mM phenylmethylsulfonylfluoride, and 1 x proteinase
inhibitor cocktail; Compete Mini, Roche Molecular Biochemicals, Mannheim, Germany] were incubated with GST-SF-1
(100 ng) or human recombinant DAX-1 (100 ng), which have a His tag, for
1 h at 4 C in 500 µl IP buffer [50 mM Tris-HCl (pH
7.4), 100 mM NaCl, 1.5 mM EGTA, 0.1% Triton
X-100, 1 mM dithiothreitol, 1 mM
phenylmethylsulfonylfluoride, and 1 x proteinase inhibitor
cocktail]. After incubating, 20 µl glutathione-Sepharose 4B
(Amersham Pharmacia Biotech) or His-Bind Resin (Novagen)
were added, and the mixture was incubated for 1 h at 4 C. The
bound complex was then washed three times with IP buffer. The
precipitated proteins were eluted with 20 µl 2 x SDS sample
buffer and resolved on a 12% SDS-polyacrylamide gel. Western analysis
was performed using a rabbit polyclonal anti-DAX-1 IgG (Santa Cruz Biotechnology, Inc., Santa Cruz, CA) at a 1:1000 dilution
or a rabbit polyclonal anti-RIP 140 IgG (Affinity BioReagents, Inc., Golden, CA) at a 1:500 dilution.
Yeast two-hybrid interaction screening
A human testis cDNA library (CLONTECH Laboratories, Inc.) in the activation domain vector pACT2 was amplified using
the supplier’s recommended protocol. To identify SF-1 interacting
proteins, the human testis cDNA library in pACT2 was introduced into
the yeast reporter strain CG-1945 (MATa, ura3-52, his3-200,
ade2-101, lys2-801, trp1-901, leu2-3,112, gal4-542, gal80-538,
cyhr2,
LYS2::GAL1UAS-GAL1TATA-HIS3,
URA3::GAL417-mers(x3)-CYC1TATA-lacZ);
MATCHMAKER Two-Hybrid System 2, CLONTECH Laboratories, Inc.) bearing a plasmid expressing GAL4-SF-1 fusion. One x
106 transformants were plated onto a selective
synthetic medium lacking histidine, leucine, and tryptophan and grown
for 3–5 d at 30 C. A ß-galactosidase filter assay was used for
determining ß-galactosidase activity according to the recommended
protocol of the manufacturer. Plasmid DNA from all
His+ and LacZ+
colonies was isolated after electroporation of total yeast DNA into
Escherichia coli stain HB101 and selection of M9 medium
lacking leucine. After restriction analysis, cDNA inserts were
sequenced using a GAL4 AD sequencing primer.
Yeast two-hybrid interaction assays
Yeast two-hybrid interaction assays were used to verify the
interaction between SF-1 and RIP 140 and between RIP 140 and DAX-1.
Yeast strain Y187 (CLONTECH Laboratories, Inc.) with a
genotype of MAT
, ura3-52, his3-200, ade2-101, trp1-901,
leu2-3,112, gal4
, met-, gal80,
URA3::GAL1UAS-GAL1TATA-lacZ
was used for the assays. The plasmid GAL4 and GAD fusion constructs
were transformed into the Y187 strain using the YEASTMAKER Yeast
Transformation System (CLONTECH Laboratories, Inc.).
Quantitative liquid ß-galactosidase activity assays were performed
according to the protocol of the manufacturer (CLONTECH Laboratories, Inc.). Briefly, transformants were cultured in a
selective synthetic medium lacking leucine and tryptophan and grown for
2 d at 30 C (SF-1 and RIP 140 interaction). Transformants were
cultured in a synthetic medium medium lacking leucine and tryptophan
and grown overnight at 30 C. On the following day, 2 ml of the
overnight culture were transferred to 8 ml YPD medium and cultured for
3 h at 30 C (DAX-1 and RIP 140). One and a half milliliters of
culture were centrifuged, and the cells were washed with Z buffer
(CLONTECH Laboratories, Inc.). The cells were resuspended
with 300 µl Z buffer and used for the ß-galactosidase assay.
Activity was normalized to growth (OD600) and
assay time. pVA3–1 encodes DNA-BD/murine p53 protein in pAS2–1.
pTD1–1 encodes an AD/simian virus 40 large T antigen protein in pACT2.
The ß-galactosidase activity of pVA3–1 and pTD1–1 vector was used
as a positive control.
Data analysis
Values are presented as the mean ± SE.
Significance between experimental groups was determined by unpaired
t test. P < 0.05 was taken as the level of
significance.
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Results |
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). To
quantify the interaction between SF-1 and RIP 140, liquid cultures were
assayed for ß-galactosidase activity with o-nitrophenyl
ß-D-galactopyranoside. The empty vectors GAL4
and GAD did not activate the reporter gene. Cotransformation with a
GAL4 expression vector and a GAD-RIP 140 fusion expression vector or
GAL4-SF-1 and GAD did not increase reporter activity. However,
GAL4-SF-1 and GAD-RIP 140 induced a 6-fold greater activation of the
reporter gene compared with the activity observed when GAL4 and GAD
expression vectors were cotransformed into yeast strain Y187 (Fig. 1). These results suggest that there is
interaction between SF-1 and RIP 140 in vivo.
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). In
vitro-translated [35S]RIP 140 was mixed
with GST or GST-SF-1 and then subjected to SDS-PAGE and
autoradiography. These experiments revealed that RIP 140 interacts
directly with GST-SF-1, but not with GST. Coimmunoprecipitation was
performed to confirm the physical interaction between RIP 140 and SF-1
(Fig. 2B). [35S]RIP 140 and GST-SF-1 fusion
proteins were incubated and cross-linked with dithiobis[succinimidyl
propionate], a bifunctional reversible cross-linker. The protein
complexes were immunoprecipitated with RIP 140 antibody, SF-1
antiserum, or preimmune serum and protein G-Sepharose. Washed beads
were boiled in SDS sample buffer to reverse the cross-links.
35S-Labeled RIP 140 and GST-SF-1 complexes were
precipitated with the SF-1 antibody and RIP 140 antibody, but not with
preimmune serum. Moreover, unprogrammed reticulocyte lysate did not
yield an immunoprecipitation radioactive band with the SF-1 or RIP 140
antiserum. These results confirm the interaction between SF-1 and RIP
140 in vitro.
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). To quantify the interaction
between DAX-1 and RIP 140, liquid cultures were assayed for
ß-galactosidase activity. Cotransformation with GAL4-DAX-1 and
GAD-RIP 140 induced a 1.6-fold greater activation of the reporter gene
compared with the activity observed with GAL4 and GAD vectors (Fig. 3). Even though RIP 140 has a low
affinity interaction with DAX-1, these results indicate that there is
interaction between DAX-1 and RIP 140 in vivo.
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).
[35S]RIP 140 and human recombinant DAX-1
protein were incubated and cross-linked with dithiobis[succinimidyl
propionate]. The protein complexes were immunoprecipitated with DAX-1
antibody or preimmune serum and protein G-Sepharose.
[35S]RIP 140 and DAX-1 complexes were
precipitated with the DAX-1 antibody, but not with preimmune serum.
Transcription factors, 35S-labeled Oct-1 as a
negative control, was not precipitated with the DAX-1 antibody. The
immunoprecipitation results showed that there is a direct interaction
between DAX-1 and RIP 140 in vitro.
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).
35S-Labeled SF-1 and DAX-1 complexes were
precipitated with the DAX-1 antibody. The immunoprecipitation results
showed that there is also a direct interaction between DAX-1 and SF-1
in vitro.
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). Whole cell extracts from mouse Y-1
cells or human granulosa-like tumor cells, KGN cells, were
incubated with GST-SF-1 or His-tagged human DAX-1 recombinant protein.
The protein complex was precipitated with glutathione-Sepharose-4B or
His-Bind resin. The protein complexes were analyzed on a Western blot
using DAX-1 antibody or RIP 140 antibody. As shown in Fig. 6A, the
DAX-1 antibody detected a specific band at 55 kDa in Y-1 cells and SKG
cells (lanes 1 and 4). The DAX-1 protein was precipitated by GST-SF-1
fusion protein in both Y-1 cells and KGN cells (lanes 3 and 6). This
coprecipitation result presented DAX-1-interacted SF-1 in steroid
hormone-producing cells. The RIP 140 antibody detected 140 kDa in Y-1
cells and KGN cells in Fig. 6B (lanes 1 and 6). The RIP 140 protein was
precipitated by GST-SF-1 fusion protein (lanes 3 and 7) and His-tagged
DAX-1 fusion protein (lanes 5 and 10). The coprecipitation results
showed that RIP 140 interacted with DAX-1 and that RIP 140 interacted
with SF-1 in steroid-producing cells. The coprecipitation results
showed interactions between SF-1 and DAX-1, SF-1 and RIP 140, and DAX-1
and RIP 140 in cells. These results showed that DAX-1 physically
interacts with RIP 140 and SF-1 to control the human StAR promoter.
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). pGL2 StAR,
which was constructed from the -235 to +39 fragment, contains two
SF-1-binding sites (-105 to -96 and -43 to -36). To determine
whether the inhibitory effect of RIP 140 on StAR promoter activity is
dependent upon the presence of SF-1, the RIP 140 expression vector and
pGL2StAR were cotransfected into COS-1 cells,
which do not have endogenous SF-1, with (Fig. 8A) or without (Fig. 8B) an SF-1
expression vector. When COS-1 cells were transfected with the RIP 140
expression vectors in the absence of SF-1, basal and cAMP-stimulated
pGL2StAR promoter activities were not affected.
However, the introduction of exogenous RIP 140 resulted in a
dose-dependent decrease in pGL2StAR promoter
activity in both the presence and absence of 1 mM
8-bromo-cAMP in COS-1 cells transfected with the SF-1 expression
vector. Thus, the action of RIP 140 on the StAR promoter is dependent
on SF-1.
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).
The basal activity of pTKLuc4xSF-1 increased in the presence of a
small amount of the RIP 140 expression vector (Fig. 9B). However, the
cAMP induction of promoter activity was ablated at high concentrations
of the RIP 140 expression plasmid (Fig. 9B). The basal promoter
activity was increased by cotransfection with RIP 140 and DAX-1.
However, with 500 ng RIP 140 expression plasmid and 500 ng DAX-1
expression plasmid, basal promoter activity was not increased, and
cAMP-stimulated human promoter activity was blocked. That is, when both
RIP 140 and DAX-1 plasmids were transfected, cAMP induction of the StAR
promoter activity was inhibited at lower concentrations than when RIP
140 or DAX-1 was transfected alone (Fig. 9C).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The StAR protein is important for the synthesis of steroid hormones because it promotes cholesterol movement to the mitochondrial inner membranes, which is the rate-limiting step in steroidogenesis (9, 36). Tropic hormones (ACTH, LH, and FSH) regulate steroid hormone synthesis through several signal transduction pathways, including cAMP-dependent PKA, Ca2+/calmodulin-dependent protein kinase, PKC, and mitogen-activated protein kinase. Human StAR gene expression is increased by a cAMP analog, 8-bromo-cAMP (37). The promoter of human StAR is also stimulated by a cAMP analog, and SF-1 plays a role in controlling the cAMP-stimulated promoter activity (16). DAX-1 is one of the transcription factors that suppresses StAR gene promoter activity (26, 38), although the mechanism of suppression is not clear. DAX-1 has been reported to regulate human StAR gene transcription by binding to a hairpin structure in the proximal promoter, causing allosteric inhibition of the binding site of SF-1 (26). It has also been reported that DAX-1 interacts directly with SF-1 and inhibits the transcriptional activity of SF-1 (34, 35, 39). 8-Bromo-cAMP-stimulated synthesis of human StAR mRNA in human ovarian cells was inhibited by cycloheximide (37, 40), suggesting that newly synthesized proteins are required for cAMP-stimulated StAR gene transcription. The transcriptional activity of SF-1 appears to require direct interaction with other transcription factors. Indeed, SF-1 has been shown to interact with Sp1 to control human StAR expression (29). Although cAMP-induced promoter activity was not completely inhibited by 2 µg of the transfected RIP 140 expression vector, the RIP 140 expression vector transfected into Y-1 cells, which have endogenous SF-1, decreased basal and cAMP-stimulated human StAR promoter activities with increasing amounts of the RIP 140 vector. Interaction of other factors with RIP 140 is needed to repress the cAMP-induced StAR promoter activity. Although RIP 140 did not affect cAMP induction of the human promoter activity, StAR promoter activity decreased after cotransfection of RIP 140 and SF-1 expression vectors into COS-1 cells, which do not express SF-1. Thus, the inhibitory effect of RIP 140 on the human StAR promoter activity is dependent on the presence of SF-1.
When transfected with the DAX-1 expression vectors alone, basal and cAMP-stimulated promoter activities of pTKLuc4xSF-1 were not repressed at a low concentration of the transfected plasmid. Our results are consistent with the reported finding that DAX-1 is incapable of repressing SF-1 action through a single SF-1 site even though SF-1 trans-activation is present (41). When transfected with the DAX-1 or RIP 140 expression vector alone, cAMP-stimulated promoter activity of pTKLuc4xSF-1 was ablated at a high concentration of the transfected plasmid. However, the cAMP-stimulated promoter activity was inhibited when both RIP 140 and DAX-1 expression plasmids were cotransfected at low concentrations. These results demonstrate a functional significance of RIP 140, SF-1, and DAX-1 interactions in terms of control of human StAR promoter activity.
A coactivator is defined as a molecule that interacts with nuclear receptors and enhances their promoter activities, whereas a corepressor is defined as a molecule that lowers transcription. RIP 140 can function as an activator or a repressor depending on the cell environment, the interacting nuclear receptor, and the promoter. RIP 140 has a biphasic effect on ER-mediated reporter gene expression. At a low level of RIP 140, transcription of an ER gene increased, but it was strongly suppressed at high levels of RIP 140 plasmid (1). Our results are consistent with those findings, in that StAR promoter activity was increased when small amounts of RIP 140 plasmid were transfected, but was inhibited when a large amount of RIP 140 plasmids was transfected. RIP 140 suppressed the promoter activity in the basal and cAMP-stimulated states in a dose-dependent manner in Y-1 cells, which have endogenous SF-1. However, in COS-1 cells, which do not have endogenous SF-1, RIP 140 did not inhibit StAR promoter activity. With increasing amounts of RIP 140 and DAX-1 plasmids, cAMP-stimulated promoter activity was inhibited at lower concentrations than when RIP 140 or DAX-1 was transfected alone. This synergism may be due to inhibition of SF-1 function by the enhanced action of DAX-1. On the other hand, at lower plasmid concentrations, basal promoter activity was increased, possibly because RIP 140 stimulated SF-1 trans-activity action and prevented the inhibitory action of DAX-1.
In conclusion, the present study has provided evidence of physical interaction between RIP 140, SF-1, and DAX-1 and evidence of a role of these interactions in the control of human StAR gene transcription. The effects of RIP 140 on StAR promoter activity are dose dependent and dependent on the presence of SF-1.
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Acknowledgments |
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Footnotes |
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Received December 20, 2000.
Accepted for publication April 6, 2001.
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