1
40
2
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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/10.2741/a273" target="_blank" rel="noreferrer noopener">http://doi.org/10.2741/a273</a>
Pages
d176–193
Volume
3
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 bile acid synthesis.
Publisher
An entity responsible for making the resource available
Frontiers in bioscience : a journal and virtual library
Date
A point or period of time associated with an event in the lifecycle of the resource
1998
1998-02
Subject
The topic of the resource
Humans; Animals; Gene Expression Regulation; Liver/metabolism; Cytochrome P-450 Enzyme System/metabolism; Bile Acids and Salts/*biosynthesis; Cholesterol/metabolism; Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism; Cytochrome P450 Family 7; Cholestanetriol 26-Monooxygenase; Steroid 12-alpha-Hydroxylase/metabolism; Steroid Hydroxylases/metabolism
Creator
An entity primarily responsible for making the resource
Chiang J Y
Description
An account of the resource
Bile acids are important physiological agents required for disposal of cholesterol and absorption of vitamins and fats. Bile acids are synthesized from cholesterol in the liver. Enterohepatic circulation of bile acids is very efficient and plays an important physiological role in lipid absorption and secretion, and regulation of bile acid biosynthesis and cholesterol homeostasis. Conversion of cholesterol to bile acids requires 15 different enzymatic steps. Four cytochrome P450 enzymes play important roles in bile acid biosynthesis. The classic bile acid biosynthesis pathway starts with modification of the sterol ring and followed by side chain cleavage reactions to synthesize cholic acid (CA) and chenodeoxycholic acid (CDCA), the primary bile acids in most species. The first and rate-limiting enzyme in this pathway is cholesterol 7alpha -hydroxylase, a microsomal cytochrome P450, CYP7A. Another microsomal cytochrome P450 sterol 12alpha-hydroxylase (CYP12) is required for the synthesis of cholic acid. Mitochondrial cytochrome P450 sterol 27-hydroxylase (CYP27) catalyzes sterol side chain oxidation to convert C27 sterol to C24 bile acids. An alternative bile acid biosynthesis pathway (acidic) has been known for sometime but only recently has attracted much attention. In this pathway, side chain oxidation precedes modification of the sterol ring. Mitochondrial sterol
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.2741/a273" target="_blank" rel="noreferrer noopener">10.2741/a273</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).
1998
Animals
Bile Acids and Salts/*biosynthesis
Chiang J Y
Cholestanetriol 26-Monooxygenase
Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism
Cholesterol/metabolism
Cytochrome P-450 Enzyme System/metabolism
Cytochrome P450 Family 7
Department of Integrative Medical Sciences
Frontiers in bioscience : a journal and virtual library
Gene Expression Regulation
Humans
Liver/metabolism
NEOMED College of Medicine
Steroid 12-alpha-Hydroxylase/metabolism
Steroid Hydroxylases/metabolism