ArticleMolecular and cellular biology1992
Novel DNA-binding proteins regulate intestine-specific transcription of the sucrase-isomaltase gene.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 117 citations in OpenAlex.
- α-Amylase expressed in human small intestinal epithelial cells is essential for cell proliferation and differentiation.Journal of cellular biochemistry · 2020Article
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- Extending the functions of the homeotic transcription factor Cdx2 in the digestive system through nontranscriptional activities.World journal of gastroenterology · 2015Review
- CDX2 is an amplified lineage-survival oncogene in colorectal cancer.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Biology of Barrett's esophagus and esophageal adenocarcinoma.Gastrointestinal endoscopy clinics of North America · 2011Review
- Beta-catenin/TCF4 transactivates miR-30e during intestinal cell differentiation.Cellular and molecular life sciences : CMLS · 2010Article
- Genome-wide analysis of CDX2 binding in intestinal epithelial cells (Caco-2).The Journal of biological chemistry · 2010Article
- Cdx genes, inflammation, and the pathogenesis of intestinal metaplasia.Progress in molecular biology and translational science · 2010Review
- Enhanced expression of resistin-like molecule beta in human colon cancer and its clinical significance.Digestive diseases and sciences · 2009Article
- A novel colonic repressor element regulates intestinal gene expression by interacting with Cux/CDP.Molecular and cellular biology · 2002Article
- Activity of hepatocyte nuclear factor 1alpha and hepatocyte nuclear factor 1beta isoforms is differently affected by the inhibition of protein phosphatases 1/2A.The Biochemical journal · 2001Article
- Interaction between the homeodomain proteins Cdx2 and HNF1alpha mediates expression of the lactase-phlorizin hydrolase gene.The Biochemical journal · 2000Article
- A novel therapy for colitis utilizing PPAR-gamma ligands to inhibit the epithelial inflammatory response.The Journal of clinical investigation · 1999Article
- Two HNF-1 binding sites govern the glucose repression of the human sucrase-isomaltase promoter.The Biochemical journal · 1998Article
- Control of gene expression in intestinal epithelial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1998Review
- Activation of enhancer elements by the homeobox gene Cdx2 is cell line specific.Nucleic acids research · 1997Article
- Regulation of lactase-phlorizin hydrolase gene expression by the caudal-related homoeodomain protein Cdx-2.The Biochemical journal · 1997Article
- Article
- The transcriptional activator hepatocyte nuclear factor 6 regulates liver gene expression.Molecular and cellular biology · 1996Article
- A limited upstream region of the human sucrase-isomaltase gene confers glucose-regulated expression on a heterologous gene.The Biochemical journal · 1996Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sucrase-isomaltase (SI) is an enterocyte-specific gene which exhibits a complex pattern of expression during intestinal development and in the adult intestinal mucosa. In the studies described in this report, we demonstrate that enterocyte-specific transcription of the SI gene is regulated by an evolutionarily conserved promoter that extends approximately 180 bp upstream of the transcription start site. DNase I footprint analysis allowed the identification of three nuclear protein-binding sites within the SI promoter (SIF1, SIF2, and SIF3 [SI footprint]), each of which acted as a positive regulatory element for transcription in intestinal cell lines. SIF1 was shown to bind nuclear protein complexes present in primary mouse small intestinal cell and in an intestinal cell line (Caco-2). However, SIF1-binding proteins were absent in a variety of other epithelial and nonepithelial cells. In vitro mutagenesis experiments demonstrated that the SIF1 site is required for high-level promoter activity in intestinal cells. The SIF3 element formed prominent binding complexes with intestinal and liver nuclear extracts, whereas nuclear proteins from other epithelial and nonepithelial cells formed weaker complexes of different mobilities. The SIF2 element bound nuclear proteins in a pattern similar to that of SIF3, and cross-competition studies suggested that SIF2 and SIF3 may bind the same nuclear proteins. Taken together, these data have allowed the identification of novel DNA-binding proteins that play an important role in regulating intestine-specific transcription of the SI gene.
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