1
40
4
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
Pages
63–73
Issue
1
Volume
1583
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
On the mechanism of bile acid inhibition of rat sterol 12alpha-hydroxylase gene (CYP8B1) transcription: roles of alpha-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha.
Publisher
An entity responsible for making the resource available
Biochimica et biophysica acta
Date
A point or period of time associated with an event in the lifecycle of the resource
2002
2002-06
Subject
The topic of the resource
Animals; Rats; Gene Expression Regulation; Base Sequence; Cattle; Cytochrome P-450 Enzyme System/*genetics; Hepatocyte Nuclear Factor 4; *DNA-Binding Proteins; Bile Acids and Salts/*pharmacology; Steroid Hydroxylases/*genetics; alpha-Fetoproteins/genetics/*physiology; DNA; Phosphoproteins/genetics/*physiology; Steroid 12-alpha-Hydroxylase; Transcription Factors/genetics/*physiology; Sprague-Dawley; RNA; Transcription; Genetic; Promoter Regions; Messenger/genetics; Enzymologic/*drug effects/physiology; Genetic/*drug effects
Creator
An entity primarily responsible for making the resource
Yang Yizeng; Zhang Ming; Eggertsen Gosta; Chiang John Y L
Description
An account of the resource
The sterol 12alpha-hydroxylase (CYP8B1) is a key enzyme of the bile acid biosynthetic pathway. It regulates the composition of bile acids in bile, i.e. ratio between cholic acid (CA) and chenodeoxycholic acid (CDCA). In similarity with cholesterol 7alpha-hydroxylase (CYP7A1), this enzyme is subjected to a negative feedback regulation by bile acids. It has been recently reported that bile acid-activated farnesoid X receptor (FXR) induces the small heterodimer partner (SHP) that interacts with alpha-fetoprotein transcription factor (FTF) and down-regulates CYP7A1 transcription. We studied whether the same mechanism also regulated rat CYP8B1 gene transcription. Feeding rats with CDCA caused a
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*DNA-Binding Proteins
2002
alpha-Fetoproteins/genetics/*physiology
Animals
Base Sequence
Bile Acids and Salts/*pharmacology
Biochimica et biophysica acta
Cattle
Chiang John Y L
Cytochrome P-450 Enzyme System/*genetics
Department of Integrative Medical Sciences
DNA
Eggertsen Gosta
Enzymologic/*drug effects/physiology
Gene Expression Regulation
Genetic
Genetic/*drug effects
Hepatocyte Nuclear Factor 4
Messenger/genetics
NEOMED College of Medicine
Phosphoproteins/genetics/*physiology
Promoter Regions
Rats
RNA
Sprague-Dawley
Steroid 12-alpha-Hydroxylase
Steroid Hydroxylases/*genetics
Transcription
Transcription Factors/genetics/*physiology
Yang Yizeng
Zhang Ming
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
Pages
514–520
Issue
4
Volume
41
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Peroxisome proliferator-activated receptor alpha (PPARalpha) and agonist inhibit cholesterol 7alpha-hydroxylase gene (CYP7A1) transcription.
Publisher
An entity responsible for making the resource available
Journal of lipid research
Date
A point or period of time associated with an event in the lifecycle of the resource
2000
2000-04
Subject
The topic of the resource
Humans; Animals; Binding Sites; Protein Binding; Rats; Gene Expression Regulation; Species Specificity; Liver/metabolism; Transcriptional Activation; Hepatocyte Nuclear Factor 4; Response Elements; *DNA-Binding Proteins; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Retinoid X Receptors; Anticholesteremic Agents/pharmacology; Cholesterol 7-alpha-Hydroxylase/biosynthesis/*genetics; Clofibric Acid/pharmacology; Peroxisome Proliferators/pharmacology; Phosphoproteins/metabolism; Pyrimidines/pharmacology; Transcription Factors/*agonists/metabolism; Genes; Receptors; Models; Transcription; Genetic; Enzymologic; Reporter; Retinoic Acid/metabolism; Promoter Regions; Nucleic Acid; Cytoplasmic and Nuclear/*agonists; *Regulatory Sequences
Creator
An entity primarily responsible for making the resource
Marrapodi M; Chiang J Y
Description
An account of the resource
Fibrates are widely used hypolipidemic drugs that regulate the expression of many genes involved in lipid metabolism by activating the peroxisome proliferator-activated receptor alpha (PPARalpha). The objective of this study was to investigate the mechanism of action of peroxisome proliferators and PPARalpha on the transcription of cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in the conversion of cholesterol to bile acids in the liver. When cotransfected with the expression vectors for PPARalpha and RXRalpha, Wy14,643 reduced human and rat cholesterol 7alpha-hydroxylase gene (CYP7A1)/luciferase reporter activities by 88% and 43%, respectively, in HepG2 cells, but not in CV-1 or CHO cells. We have mapped the peroxisome proliferator response element (PPRE) to a conserved sequence containing the canonical AGGTCA direct repeats separated by one nucleotide (DR1). This DR1 sequence was mapped previously as a binding site for the hepatocyte nuclear factor 4 (HNF-4) which stimulates CYP7A1 transcription. Electrophoretic mobility shift assay (EMSA) showed no direct binding of in vitro synthesized PPARalpha/RXRalpha heterodimer to the DR1 sequence. PPARalpha and Wy14,643 did not affect HNF-4 binding to the DR1. However, Wy14,643 and PPARalpha/RXRalpha significantly reduced HNF-4 expression in HepG2 cells. These results suggest that PPARalpha and agonist repress cholesterol 7alpha-hydroxylase activity by reducing the availability of
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*DNA-Binding Proteins
*Regulatory Sequences
2000
Animals
Anticholesteremic Agents/pharmacology
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Binding Sites
Chiang J Y
Cholesterol 7-alpha-Hydroxylase/biosynthesis/*genetics
Clofibric Acid/pharmacology
Cytoplasmic and Nuclear/*agonists
Department of Integrative Medical Sciences
Enzymologic
Gene Expression Regulation
Genes
Genetic
Hepatocyte Nuclear Factor 4
Humans
Journal of lipid research
Liver/metabolism
Marrapodi M
Models
NEOMED College of Medicine
Nucleic Acid
Peroxisome Proliferators/pharmacology
Phosphoproteins/metabolism
Promoter Regions
Protein Binding
Pyrimidines/pharmacology
Rats
Receptors
Reporter
Response Elements
Retinoic Acid/metabolism
Retinoid X Receptors
Species Specificity
Transcription
Transcription Factors/*agonists/metabolism
Transcriptional Activation
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
Pages
71–82
Volume
313
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Regulation of human sterol 27-hydroxylase gene (CYP27A1) by bile acids and hepatocyte nuclear factor 4alpha (HNF4alpha).
Publisher
An entity responsible for making the resource available
Gene
Date
A point or period of time associated with an event in the lifecycle of the resource
2003
2003-08
Subject
The topic of the resource
Humans; Cell Line; Transfection; Gene Expression Regulation/drug effects; Base Sequence; Binding Sites/genetics; Response Elements/genetics; Molecular Sequence Data; Mutation; Chenodeoxycholic Acid/pharmacology; Transcription Factors/genetics/*metabolism; Hepatocyte Nuclear Factor 4; Mutagenesis; *DNA-Binding Proteins; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Bile Acids and Salts/*pharmacology; Cholestanetriol 26-Monooxygenase; DNA/chemistry/genetics; Luciferases/genetics/metabolism; Phosphoproteins/genetics/*metabolism; Recombinant Fusion Proteins/genetics/metabolism; Steroid Hydroxylases/*genetics; DNA; Dose-Response Relationship; Drug; Cultured; Receptors; Tumor Cells; Cloning; Molecular; Sequence Analysis; Promoter Regions; Genetic/*genetics; Cytoplasmic and Nuclear/genetics/metabolism; Site-Directed
Creator
An entity primarily responsible for making the resource
Chen Wenling; Chiang John Y L
Description
An account of the resource
Mitochondrial sterol 27-hydroxylase (CYP27A1) catalyses sterol side-chain oxidation of bile acid synthesis from cholesterol, and the first reaction of the acidic bile acid biosynthetic pathway. Hydrophobic bile acids suppress human CYP27A1 gene reporter activity when assayed in human hepatocellular blastoma HepG2 cells. Bile acids also inhibit CYP27A1 reporter activity in human embryonic kidney 293 cells. A putative bile acid response element (BARE) was mapped to a region downstream of nt -147 of the human CYP27A1 gene, within which a binding site for a liver-specific nuclear receptor, HNF4alpha, is identified. HNF4alpha strongly stimulates CYP27A1 gene transcription and mutation of its binding site markedly reduced promoter activity. Results suggest that human CYP27A1 gene transcription is suppressed by bile acids and HNF4alpha plays a pivotal role in transcriptional regulation of this gene.
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*DNA-Binding Proteins
2003
Base Sequence
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Bile Acids and Salts/*pharmacology
Binding Sites/genetics
Cell Line
Chen Wenling
Chenodeoxycholic Acid/pharmacology
Chiang John Y L
Cholestanetriol 26-Monooxygenase
Cloning
Cultured
Cytoplasmic and Nuclear/genetics/metabolism
Department of Integrative Medical Sciences
DNA
DNA/chemistry/genetics
Dose-Response Relationship
Drug
gene
Gene Expression Regulation/drug effects
Genetic/*genetics
Hepatocyte Nuclear Factor 4
Humans
Luciferases/genetics/metabolism
Molecular
Molecular Sequence Data
Mutagenesis
Mutation
NEOMED College of Medicine
Phosphoproteins/genetics/*metabolism
Promoter Regions
Receptors
Recombinant Fusion Proteins/genetics/metabolism
Response Elements/genetics
Sequence Analysis
Site-Directed
Steroid Hydroxylases/*genetics
Transcription Factors/genetics/*metabolism
Transfection
Tumor Cells
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1074/jbc.M105117200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M105117200</a>
Pages
41690–41699
Issue
45
Volume
276
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Transcriptional regulation of the human sterol 12alpha-hydroxylase gene (CYP8B1): roles of heaptocyte nuclear factor 4alpha in mediating bile acid repression.
Publisher
An entity responsible for making the resource available
The Journal of biological chemistry
Date
A point or period of time associated with an event in the lifecycle of the resource
2001
2001-11
Subject
The topic of the resource
*DNA-Binding Proteins; *Transcription; Base Sequence; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Bile Acids and Salts/*pharmacology; Binding Sites; Cholesterol 7-alpha-Hydroxylase/genetics; Cultured; Cytochrome P-450 Enzyme System/*genetics; Cytoplasmic and Nuclear/physiology; Genetic; Genetic/physiology; Hepatocyte Nuclear Factor 4; Humans; Molecular Sequence Data; Phosphoproteins/*physiology; Promoter Regions; Receptors; Repressor Proteins/*pharmacology; Steroid 12-alpha-Hydroxylase; Steroid Hydroxylases/*genetics; Transcription Factors/*physiology; Tumor Cells
Creator
An entity primarily responsible for making the resource
Zhang M; Chiang J Y
Description
An account of the resource
Sterol 12alpha-hydroxylase catalyzes the synthesis of cholic acid and controls the ratio of cholic acid over chenodeoxycholic acid in the bile. Transcription of CYP8B1 is inhibited by bile acids, cholesterol, and insulin. To study the mechanism of CYP8B1 transcription by bile acids, we have cloned and determined 3389 base pairs of the 5'-upstream nucleotide sequences of the human CYP8B1. Deletion analysis of CYP8B1/luciferase reporter activity in HepG2 cells revealed that the sequences from -57 to +300 were important for basal and liver-specific promoter activities. Hepatocyte nuclear factor 4alpha (HNF4alpha) strongly activated human CYP8B1 promoter activities, whereas cholesterol 7alpha-hydroxylase promoter factor (CPF), an NR5A2 family of nuclear receptors, had much less effect. Electrophoretic mobility shift assay identified an overlapping HNF4alpha- and CPF-binding site in the +198/+227 region. The human CYP8B1 promoter activities were strongly repressed by bile acids, and the bile acid response element was localized between +137 and +220. Site-directed mutagenesis of the HNF4alpha-binding site markedly reduced promoter activity and its response to bile acid repression. On the other hand, mutation of the
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M105117200" target="_blank" rel="noreferrer noopener">10.1074/jbc.M105117200</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*DNA-Binding Proteins
*Transcription
2001
Base Sequence
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Bile Acids and Salts/*pharmacology
Binding Sites
Chiang J Y
Cholesterol 7-alpha-Hydroxylase/genetics
Cultured
Cytochrome P-450 Enzyme System/*genetics
Cytoplasmic and Nuclear/physiology
Department of Integrative Medical Sciences
Genetic
Genetic/physiology
Hepatocyte Nuclear Factor 4
Humans
Molecular Sequence Data
NEOMED College of Medicine
Phosphoproteins/*physiology
Promoter Regions
Receptors
Repressor Proteins/*pharmacology
Steroid 12-alpha-Hydroxylase
Steroid Hydroxylases/*genetics
The Journal of biological chemistry
Transcription Factors/*physiology
Tumor Cells
Zhang M