DNA binding and regulatory effects of transcription factors SP1 and USF at the rat amyloid precursor protein gene promoter

Hoffman, Peter W.; Chernak, Jeffrey M.

doi:10.1093/nar/23.12.2229

Cited by 53 publications

(45 citation statements)

References 20 publications

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“…Such motifs have been reported to be potential binding sites for basic helix-loop-helix (bHLH) transcription factors, c-myc, Myo D, and ubiquitous transcription factors USF-1 and USF-2 proteins (Maekawa et al 1991, Hoffman & Chernak 1995, Elnitski et al 1997, Gao et al 1997, Gupta et al 1997, Scholtz et al 1997. Previous studies have demonstrated that E2 transiently induces c-myc gene expression in MCF-7 cells, and a synthetic antisense c-myc oligonucleotide partially inhibited E2-induced growth of MCF-7 cells (Dubik et al 1987, Watson et al 1991.…”

Section: Discussionmentioning

confidence: 99%

Mechanism of transcriptional regulation of LRP16 gene expression by 17-β estradiol in MCF-7 human breast cancer cells

Zhao

Han²,

Q³

et al. 2005

Journal of Molecular Endocrinology

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LRP16 gene expression is induced by 17-estradiol (E2) via estrogen receptor alpha (ER ) in MCF-7 human breast cancer cells. A previous study also demonstrated that ectopic expression of LRP16 gene promoted MCF-7 cell proliferation. To explore the mechanism of hormone-induced LRP16 gene expression, the LRP16 gene promoter region (-2600 to -24 bp upstream of the LRP16 gene translation starting site) was analyzed in the present study by using different 58-truncated constructs, and a luciferase reporter. The 58-flanking sequence of -676 to -24 bp (pGL3-S5) was found to be E2-responsive. After exchange of the fragment from -213 to -24 bp with the TK gene proximal promoter region in pGL3-S5, E2 still induced reporter gene activity in MCF-7 and HeLa cells. Sequence analysis showed that the pGL3-S6 (-676 to -214) sequence contains two motifs that may contribute to E2-induced transactivation; namely, an estrogen-responsive element (ERE) half-site/Sp1 at -246 to -227 bp and an E-box site at -225 to -219 bp. Further deletion and mutation analysis of these two motifs indicated that both the 1/2 ERE and Sp1 binding sites were required for E2 action, while E-box deletion did not affect the luciferase activity in MCF-7 and HeLa cells. The results of gel mobility shift and chromatin immunoprecipitation assays confirmed that both ER and Sp1 were required for hormone-induced transactivation, which involved both ER and Sp1 directly binding to DNA. Taken together, these findings suggest that ER and Sp1 play a role in activation of the human LRP16 gene promoter.

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Section: Discussionmentioning

confidence: 99%

Mechanism of transcriptional regulation of LRP16 gene expression by 17-β estradiol in MCF-7 human breast cancer cells

Zhao

Han²,

Q³

et al. 2005

Journal of Molecular Endocrinology

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“…It has been shown that the ATF/CRE site is essential for the COX-2 expression induced by v-src, serum, and platelet-derived growth factor in NIH3T3 cells (21)(22)(23), whereas the E-box was required for COX-2 expression in rat ovarian granulosa cells in response to various hormones (18). When nuclear extracts of JWF2 cells were incubated with the radiolabeled ATF/ CRE⅐E-box oligonucleotides in the presence of wild-type, mutant, and consensus oligonucleotides of CREB (32) or E-boxbinding protein USF (33), the protein-DNA complexes were completely competed out by consensus USF oligonucleotides (Fig. 4A, seventh lane), whereas consensus ATF/CRE oligonucleotides had no significant effect on the binding (Fig.…”

Section: Murine Cox-2 Promoter Contains Two Positive Regulatorymentioning

confidence: 99%

Transcriptional Regulation of Cyclooxygenase-2 in Mouse Skin Carcinoma Cells

Kim

Fischer

1998

Journal of Biological Chemistry

188

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Many studies have suggested that overexpression of cyclooxygenase-2 (COX-2) contributes to the development of tumors in several tissues. COX-2 expression tends to be up-regulated in various types of tumors and transformed cell lines, and the overexpression of COX-2 is caused by enhanced transcription of the gene. In an attempt to characterize the signaling pathway leading to the overexpression of COX-2 in the mouse skin carcinoma cell line JWF2, we investigated cis-and transacting factors required for COX-2 expression and demonstrated a molecular mechanism by which COX-2 is expressed differentially in normal and neoplastic tissues. Two regions of the COX-2 promoter containing an E-box and nuclear factor IL6 site were identified as the positive regulatory elements through transient transfections with luciferase reporter vectors containing the various 5-flanking regions of the promoter. Moreover, electrophoretic mobility shift assays and cotransfection experiments showed that upstream stimulatory factors and CCAAT/enhancer-binding proteins (C/EBPs) bind to the E-box and nuclear factor IL6 site, respectively, and functionally transactivate the COX-2 promoter. We also found that C/EBP isoforms are expressed differentially during mouse skin carcinogenesis, suggesting that overexpression of COX-2 in tumors may be caused by a change in C/EBP expression levels. Prostaglandins (PGs)1 are involved in many normal and pathophysiological responses (1). As a rate-limiting enzyme in the synthesis of PGs, cyclooxygenase (COX)

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“…The proximal APP promoter region also contains an sp1 site (25,26) and two nuclear factor binding domains designated as APB␣ and APB␤ (27). The factors that bind to these domains display sequence specificity, and it was demonstrated that the primary cellular factor that binds to APB␣ is a heterodimer of USF43 and USF44 (25, 28 -30).…”

mentioning

confidence: 99%

The Zinc Finger Protein CTCF Binds to the APBβ Domain of the Amyloid β-Protein Precursor Promoter

Vostrov

Quitschke

1997

Journal of Biological Chemistry

174

159

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The promoter of the amyloid ␤-protein precursor (APP) gene directs high levels of cell type-specific transcription with 94 base pairs 5 to the main transcriptional start site. An essential activator domain in this proximal APP promoter is a nuclear factor binding site designated as APB␤. The recognition domain for the APB␤ binding factor is located between position ؊93 and ؊82 relative to the main transcriptional start site.The nuclear factor that binds to the APB␤ site was partially purified by multiple steps of ion exchange and hydroxyapatite chromatography. Based on UV crosslinking results, a protein with an apparent molecular mass of 140 kDa was selected as the putative APB␤ binding protein. After the final purification step consisting of preparative SDS-polyacrylamide gel electrophoresis, partial peptide sequences were obtained that completely matched the transcriptional factor CTCF. This protein is a known regulator of c-myc and lysozyme gene expression, and it binds to a variety of diverse DNA sequences.The binding of CTCF to the APB␤ domain was further established by competition with CTCF binding oligonucleotides in mobility shift electrophoresis. The identity was also confirmed by the observation that the APB␤ binding factor is recognized by antibodies against Cand N-terminal sequences of CTCF. In addition, oligonucleotide competition during in vitro transcription affirmed that CTCF acts as a transcriptional activator in the APP gene promoter.

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DNA binding and regulatory effects of transcription factors SP1 and USF at the rat amyloid precursor protein gene promoter

Cited by 53 publications

References 20 publications

Mechanism of transcriptional regulation of LRP16 gene expression by 17-β estradiol in MCF-7 human breast cancer cells

Mechanism of transcriptional regulation of LRP16 gene expression by 17-β estradiol in MCF-7 human breast cancer cells

Transcriptional Regulation of Cyclooxygenase-2 in Mouse Skin Carcinoma Cells

The Zinc Finger Protein CTCF Binds to the APBβ Domain of the Amyloid β-Protein Precursor Promoter

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