Molecular Human Reproduction, Vol. 8, No. 2, 167-175,
February 2002
© 2002 European Society of Human Reproduction and Embryology
Uterine physiology |
Cloning and characterization of the human oviduct-specific glycoprotein (HuOGP) gene promoter*
Department of Obstetrics and Gynaecology, Queen Mary Hospital, The University of Hong Kong, Hong Kong, People's Republic of China
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Oviduct-specific glycoprotein (OGP) is a high molecular weight glycoprotein belonging to the chitinase protein family. OGPs are found to associate with the zona pellucida and plasma membrane of the oocyte and developing embryo. Recent studies have shown that OGP plays an important role in pre-fertilization reproductive events (i.e. sperm capacitation, sperm–zona binding and zona penetration). To have a better understanding of human OGP (HuOGP) gene expression, a 3.3 kb DNA fragment containing the 5'-flanking and the intron I region of the HuOGP gene was isolated. DNA sequence analysis of the HuOGP putative promoter revealed little homology with its hamster and mouse ogp gene counterparts. One transcription initiation site was found 12 nucleotides upstream of the first ATG codon of the HuOGP gene. The HuOGP gene promoter lacked typical CAAT or GC boxes, but contained eight half estrogen-responsive elements (ERE) and an imperfect ERE (iERE; 5'-GGTCANNNTGACT-3') site. Deletion mutants of the 3.3 kb DNA fragment were generated and fused to a promoterless ß-galactosidase (ß-Gal) gene. Transfection studies revealed that in the presence of 100 nmol/l estradiol-17ß (E2), a minimal 0.3 kb promoter construct (pH–298/+25ßGal) mediated a high level of ß-Gal expression in immortalized human oviductal epithelial OE-E6/E7 cells, but not in MCF-7 and CHO-K1 cells. By electromobility shift assay and specific estrogen receptor antibodies, we demonstrated that estrogen receptor ß present in the OE-E6/E7 cells binds to the iERE. These findings allow a better understanding of the regulation of OGP gene expression in the human oviduct.
cloning/estrogen/human/oviduct-specific glycoprotein/promoter
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The mammalian oviduct provides an environment that supports the processes of fertilization, early embryonic development and delivery of a viable embryo to the uterus (Boatman, 1997
). Although normal fertilization and preimplantation development are possible in vitro, our laboratory and others have demonstrated that human embryos co-cultured with oviductal cells have better morphology in terms of reduced fragmentation (Bongso et al., 1989; Yeung et al., 1992; Morgan et al., 1995), better morphological characteristics and higher cleavage (Morgan et al., 1995), blastulation (Bongso et al., 1989; Wiemer et al., 1993; Liu et al., 1995; Xu et al., 2000) and hatching rates (Yeung et al., 1992; Xu et al., 2000). However, the underlying molecular mechanisms by which oviductal factors affect mammalian fertilization and embryo development remain elusive (Lee et al., 2001a).
Recent studies suggest that oviduct-specific glycoprotein (OGP) may play a role in fertilization (Verhage et al., 1998). OGP is present in the oviduct; it is secreted from the oviductal epithelial cells and attaches itself to the ovulated oocyte and early embryo during their transit in the oviduct (Malette et al., 1995; O'Day-Bowman et al., 1996). This glycoprotein also associates with blastomeres (Kan et al., 1993; Murray and Messinger, 1994), the external surface of the cilia of oviductal cells, and the lining of the endometrium upon entry into the lumen (Léveillé et al., 1987; Martoglio and Kan, 1996). OGP enhances sperm binding to the zona pellucida in a species-specific manner (O'Day-Bowman et al., 1996; Schmidt et al., 1997a; Martus et al., 1998), while the blocking of OGP with antibodies significantly decreases species-specific sperm binding onto oocytes in vitro (Schmidt et al., 1997b). The cDNAs encoding human OGP (Arias et al., 1994) and its homologues in baboon (Donnelly et al., 1991), mouse (Sendai et al., 1995), hamster (Suzuki et al., 1995), sheep (DeSouza and Murray, 1995) and porcine (Buhi et al., 1996) have been cloned and partially characterized. The presence of human OGP (HuOGP) around the time of ovulation suggests that OGP may play a role in fertilization and/or early embryonic development (O'Day-Bowman et al., 1995). It has also been proposed that the conserved chitinase/mucin-like domains of OGP may interact with the zona pellucida, thereby protecting the preimplantation embryo in the reproductive tract (Malete et al., 1995).
Recently, the mouse ogp gene has been mapped to chromosome 3 (Takahashi et al., 2000) and the HuOGP gene has been located on chromosome 1 by linkage homology (Lyon et al., 1997). The function of the mouse OGP gene promoter has been partially characterized (Takahashi et al., 2000), but the hamster (Merlen and Bleau, 2000) and human counterparts (R.C.Jaffe, GenBank U58001) have not. Transient transfection studies have demonstrated that the mouse OGP promoter is responsive to estradiol-17ß (E2) induction in the estrogen receptor (ER)-positive MCF-7 cells, but not in the ER-negative CHO-K1 cells (Takahashi et al., 2000).
To further understand the regulation and the hormonal control of OGP expression in humans, we report here the cloning and characterization of HuOGP gene promoter. Chimeric promoter constructs were transiently transfected into ER-positive and ER-negative cell lines in order to identify the minimal promoter region that responds to estrogen stimulation. Furthermore, to define the role of the imperfect estrogen-responsive element (iERE) in the estrogen regulation of the HuOGP promoter, electromobility shift assays were carried out.
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Plasmids, bacteria and reagents
pBlue-TOPO reporter vector and pGEM-T easy PCR cloning vectors were purchased from Invitrogen (Carlsbad, CA, USA) and Promega (Madison, WI, USA) respectively. DH5
competent cells were prepared as previously described (Sambrook et al., 1989). Restriction endonucleases, T4 DNA ligase and T4 polynucleotide kinase were purchased from New England Biolabs (Beverly, MA, USA). Bradford reagent was from Bio-Rad (Hercules, CA, USA). Other reagents were from Sigma (St Louis, MO, USA).
Isolation of the 5'-flanking region of the HuOGP gene
The 5'-flanking region of the HuOGP gene was isolated using the human GenomeWalker kit (Clontech, Palo Alto, CA, USA) and ExpandLong DNA polymerase (Boehringer Mannheim, Germany). A two-step PCR was performed for the five genomic libraries (Clontech) as previously described (Lee et al., 2000). In brief, the primary PCR (seven cycles of 94°C for 25 s and 72°C for 4 min, then 32 cycles of 94°C for 25 s and 67°C for 4 min, and a final extension step at 67°C for 4 min) was done in a final volume of 50 µl with 10 pmol of a gene-specific primer 1 (HuOGP-3; 5'-TGGCCGACTGTGTGCCCAGTTGGTG-3', at position +120 to +96 of the HuOGP cDNA sequence, accession no.: NM002557) and adaptor primer 1 (5'-GTAATACGACTCACTATAGGGC-3').
The secondary PCR (five cycles of 94°C for 25 s and 72°C for 4 min, then 22 cycles of 94°C for 25 s and 67°C for 4 min, and a final extension step at 67°C for 4 min) was done using 1 µl of the primary PCR product, gene-specific primer 2 (HuOGP-2; 5'-ATCGTGGTGTTTCAGCACAAGAACC-3', at position +66 to +52 of the HuOGP cDNA; accession no. NM002557) and nested adaptor primer 2 (5'-ACTATAGGGCACGCGTGGT-3'). PCR products were gel-purified and subcloned into pGEM-T easy vector (Promega) or pBlue-TOPO reporter vector. Both strands of the cloned fragments were sequenced using the ABI prism 310 Genetic Analyser (Perkin-Elmer Biosys., Foster City, CA, USA). The promoter fragments were assembled using DNasis computer program (Hitachi Software Engineering, San Bruno, CA, USA) and the DNA sequence was analysed using on-line TFSEARCH (http://pdap1.trc.rwcp.or.jp/research/db/TFSEARCH.html), GCG SeqWeb and ClustalW (http://www.ebi.ac.uk/clustalw) programs.
PCR amplification of human genomic DNA
To confirm the cloned DNA fragment is continuous in the human genome, several primers (HuOGP-19, -16, -17, -5, -6R and -1) complementary to the promoter and the coding region of the HuOGP (Figure 1) were synthesized. PCR (94°C for 1 min, then 30 cycles of 94°C for 1 min, 60°C for 1 min and 72°C for 4 min) was performed in a final volume of 50 µl. The PCR products were resolved on a 1% agarose gel.
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Location of the transcriptional start site
Human oviduct was removed from patients with their consent during their total abdominal hysterectomies for uterine fibroids. This study was approved by the ethics committee at the University of Hong Kong. Total RNA from human oviduct and from an immortalized human oviductal epithelial cell line (OE-E6/E7) (Lee et al., 2001b
) were isolated using TRIzol reagent (Gibco BRL, Grand Island, NY, USA). In a 10 µl reaction mixture, 5 µg of total RNA was annealed with a 32P-labelled downstream primer (PEA-H1, 5'-CAACCCACAGCAACAGCT-3') in 1X First Strand Buffer (50 mmol/l Tris-HCl; pH 8.3, 75 mmol/l KCl, 3 mmol/l MgCl2) at 58°C for 20 min and then followed by 10 min at room temperature. The annealed mixture was mixed with 10 µl of reaction buffer [50 mmol/l Tris-HCl; pH 8.3, 75 mmol/l KCl, 3 mmol/l MgCl2, 50 mmol/l dithiothreitol (DTT), 1 mmol/l dNTPs] and 200 U of SuperScript II RNase H- reverse transcriptase (Gibco BRL), and incubated at 47°C for 30 min. The reaction was stopped by the addition of loading buffer. A total of 10 µl of the samples were resolved by 5% denaturing polyacrylamide gel electrophoresis. As a size standard, a sequencing reaction was carried out for pH–1402/+25ßGal (see below) using 32P-labelled PEA-H1 primer and loaded next to the primer extension product.
Plasmid constructs for reporter assay
Reporter assays were performed with HuOGP promoter fragments fused to a ß-galactosidase reporter gene in pBlue-TOPO cloning vector (Invitrogen). Promoter fragments of sizes 2.7 kb (pH–2633/+25ßGal), 2.0 kb (pH–1976/+25ßGal), 1.4 kb (pH–1402/+25ßGal), 0.8 kb (pH–777/+25ßGal) and 0.3 kb (pH–298/+25ßGal) were generated and transfected into human oviductal epithelial OE-E6/E7, human breast cancer MCF-7 and Chinese hamster ovary CHO-K1 cells. The nucleotide sequences of all chimeric constructs were confirmed by DNA sequencing.
Cell culture and transfection
The CHO-K1 cells were cultured in HAM/F-12 medium (Gibco BRL, Gaithersburg, MD) supplemented with 10% fetal bovine serum, penicillin (50 IU/ml), streptomycin (50 IU/ml) and 2 mmol/l L-Glutamine at 37°C and 5% CO2. The MCF-7 and OE-E6/E7 cells were cultured in DMEM/F-12 medium (Gibco BRL, Gaithersburg, MD, USA) with the same supplements. Cell transfection experiments were carried out with the test plasmid (promoter fragments fused with a ß-galactosidase reporter gene) using FuGene 6 transfection reagent (Roche Molec. Biochem., Germany) according to the manufacturer's protocol. Briefly, about 2x105 cells were grown overnight in a 35 mm culture dish in 10% charcoal-stripped fetal bovine serum containing medium. For each dish, 100 µl of OPTI-MEM containing 3 µl of FuGene 6 was mixed with 1 µg of test plasmid for CHO-K1 and 2 µg of test plasmid for MCF-7 and OE-E6/E7 cells, and incubated for 15 min at room temperature. FuGene 6-DNA-complex was added slowly to each dish, and the dish was incubated at 37°C for 48 h with or without 100 nmol/l estradiol-17ß (E2). The ß-galactosidase enzyme was quantified using ß-Gal ELISA kits (Roche) in accordance with the manufacturer's protocols. In all the transfection experiments, positive (pCMVß-Gal) and negative (pBlue-TOPO) control experiments were included to evaluate the transfection efficiency. Our preliminary experiments also showed no difference in transfection efficiency when different chimeric constructs were co-transfected with the pCAT-3 control vector. Statistical analysis was performed using analysis of varience and Student–Newman–Keul's test.
Electromobility shift assay (EMSA)
Nuclear protein extracts from OE-E6/E7 cells were prepared as described (Dignam et al., 1983) and quantitated by the Bradford assay (Bio-Rad). The iERE probe (5'-GTTCTGGGGTCACTGTGACTCTCATAA-3', HuOGP gene promoter) was labelled with [
-32P]ATP (Amersham Pharmacia Biotech., Piscataway, NJ, USA). Unincorporated nucleotides were removed by spin column in the Tris-EDTA buffer. A total of 10 µg of OE-E6/E7 nuclear extract was incubated with or without ER (F-10) or ERß (N-19) antibodies (Santa Cruz Biotech. Inc., Santa Cruz, CA, USA) in 1X binding buffer (4% glycerol, 1 µg poly(dI-dC).(dI-dC), 10 mmol/l Tris-HCl (pH 7.5), 50 mmol/l NaCl, 1 mmol/l MgCl2, 0.5 mmol/l EDTA and 0.5 mmol/l DTT) in a 50 µl reaction for 20 min at 4°C. Then, the radiolabelled probe was added and incubated for a further 20 min at room temperature. The reaction products were analysed on a 6% non-denaturing polyacrylamide gel. The gels were dried under vacuum and autoradiographed on Kodak MS films overnight at –70°C.
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Results |
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Using human GenomeWalker kit, we amplified fragments from all of the five libraries: EcoRV (0.4 kb), ScaI (0.4 kb), DraI (0.45 kb), PvuII (1.8 kb) and SspI (1.8 kb). DNA sequence analysis confirmed that they were identical at the 3' ends. A short intron I containing a DNA sequence of 588 bp was identified and the exon–intron splice site obeyed the GT/AG rule (Breathnach and Chambon, 1981
). In order to obtain a further upstream promoter region of HuOGP, another round of genome walking was carried out using gene-specific primer 3 (HuOGP-6; 5'-CCCATATGGTAGCAGCATTC-3', at position –298 to –279) and adaptor primer 1, and followed by gene-specific primer 4 (HuOGP-12; 5'-GACCCAGTGTTGCTGGATCCTTCAG-3', at position –875 to –851) and adaptor primer 2 for PCR amplifications. We successfully isolated upstream fragments from EcoRV (0.8 kb) and ScaI (1.8 kb) libraries. Sequence analysis confirmed that these fragments were located distal to the putative promoter region of the HuOGP gene. The complete 3.3 kb fragment was generated by PCR and sequenced. Putative transcription factor binding sites were identified (Figure 1A
). To confirm that the cloned DNA fragments are continuous in human genomic DNA, several primers (HuOGP-19, -16, -17, -5, -6R and -1) complementary to the promoter and the coding region of the HuOGP DNA were synthesized. We found that all the PCR products were of the expected sizes (Figure 1B), confirming that the isolated fragments are indeed located at the 5'-flanking region of the HuOGP gene in human genomic DNA.
Sequence analysis of the 5'-flanking region revealed a putative TATA-box (TATAA) (Figure 1A). Additionally, an imperfect estrogen-responsive element (5'-GGTCANNNTGACT-3') was found at position –150 to –162, and several half-ERE sites were found throughout the putative promoter region (Figure 2A). Interestingly, two half-ERE sites were also found in the intron I of human and mouse, but not in the hamster ogp gene. Alignment of the human, mouse and hamster imperfect ERE (5'-GGTCANNNTGACT-3') sites and the flanking DNA sequences suggested a conserved change of the nucleotide (C to T) at the 3'-end, whereas the proximal 5'- and 3'-flanking DNA sequences shared little homology among them (Figure 2B). Furthermore, a sequence comparison of the entire 5'-flanking region of the human OGP promoter with the mouse and hamster counterparts using the GCG SeqWeb program did not show any significant homology.
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The transcription start site of HuOGP was determined by a primer extension assay using PEA-H1 and human oviduct RNA. The primer extension product indicated a unique transcription start site, 12 nucleotides ahead of the translation start site, and this agrees with the published data (Arias et al., 1994
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Chimeric constructs containing various lengths of the HuOGP promoter were tested in the ER-positive OE-E6/E7, MCF-7 and the ER-negative CHO-K1 cells (Figure 3). The activity of pH–298/+25ßGal (0.3 kb) in OE-E6/E7 was significantly (11.5-fold) increased in the presence of 100 nmol/l E2 when compared with that in cells without E2 treatment (Figure 3A). The expression of the fragment was 18-fold higher (P < 0.05) than that with the control vector in the same cell line. The activity of pH–777/+25ßGal (0.8 kb) was similarly increased almost 9-fold in the presence of 100 nmol/l E2 and was 22-fold higher than that of the control. However, further increases in the size of the HuOGP promoter constructs decreased the transactivation activity. In the presence of E2, there was a significant difference (P < 0.05) in the activity of pH–298/+25ßGal (0.3 kb) when compared with that of pH–1976/+25ßGal (2.0 kb) and pH–2633/+25ßGal (2.6 kb) constructs in the OE-E6/E7 cell line. On the other hand, all of the chimeric constructs showed minimal transactivation activities in the MCF-7 and CHO-K1 cell lines irrespective of their length and E2 treatment (Figure 3B,C).
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EMSA of the iERE using OE-E6/E7 nuclear extract showed the presence of two retarded bands (Figure 4
). In order to confirm the specific protein–DNA interaction, we used specific antibodies in the EMSA. The lower retarded band disappeared in the presence of ERß antibody, but not in the presence of ER antibody. Conjointly, a supershift band was observed on the top, suggesting that the lower retarded band contained ERß. The other retarded band might represent a complex between other unidentified protein(s) and the iERE.
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Discussion |
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OGP is a high molecular weight glycoprotein secreted by the epithelial cells in both ampullary and isthmic regions of the oviduct (O'Day-Bowman et al., 1995
). The role of OGP in fertilization and early embryo development remains elusive. In the present study, we used a PCR-based genomic amplification protocol to isolate a 3.3 kb DNA fragment containing the 5'-flanking region and intron I of the human OGP gene and demonstrated that the cloned fragment is continuous on the human genomic DNA. During preparation of this manuscript, a 153 kb cosmid clone containing the human OGP genomic sequence (accession number AL390195) was released. In comparison with the human OGP cDNA sequence (accession numbers U58001–U58010), 10 introns of sizes from 103 bp (intron III) to 3151 bp (intron IX) were located and the intron–exon boundaries followed the GT/AG rule (Breathnach and Chambon, 1981).
Gene expression is frequently controlled at the level of transcription (de la Brousse and McKnight, 1993). The control region of typical eukaryotic genes comprises of proximal (core) and distal (enhancer) promoter regions. The core promoter region consists predominantly of two elements: the TATA-box and/or the Inr elements, which can be present either alternately (i.e. either TATA+Inr- or TATA-Inr+) or in limited cases, simultaneously (TATA+Inr+) (Novina and Roy, 1996). The intrinsic responsiveness of a given gene may be determined by the core promoter (Merli et al., 1996). In the hamster and mouse ogp promoters, no typical CAAT and TATA-box were found (Merlen and Bleau, 2000; Takahashi et al., 2000), while a consensus TATA-box was identified in the HuOGP promoter. The TATA-box is known to bind the basal level transcriptional complex via TATA-binding protein that determines the direction and start site of transcription (White and Jackson, 1992). It was also noted that no initiator sequence (Inr = YAYTCYYY, Y = pyrimidine) (Roeder, 1991) is present downstream of the HuOGP start site. Thus, the HuOGP promoter can be classified as a distinct promoter (Novina and Roy, 1996). In this study, the minimal 0.3 kb human OGP promoter displayed cell type-specificity and E2 responsiveness, while the larger promoters were less effective, suggesting that there is no enhancer region located distal to the promoter region. Moreover, DNA sequence comparison of the OGP promoters from human, hamster and mouse suggested very little similarity among them, although a stronger homology was found between the latter promoters.
It is well known that OGP synthesis is regulated by estrogen and is at a maximum during the late follicular phase of the menstrual cycle (Arias et al., 1994; O'Day Bowman et al., 1995). Computer analysis of our isolated 3.3 kb fragment demonstrated eight half-estrogen responsive elements and an iERE [5'-GGTCANNNTGACT-3' (the mutated nucleotide is underlined), position –162 to –150] at the 5'-flanking region of the HuOGP. Additionally, two half-ERE sites were found in the intron I of the human and mouse OGP genes but not in the hamster ogp gene. Although the role of these ERE sites remains elusive, we found that iERE (5'-GGTCAACTGTGACT-3') can form protein–DNA complexes using OE-E6/E7 nuclear extract in electromobility shift assays. The presence of two protein–DNA complexes instead of one suggests that other transcription factor(s) may be involved in the formation of the complexes. In fact, only one of the two complexes was identified by the ERß antibody in the supershift assay. Interestingly, the formation of a relative weak gel-shift band by the ERß–iERE complex suggests that other protein(s) might be necessary for strong protein–iERE interaction. However, the identity of this protein(s) remains elusive. The E2 responsiveness of the HuOGP promoter through the ERß and iERE interaction needs further investigation.
The functional activity and the E2 response of the human OGP promoter fragments were determined by transient transfection of the chimeric constructs in oviductal cells with estrogen receptor (OE-E6/E7) and cells of non-oviductal origins with (MCF-7) and without estrogen receptor (CHO-K1). It is known that primary human oviductal epithelial cell lines have a limited proliferative lifespan in culture. Hence, we used immortalized human oviductal epithelial cells established in our laboratory (Lee et al., 2001b) for the transfection study. A previous study using the mouse ogp promoter has demonstrated transactivation and E2 responsiveness in the ER-positive human breast cancer MCF-7 cells (Takahashi et al., 2000). However, the human promoter did not show transactivation activity in the CHO-K1 and MCF-7 cells, but did in OE-E6/E7 cells, suggesting that the promoter activity may be species and cell type-specific, and that the presence of the estrogen receptor is not the only requirement for transactivation. The latter may be because the OGP gene is normally suppressed in cells other than the oviductal cells. It would be interesting to determine if the mouse and hamster ogp promoters exhibit stronger transactivation in the immortalized human oviductal epithelial OE-E6/E7 cells compared with the human breast MCF-7 cells.
Transient transfection of the HuOGP chimeric constructs showed that a 0.3 kb fragment of the 5'-flanking region specifically directs the transcription of a reporter gene in the ER-positive OE-E6/E7 cells after E2 treatment. Coincidentally, this minimal promoter region contains an iERE site. However, increasing the size of the chimeric constructs (up to 2.7 kb) suppressed promoter activity and E2 responsiveness. As discussed above, the transfection activities of the human and mouse ogp promoters show a fundamental difference in the ER-positive cell lines (OE-E6/E7 and MCF-7 respectively). The 2.2 kb mouse ogp promoter showed similar transactivation and estrogen responsiveness to the minimal promoter (270 bp) in the MCF-7 cells (Takahashi et al., 2000). In contrast, increasing the length of the HuOGP promoter in this study suppressed promoter activity and E2 responsiveness. These results indicate the presence of potential silencing element(s) in the upstream region of the HuOGP promoter region to modulate promoter activity in vitro. Yet, whether it reflects the in-vivo situation and/or whether other distal regulatory element(s) are involved in regulation of OGP expression needs further investigation.
Several estrogen-responsive genes identified to date contain one or more imperfect EREs or multiple copies of the ERE half-site (Kato et al., 1995). Estrogen regulation via half-ERE sites has been reported in the chicken ovalbumin upstream promoter (COUP) (Kato et al., 1992), the human catechol-O-methyltransferase gene (Xie et al., 1999) and the human cathepsin D gene (Wang et al., 1997). An association between ER and a half-ERE via co-activators/orphan receptors such as COUP-TF has been demonstrated in the chicken ovalbumin upstream promoter (Klinge et al., 1997). However, the role of the half-ERE sites located at the distal part of HuOGP in regulating the gene expression is uncertain because elimination of these sites did not prevent E2-induced expression of the gene. Detailed EMSA and DNA footprinting studies will help us to delineate the role of the iERE/half-ERE sites in estrogen regulation of the OGP promoter in vitro and in vivo.
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Acknowledgements |
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The authors thank Dr S.W.Tsao, Department of Anatomy, The University of Hong Kong for the establishment of the immortalized OE-E6/E7 cells. We are obliged to J.F.C.Chow, K.L.Kwok and Y.L.Lee for their excellent technical assistance. The authors are also grateful to Drs H.G.Verhage and W.C.Buhi for their critique and valuable suggestions. This work was supported in part by a CRCG grant (10203102) of the University of Hong Kong and Hong Kong Research Grant Council (HKU7327/00M) to K.F.Lee.
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1 To whom correspondence should be addressed. E-mail: ckflee{at}hkucc.hku.hk
* Sequence data from this article have been deposited with the GenBank Database under the accession number AF189710.
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References |
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Submitted on March 27, 2001; resubmitted on August 20, 2001; accepted on November 16, 2001.
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