1
40
14
-
Text
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URL Address
<a href="http://doi.org/10.1002/jcp.25900" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/jcp.25900</a>
Pages
409–421
Issue
1
Volume
233
Dublin Core
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Title
A name given to the resource
Osteoactivin regulates head and neck squamous cell carcinoma invasion by modulating matrix metalloproteases.
Publisher
An entity responsible for making the resource available
Journal of cellular physiology
Date
A point or period of time associated with an event in the lifecycle of the resource
2018
2018-01
Subject
The topic of the resource
*Cell Movement; Carcinoma; Cell Line; cell lines; Enzymologic; extracellular matrix; Gene Expression Regulation; Head and Neck Neoplasms/*enzymology/genetics/pathology; human; Humans; matrix metalloproteinases; Matrix Metalloproteinases; Membrane Glycoproteins/genetics/*metabolism; Messenger/genetics/metabolism; neoplasm invasion; Neoplasm Invasiveness; Neoplastic; RNA; RNA Interference; Secreted/genetics/*metabolism; Signal Transduction; Squamous Cell Carcinoma of Head and Neck; Squamous Cell/*enzymology/genetics/pathology; Transfection; Tumor
Creator
An entity primarily responsible for making the resource
Arosarena Oneida A; Barr Eric W; Thorpe Ryan; Yankey Hilary; Tarr Joseph T; Safadi Fayez F
Description
An account of the resource
Nearly 60% of patients with head and neck squamous cell carcinoma (HNSCC) die of metastases or locoregional recurrence. Metastasis is mediated by cancer cell migration and invasion, which are in part dependent on extracellular matrix degradation by matrix metalloproteinases. Osteoactivin (OA) overexpression plays a role in metastases in several malignancies, and has been shown to upregulate matrix metalloproteinase (MMP) expression and activity. To determine how OA modulates MMP expression and activity in HNSCC, and to investigate OA effects on cell invasion, we assessed effects of OA treatment on MMP mRNA and protein expression, as well as gelatinase and caseinolytic activity in HNSCC cell lines. We assessed the effects of OA gene silencing on MMP expression, gelatinase and caseinolytic activity, and cell invasion. OA treatment had differential effects on MMP mRNA expression. OA treatment upregulated MMP-10 expression in UMSCC14a (p = 0.0431) and SCC15 (p \textless 0.0001) cells, but decreased MMP-9 expression in UMSCC14a cells (p = 0.0002). OA gene silencing decreased MMP-10 expression in UMSCC12 cells (p = 0.0001), and MMP-3 (p = 0.0005) and -9 (p = 0.0036) expression in SCC25 cells. In SCC15 and SCC25 cells, OA treatment increased MMP-2 (p = 0.0408) and MMP-9 gelatinase activity (p \textless 0.0001), respectively. OA depletion decreased MMP-2 (p = 0.0023) and -9 (p \textless 0.0001) activity in SCC25 cells. OA treatment increased 70 kDa caseinolytic activity in UMSCC12 cells consistent with tissue type plasminogen activator (p = 0.0078). OA depletion decreased invasive capacity of UMSCC12 cells (p \textless 0.0001). OA's effects on MMP expression in HNSCC are variable, and may promote cancer cell invasion.
Identifier
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<a href="http://doi.org/10.1002/jcp.25900" target="_blank" rel="noreferrer noopener">10.1002/jcp.25900</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Cell Movement
2018
Arosarena Oneida A
Barr Eric W
Carcinoma
Cell Line
cell lines
Department of Anatomy & Neurobiology
Enzymologic
Extracellular Matrix
Gene Expression Regulation
Head and Neck Neoplasms/*enzymology/genetics/pathology
Human
Humans
Journal of cellular physiology
matrix metalloproteinases
Membrane Glycoproteins/genetics/*metabolism
Messenger/genetics/metabolism
NEOMED College of Medicine
neoplasm invasion
Neoplasm Invasiveness
Neoplastic
RNA
RNA Interference
Safadi Fayez F
Secreted/genetics/*metabolism
Signal Transduction
Squamous Cell Carcinoma of Head and Neck
Squamous Cell/*enzymology/genetics/pathology
Tarr Joseph T
Thorpe Ryan
Transfection
Tumor
Yankey Hilary
-
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/10.1006/abbi.2000.1836" target="_blank" rel="noreferrer noopener">http://doi.org/10.1006/abbi.2000.1836</a>
Pages
364–376
Issue
2
Volume
378
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
Promoter activity and regulation of the CYP4F2 leukotriene B(4) omega-hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells.
Publisher
An entity responsible for making the resource available
Archives of biochemistry and biophysics
Date
A point or period of time associated with an event in the lifecycle of the resource
2000
2000-06
Subject
The topic of the resource
*Gene Expression Regulation; *Promoter Regions; Amino Acid Sequence; Base Sequence; Cell Line; Cloning; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System/*genetics/metabolism; Cytochrome P450 Family 4; Cytoplasmic and Nuclear/metabolism; DNA; DNA Footprinting; Enzymologic; Exons; Genes; Genetic; Genetic/drug effects; Humans; Introns; Leukotriene B4/metabolism; Mixed Function Oxygenases/metabolism; Models; Molecular; Molecular Sequence Data; Peroxisome Proliferators/*metabolism; Receptors; Reporter; Retinoic Acid Receptor alpha; Retinoic Acid/metabolism; Sequence Analysis; Transcription; Transcription Factors/metabolism; Transfection; Tretinoin/*metabolism
Creator
An entity primarily responsible for making the resource
Zhang X; Chen L; Hardwick J P
Description
An account of the resource
The human liver CYP4F2 gene (Accession No. AF221943) encodes a leukotriene B(4) omega-hydroxylase that metabolizes leukotriene B(4) (LTB(4)) to a less potent proinflammatory eicosanoid, 20-OH-LTB(4). We sequenced a 6.7-kb genomic fragment of the human CYP4F2 gene that has the first five exons and 500 bp of the 5'-flanking region. The major transcription start site was found to be 49 bp upstream of the 3' end of exon 1 and the ATG translation initiation codon was located in exon 2. Besides the TATA box at -39 bp and basal transcription factor binding sites, the promoter region and 412-bp intron 1 have several putative binding sites for nuclear factors that may mediate the inflammatory response and lipid homeostasis. We found two DR1 elements in the 5' promoter, a DR2 element in intron 1, and RXR/RAR binding sites in both intron 1 and the 5' promoter. DNase I footprinting revealed three protected sequences, with the region containing two CAATT boxes at -71 and -111 bp important in CYP4F2 gene expression. Luciferase reporter assays showed that the 500-bp upstream sequence has strong promoter activity. Transient transfection experiments identified two sites in the 5' promoter and intron 1 that cooperate in gene transcription while exon 1 and a
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1006/abbi.2000.1836" target="_blank" rel="noreferrer noopener">10.1006/abbi.2000.1836</a>
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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).
*Gene Expression Regulation
*Promoter Regions
2000
Amino Acid Sequence
Archives of biochemistry and biophysics
Base Sequence
Cell Line
Chen L
Cloning
Cytochrome P-450 CYP4A
Cytochrome P-450 Enzyme System/*genetics/metabolism
Cytochrome P450 Family 4
Cytoplasmic and Nuclear/metabolism
Department of Integrative Medical Sciences
DNA
DNA Footprinting
Enzymologic
Exons
Genes
Genetic
Genetic/drug effects
Hardwick J P
Humans
Introns
Leukotriene B4/metabolism
Mixed Function Oxygenases/metabolism
Models
Molecular
Molecular Sequence Data
NEOMED College of Medicine
Peroxisome Proliferators/*metabolism
Receptors
Reporter
Retinoic Acid Receptor alpha
Retinoic Acid/metabolism
Sequence Analysis
Transcription
Transcription Factors/metabolism
Transfection
Tretinoin/*metabolism
Zhang X
-
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/10.1016/j.bcp.2008.03.004" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bcp.2008.03.004</a>
Pages
2263–2275
Issue
12
Volume
75
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
Cytochrome P450 omega hydroxylase (CYP4) function in fatty acid metabolism and metabolic diseases.
Publisher
An entity responsible for making the resource available
Biochemical pharmacology
Date
A point or period of time associated with an event in the lifecycle of the resource
2008
2008-06
Subject
The topic of the resource
*Cytochrome P-450 Enzyme System/genetics/metabolism/physiology; Animals; Cytochrome P-450 CYP4A/genetics/metabolism/physiology; Enzymologic; Fatty Acids/*metabolism; Gene Expression Regulation; Humans; Metabolic Diseases/enzymology/*metabolism
Creator
An entity primarily responsible for making the resource
Hardwick James P
Description
An account of the resource
The cytochrome P450 gene 4 family (CYP4) consists of a group of over 63 members that omega-hydroxylate the terminal carbon of fatty acids. In mammals, six subfamilies have been identified and three of these subfamily members show a preference in the metabolism of short (C7-C10)-CYP4B, medium (C10-C16)-CYP4A, and long (C16-C26)-CYP4F, saturated, unsaturated and branched chain fatty acids. These omega-hydroxylated fatty acids are converted to dicarboxylic acids, which are preferentially metabolized by the peroxisome beta-oxidation system to shorter chain fatty acids that are transported to the mitochondria for complete oxidation or used either to supply energy for peripheral tissues during starvation or in lipid synthesis. The differential regulation of the CYP4A and CYP4F genes during fasting, by peroxisome proliferators and in non-alcoholic fatty liver disease (NAFLD) suggests different roles in lipid metabolism. The omega-hydroxylation and inactivation of pro-inflammatory eicosanoids by members of the CYP4F subfamily and the association of the CYP4F2 and CYP4F3 genes with inflammatory celiac disease indicate an important role in the resolution of inflammation. Several human diseases have been genetically linked to the expression CYP4 gene polymorphic variants, which may link human susceptibility to diseases of lipid metabolism and the activation and resolution phases of inflammation. Understanding how the CYP4 genes are regulated during the fasting and feeding cycles and by endogenous lipids will provide therapeutic avenues in the treatment of metabolic disorders of lipid metabolism and inflammation.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.bcp.2008.03.004" target="_blank" rel="noreferrer noopener">10.1016/j.bcp.2008.03.004</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Cytochrome P-450 Enzyme System/genetics/metabolism/physiology
2008
Animals
Biochemical pharmacology
Cytochrome P-450 CYP4A/genetics/metabolism/physiology
Department of Integrative Medical Sciences
Enzymologic
Fatty Acids/*metabolism
Gene Expression Regulation
Hardwick James P
Humans
Metabolic Diseases/enzymology/*metabolism
NEOMED College of Medicine
-
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.M111.305789" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M111.305789</a>
Pages
1861–1873
Issue
3
Volume
287
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
Glucose and insulin induction of bile acid synthesis: mechanisms and implication in diabetes and obesity.
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
2012
2012-01
Subject
The topic of the resource
*Gene Expression Regulation; Animals; Bile Acids and Salts/*biosynthesis; Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism; Cytoplasmic and Nuclear/genetics/metabolism; Diabetes Mellitus; Dietary Fats/administration & dosage/adverse effects; Enzymologic; Epigenesis; Experimental/genetics/*metabolism; Fasting/metabolism; Genetic/genetics; Glucose/*metabolism/pharmacology; Insulin/*metabolism; Mice; Obesity/etiology/genetics/*metabolism; Postprandial Period/genetics; Receptors; Sweetening Agents/pharmacology; Transgenic
Creator
An entity primarily responsible for making the resource
Li Tiangang; Francl Jessica M; Boehme Shannon; Ochoa Adrian; Zhang Youcai; Klaassen Curtis D; Erickson Sandra K; Chiang John Y L
Description
An account of the resource
Bile acids facilitate postprandial absorption of nutrients. Bile acids also activate the farnesoid X receptor (FXR) and the G protein-coupled receptor TGR5 and play a major role in regulating lipid, glucose, and energy metabolism. Transgenic expression of cholesterol 7alpha-hydroxylase (CYP7A1) prevented high fat diet-induced diabetes and obesity in mice. In this study, we investigated the nutrient effects on bile acid synthesis. Refeeding of a chow diet to fasted mice increased CYP7A1 expression, bile acid pool size, and serum bile acids in wild type and humanized CYP7A1-transgenic mice. Chromatin immunoprecipitation assays showed that glucose increased histone acetylation and decreased histone methylation on the CYP7A1 gene promoter. Refeeding also induced CYP7A1 in fxr-deficient mice, indicating that FXR signaling did not play a role in postprandial regulation of bile acid synthesis. In streptozocin-induced type I diabetic mice and genetically obese type II diabetic ob/ob mice, hyperglycemia increased histone acetylation status on the CYP7A1 gene promoter, leading to elevated basal Cyp7a1 expression and an enlarged bile acid pool with altered bile acid composition. However, refeeding did not further increase CYP7A1 expression in diabetic mice. In summary, this study demonstrates that glucose and insulin are major postprandial factors that induce CYP7A1 gene expression and bile acid synthesis. Glucose induces CYP7A1 gene expression mainly by epigenetic mechanisms. In diabetic mice, CYP7A1 chromatin is hyperacetylated, and fasting to refeeding response is impaired and may exacerbate metabolic disorders in diabetes.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M111.305789" target="_blank" rel="noreferrer noopener">10.1074/jbc.M111.305789</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).
*Gene Expression Regulation
2012
Animals
Bile Acids and Salts/*biosynthesis
Boehme Shannon
Chiang John Y L
Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism
Cytoplasmic and Nuclear/genetics/metabolism
Department of Integrative Medical Sciences
Diabetes Mellitus
Dietary Fats/administration & dosage/adverse effects
Enzymologic
Epigenesis
Erickson Sandra K
Experimental/genetics/*metabolism
Fasting/metabolism
Francl Jessica M
Genetic/genetics
Glucose/*metabolism/pharmacology
Insulin/*metabolism
Klaassen Curtis D
Li Tiangang
Mice
NEOMED College of Medicine
Obesity/etiology/genetics/*metabolism
Ochoa Adrian
Postprandial Period/genetics
Receptors
Sweetening Agents/pharmacology
The Journal of biological chemistry
Transgenic
Zhang Youcai
-
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.M513420200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M513420200</a>
Pages
10081–10088
Issue
15
Volume
281
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
A Prospero-related homeodomain protein is a novel co-regulator of hepatocyte nuclear factor 4alpha that regulates the cholesterol 7alpha-hydroxylase gene.
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
2006
2006-04
Subject
The topic of the resource
*Gene Expression Regulation; Aged; Amino Acid Motifs; Bile Acids and Salts/metabolism; Cell Line; Cell Nucleus/metabolism; Cells; Cholesterol 7-alpha-Hydroxylase/*chemistry/*genetics; Cultured/metabolism; Enzymologic; Female; Genes; Genetic; Gluconeogenesis; Glutathione Transferase/metabolism; Hepatocyte Nuclear Factor 4/metabolism/*physiology; Hepatocytes/metabolism; Homeodomain Proteins/metabolism/*physiology; Humans; Immunoprecipitation; Liver/metabolism; Luciferases/metabolism; Male; Messenger/metabolism; Middle Aged; Phosphoenolpyruvate Carboxykinase (ATP)/metabolism; Plasmids/metabolism; Protein Structure; Reporter; Response Elements; Reverse Transcriptase Polymerase Chain Reaction; RNA; Small Interfering/metabolism; Tertiary; Time Factors; Transcription; Transcriptional Activation; Transfection; Tumor Suppressor Proteins; Two-Hybrid System Techniques
Creator
An entity primarily responsible for making the resource
Song Kwang-Hoon; Li Tiangang; Chiang John Y L
Description
An account of the resource
Prox1, an early specific marker for developing liver and pancreas in foregut endoderm has recently been shown to interact with alpha-fetoprotein transcription factor and repress cholesterol 7alpha-hydroxylase (CYP7A1) gene transcription. Using a yeast two-hybrid assay, we found that Prox1 strongly and specifically interacted with hepatocyte nuclear factor (HNF)4alpha, an important transactivator of the human CYP7A1 gene in bile acid synthesis and phosphoenolpyruvate carboxykinase (PEPCK) gene in gluconeogenesis. A real time PCR assay detected Prox1 mRNA expression in human primary hepatocytes and HepG2 cells. Reporter assay, GST pull-down, co-immunoprecipitation, and yeast two-hybrid assays identified a specific interaction between the N-terminal LXXLL motif of Prox1 and the activation function 2 domain of HNF4alpha. Prox1 strongly inhibited HNF4alpha and peroxisome proliferators-activated receptor gamma coactivator-1alpha co-activation of the CYP7A1 and PEPCK genes. Knock down of the endogenous Prox1 by small interfering RNA resulted in significant increase of CYP7A1 and PEPCK mRNA expression and the rate of bile acid synthesis in HepG2 cells. These results suggest that Prox1 is a novel co-regulator of HNF4alpha that may play a key role in the regulation of bile acid synthesis and gluconeogenesis in the liver.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M513420200" target="_blank" rel="noreferrer noopener">10.1074/jbc.M513420200</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).
*Gene Expression Regulation
2006
Aged
Amino Acid Motifs
Bile Acids and Salts/metabolism
Cell Line
Cell Nucleus/metabolism
Cells
Chiang John Y L
Cholesterol 7-alpha-Hydroxylase/*chemistry/*genetics
Cultured/metabolism
Department of Integrative Medical Sciences
Enzymologic
Female
Genes
Genetic
Gluconeogenesis
Glutathione Transferase/metabolism
Hepatocyte Nuclear Factor 4/metabolism/*physiology
Hepatocytes/metabolism
Homeodomain Proteins/metabolism/*physiology
Humans
Immunoprecipitation
Li Tiangang
Liver/metabolism
Luciferases/metabolism
Male
Messenger/metabolism
Middle Aged
NEOMED College of Medicine
Phosphoenolpyruvate Carboxykinase (ATP)/metabolism
Plasmids/metabolism
Protein Structure
Reporter
Response Elements
Reverse Transcriptase Polymerase Chain Reaction
RNA
Small Interfering/metabolism
Song Kwang-Hoon
Tertiary
The Journal of biological chemistry
Time Factors
Transcription
Transcriptional Activation
Transfection
Tumor Suppressor Proteins
Two-Hybrid System Techniques
-
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.M605815200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M605815200</a>
Pages
28745–28754
Issue
39
Volume
281
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
Insulin regulation of cholesterol 7alpha-hydroxylase expression in human hepatocytes: roles of forkhead box O1 and sterol regulatory element-binding protein 1c.
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
2006
2006-09
Subject
The topic of the resource
*Gene Expression Regulation; *Transcriptional Activation; Adolescent; Adult; Animals; Child; Cholesterol 7-alpha-Hydroxylase/*biosynthesis/genetics; Enzymologic; Female; Forkhead Box Protein O1; Forkhead Transcription Factors/*physiology; Hepatocytes/*enzymology; Humans; Insulin/metabolism/*physiology; Male; Middle Aged; Preschool; Rats; Sterol Regulatory Element Binding Protein 1/*physiology; Transcription Factors/*physiology
Creator
An entity primarily responsible for making the resource
Li Tiangang; Kong Xiaoying; Owsley Erika; Ellis Ewa; Strom Stephen; Chiang John Y L
Description
An account of the resource
Bile acid synthesis and pool size increases in diabetes, whereas insulin inhibits bile acid synthesis. The objective of this study is to elucidate the mechanism of insulin regulation of cholesterol 7alpha-hydroxylase gene expression in human hepatocytes. Real-time PCR assays showed that physiological concentrations of insulin rapidly stimulated cholesterol 7alpha-hydroxylase (CYP7A1) mRNA expression in primary human hepatocytes but inhibited CYP7A1 expression after extended treatment. The insulin-regulated forkhead box O1 (FoxO1) and steroid regulatory element-binding protein-1c (SREBP-1c) strongly inhibited hepatocyte nuclear factor 4alpha and peroxisome proliferator-activated receptor gamma coactivator-1alpha trans-activation of the CYP7A1 gene. FoxO1 binds to an insulin response element in the rat CYP7A1 promoter, which is not present in the human CYP7A1 gene. Insulin rapidly phosphorylates and inactivates FoxO1, whereas insulin induces nuclear SREBP-1c expression in human primary hepatocytes. Chromatin immunoprecipitation assay shows that insulin reduced FoxO1 and peroxisome proliferators-activated receptor gamma-coactivator-1alpha but increased SREBP-1c recruitment to CYP7A1 chromatin. We conclude that insulin has dual effects on human CYP7A1 gene transcription; physiological concentrations of insulin rapidly inhibit FoxO1 activity leading to stimulation of the human CYP7A1 gene, whereas prolonged insulin treatment induces SREBP-1c, which inhibits human CYP7A1 gene transcription. Insulin may play a major role in the regulation of bile acid synthesis and dyslipidemia in diabetes.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M605815200" target="_blank" rel="noreferrer noopener">10.1074/jbc.M605815200</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).
*Gene Expression Regulation
*Transcriptional Activation
2006
Adolescent
Adult
Animals
Chiang John Y L
Child
Cholesterol 7-alpha-Hydroxylase/*biosynthesis/genetics
Department of Integrative Medical Sciences
Ellis Ewa
Enzymologic
Female
Forkhead Box Protein O1
Forkhead Transcription Factors/*physiology
Hepatocytes/*enzymology
Humans
Insulin/metabolism/*physiology
Kong Xiaoying
Li Tiangang
Male
Middle Aged
NEOMED College of Medicine
Owsley Erika
Preschool
Rats
Sterol Regulatory Element Binding Protein 1/*physiology
Strom Stephen
The Journal of biological chemistry
Transcription Factors/*physiology
-
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/10.1194/jlr.M002782" target="_blank" rel="noreferrer noopener">http://doi.org/10.1194/jlr.M002782</a>
Pages
832–842
Issue
4
Volume
51
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
Glucose stimulates cholesterol 7alpha-hydroxylase gene transcription in human hepatocytes.
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
2010
2010-04
Subject
The topic of the resource
*Gene Expression Regulation; Acetylation; AMP-Activated Protein Kinases/metabolism; ATP Citrate (pro-S)-Lyase/genetics/metabolism; Bile Acids and Salts/metabolism; Cells; Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism; Cultured; DNA-Binding Proteins/metabolism; Enzymologic; Epigenesis; Genes; Genetic; Glucose/*administration & dosage; Hep G2 Cells; Hepatocyte Nuclear Factor 4/metabolism; Hepatocytes/*enzymology/metabolism; Histones/metabolism; Humans; Hyperglycemia/enzymology/*metabolism; Messenger/metabolism; Methylation; Reporter; RNA; RNA Interference
Creator
An entity primarily responsible for making the resource
Li Tiangang; Chanda Dipanjan; Zhang Yanqiao; Choi Hueng-Sik; Chiang John Y L
Description
An account of the resource
Bile acids play important roles in the regulation of lipid, glucose, and energy homeostasis. Recent studies suggest that glucose regulates gene transcription in the liver. The aim of this study was to investigate the potential role of glucose in regulation of bile acid synthesis in human hepatocytes. High glucose stimulated bile acid synthesis and induced mRNA expression of cholesterol 7alpha-hydroxylase (CYP7A1), the key regulatory gene in bile acid synthesis. Activation of an AMP-activated protein kinase (AMPK) decreased CYP7A1 mRNA, hepatocyte nuclear factor 4alpha (HNF4alpha) protein, and binding to CYP7A1 chromatin. Glucose increased ATP levels to inhibit AMPK and induce HNF4alpha to stimulate CYP7A1 gene transcription. Furthermore, glucose increased histone acetylation and decreased H3K9 di- and tri-methylation in the CYP7A1 chromatin. Knockdown of ATP-citrate lyase, which converts citrate to acetyl-CoA, decreased histone acetylation and attenuated glucose induction of CYP7A1 mRNA expression. These results suggest that glucose signaling also induces CYP7A1 gene transcription by epigenetic regulation of the histone acetylation status. This study uncovers a novel link between hepatic glucose metabolism and bile acid synthesis. Glucose induction of bile acid synthesis may have an important implication in metabolic control of glucose, lipid, and energy homeostasis under normal and diabetic conditions.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1194/jlr.M002782" target="_blank" rel="noreferrer noopener">10.1194/jlr.M002782</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).
*Gene Expression Regulation
2010
Acetylation
AMP-Activated Protein Kinases/metabolism
ATP Citrate (pro-S)-Lyase/genetics/metabolism
Bile Acids and Salts/metabolism
Cells
Chanda Dipanjan
Chiang John Y L
Choi Hueng-Sik
Cholesterol 7-alpha-Hydroxylase/genetics/*metabolism
Cultured
Department of Integrative Medical Sciences
DNA-Binding Proteins/metabolism
Enzymologic
Epigenesis
Genes
Genetic
Glucose/*administration & dosage
Hep G2 Cells
Hepatocyte Nuclear Factor 4/metabolism
Hepatocytes/*enzymology/metabolism
Histones/metabolism
Humans
Hyperglycemia/enzymology/*metabolism
Journal of lipid research
Li Tiangang
Messenger/metabolism
Methylation
NEOMED College of Medicine
Reporter
RNA
RNA Interference
Zhang Yanqiao
-
Text
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URL Address
<a href="http://doi.org/10.1194/jlr.M800140-JLR200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1194/jlr.M800140-JLR200</a>
Pages
1981–1989
Issue
9
Volume
49
Dublin Core
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Title
A name given to the resource
TGFbeta1, TNFalpha, and insulin signaling crosstalk in regulation of the rat cholesterol 7alpha-hydroxylase gene expression.
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
2008
2008-09
Subject
The topic of the resource
*Gene Expression Regulation; Animals; Cell Line; Cholesterol 7-alpha-Hydroxylase/*genetics; Enzymologic; Forkhead Transcription Factors/physiology; Humans; Insulin/*physiology; Male; Nerve Tissue Proteins/physiology; Rats; Signal Transduction; Smad3 Protein/antagonists & inhibitors/pharmacology; Sprague-Dawley; Transforming Growth Factor beta1/*physiology; Tumor; Tumor Necrosis Factor-alpha/*physiology
Creator
An entity primarily responsible for making the resource
Li Tiangang; Ma Huiyan; Chiang John Y L
Description
An account of the resource
The TGFbeta1/Smad pathway plays a critical role in cholestasis and liver fibrosis. Previous studies show that TGFbeta1, TNFalpha, and insulin inhibit cholesterol 7alpha-hydroxylase (CYP7A1) gene transcription and bile acid synthesis in human hepatocytes. In this study, we investigated insulin, TGFbeta1, and TNFalpha regulation of rat Cyp7a1 gene transcription. In contrast to inhibition of human CYP7A1 gene transcription, TGFbeta1 stimulates rat Cyp7a1 reporter activity. Smad3, FoxO1, and HNF4alpha synergistically stimulated rat Cyp7a1 gene transcription. Mutations of the Smad3, FoxO1, or HNF4alpha binding site attenuated the rat Cyp7a1 promoter activity. Furthermore, TNFalpha and cJun attenuated TGFbeta1 stimulation of rat Cyp7a1. Insulin or adenovirus-mediated expression of constitutively active AKT1 inhibited FoxO1 and Smad3 synergy. In streptozotocin-induced diabetic rats, Cyp7a1 mRNA expression levels were induced and insulin attenuated CYP7A1 mRNA levels. Chromatin immunoprecipitation assay showed that FoxO1 binding to Cyp7a1 chromatin was increased in diabetic rat livers and insulin reduced FoxO1 binding. These results suggest a mechanistic basis for induction of Cyp7a1 activity and bile acid synthesis in cholestatic rats and in diabetic rats. The crosstalk of insulin, TGFbeta and TNFalpha signaling pathways may regulate bile acid synthesis and lipid homeostasis in diabetes, fatty liver disease, and liver fibrosis.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1194/jlr.M800140-JLR200" target="_blank" rel="noreferrer noopener">10.1194/jlr.M800140-JLR200</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).
*Gene Expression Regulation
2008
Animals
Cell Line
Chiang John Y L
Cholesterol 7-alpha-Hydroxylase/*genetics
Department of Integrative Medical Sciences
Enzymologic
Forkhead Transcription Factors/physiology
Humans
Insulin/*physiology
Journal of lipid research
Li Tiangang
Ma Huiyan
Male
NEOMED College of Medicine
Nerve Tissue Proteins/physiology
Rats
Signal Transduction
Smad3 Protein/antagonists & inhibitors/pharmacology
Sprague-Dawley
Transforming Growth Factor beta1/*physiology
Tumor
Tumor Necrosis Factor-alpha/*physiology
-
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
17502–17507
Issue
26
Volume
269
Dublin Core
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Title
A name given to the resource
Identification and characterization of a putative bile acid-responsive element in cholesterol 7 alpha-hydroxylase gene promoter.
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
1994
1994-07
Subject
The topic of the resource
Humans; Animals; Rats; Gene Expression Regulation; Base Sequence; Bile Acids and Salts/*metabolism; Cholesterol 7-alpha-Hydroxylase/*genetics/metabolism; Molecular Sequence Data; Recombinant Fusion Proteins/genetics/metabolism; Luciferases/genetics; DNA-Binding Proteins/metabolism; Deoxyribonuclease I; Nuclear Proteins/metabolism; Oligodeoxyribonucleotides; Thyroid Hormones/genetics; Sprague-Dawley; Genetic; Enzymologic; Cloning; Molecular; *Promoter Regions; Antigens; Polyomavirus Transforming/genetics
Creator
An entity primarily responsible for making the resource
Chiang J Y; Stroup D
Description
An account of the resource
Nucleotide sequences of a 7997-base pair SacI fragment spanning 3643 base pairs of the upstream promoter region to exon 4 of the rat cholesterol 7 alpha-hydroxylase gene (CYP7) have been determined. DNase I footprinting and electrophoretic mobility shift assay of the proximal promoter from nucleotides -346 to +36 revealed two protected regions which specifically shifted proteins in rat liver nuclear extracts. Footprint A (nucleotides -81 to -35) contained a cluster of overlapping sequence motifs of TGT3, steroid/thyroid hormone response elements (7 alpha TRE), hepatocyte nuclear factors 1 and 4, and CAAT/enhancer-binding protein alpha and has been shown to confer bile acid repression of the CYP7 gene promoter activity. Footprint B (nucleotides -148 to -129) contained a sequence motif HNF4. When footprint A (-101 to -49) or 7 alpha TRE (-73 to -55) sequence was linked upstream to a heterologous SV40 promoter/luciferase plasmid and transiently transfected into HepG2 cells, taurodeoxycholate suppressed the SV40 promoter activity. Electrophoretic mobility shift assays revealed that one or two bands shifted by the 7 alpha TRE or by a direct repeat sequence in 7 alpha TRE were absent when liver nuclear extracts of deoxycholic acid-treated rats were used. Similar gel shift patterns were also observed when human 7 alpha TRE or human liver nuclear extracts were used. The rat direct repeat sequence interacted with two polypeptides (M(r) = 57,000 and 116,000) in both rat and human liver nuclear extracts. These results suggest that hydrophobic bile acids may suppress the CYP7 gene expression by binding to a bile acid receptor which interacts with and prevents the binding of liver nuclear protein(s) to a bile acid-responsive element and that the core of bile acid-responsive element is a direct repeat.
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Promoter Regions
1994
Animals
Antigens
Base Sequence
Bile Acids and Salts/*metabolism
Chiang J Y
Cholesterol 7-alpha-Hydroxylase/*genetics/metabolism
Cloning
Deoxyribonuclease I
Department of Integrative Medical Sciences
DNA-Binding Proteins/metabolism
Enzymologic
Gene Expression Regulation
Genetic
Humans
Luciferases/genetics
Molecular
Molecular Sequence Data
NEOMED College of Medicine
Nuclear Proteins/metabolism
Oligodeoxyribonucleotides
Polyomavirus Transforming/genetics
Rats
Recombinant Fusion Proteins/genetics/metabolism
Sprague-Dawley
Stroup D
The Journal of biological chemistry
Thyroid Hormones/genetics
-
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/10.1002/jbt.2570050303" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/jbt.2570050303</a>
Pages
147–153
Issue
3
Volume
5
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
Aflatoxin B1 metabolism by 3-methylcholanthrene-induced hamster hepatic cytochrome P-450s.
Publisher
An entity responsible for making the resource available
Journal of biochemical toxicology
Date
A point or period of time associated with an event in the lifecycle of the resource
1990
1905-06
Subject
The topic of the resource
Animals; Rats; Gene Expression Regulation; Liver/enzymology; Antibodies/immunology; Cricetinae; Enzyme Induction/drug effects; Mesocricetus; Aflatoxin B1; Liver/drug effects/*enzymology; Methylcholanthrene/*pharmacology; Aflatoxins/immunology/*metabolism; Cytochrome P-450 Enzyme System/biosynthesis/isolation & purification/*metabolism; Mutagenicity Tests; Salmonella typhimurium/enzymology/genetics; Subcellular Fractions/drug effects/enzymology; Inbred Strains; Enzymologic; Microsomes
Creator
An entity primarily responsible for making the resource
Lai T S; Chiang J Y
Description
An account of the resource
We have studied the activation of aflatoxin B1 by hamster liver microsomes and purified hamster cytochrome P-450 isozymes using a umu mutagen test. The hamster liver microsomes or S-9 fractions were much more active than rat liver microsomes or S-9 fractions in the activation of umu gene expression by aflatoxin B1 metabolites. 3-Methyl-cholanthrene treatment increased aflatoxin B1 activation by hamster liver microsomes. Two major 3-methylcholanthrene-inducible cytochrome
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1002/jbt.2570050303" target="_blank" rel="noreferrer noopener">10.1002/jbt.2570050303</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).
1990
Aflatoxin B1
Aflatoxins/immunology/*metabolism
Animals
Antibodies/immunology
Chiang J Y
Cricetinae
Cytochrome P-450 Enzyme System/biosynthesis/isolation & purification/*metabolism
Department of Integrative Medical Sciences
Enzyme Induction/drug effects
Enzymologic
Gene Expression Regulation
Inbred Strains
Journal of biochemical toxicology
Lai T S
Liver/drug effects/*enzymology
Liver/enzymology
Mesocricetus
Methylcholanthrene/*pharmacology
Microsomes
Mutagenicity Tests
NEOMED College of Medicine
Rats
Salmonella typhimurium/enzymology/genetics
Subcellular Fractions/drug effects/enzymology
-
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
12012–12019
Issue
20
Volume
265
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 cholesterol 7 alpha-hydroxylase in the liver. Cloning, sequencing, and regulation of cholesterol 7 alpha-hydroxylase mRNA.
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
1990
1990-07
Subject
The topic of the resource
Female; Animals; Rats; Amino Acid Sequence; *Gene Expression Regulation; Kinetics; Base Sequence; Immunoblotting; Molecular Sequence Data; Steroid Hydroxylases/*genetics; Circadian Rhythm; DNA/genetics/isolation & purification; Restriction Mapping; Enzyme Induction; Liver/drug effects/*enzymology; Cell Fractionation; Cholesterol 7-alpha-Hydroxylase/biosynthesis/*genetics/immunology; Cholestyramine Resin/pharmacology; Cytochrome P-450 Enzyme System/genetics; Epitopes/analysis; Polyribosomes/metabolism/ultrastructure; Inbred Strains; RNA; Enzymologic; Sequence Homology; Cloning; Nucleic Acid; Messenger/*genetics; Centrifugation; Density Gradient; Molecular/methods
Creator
An entity primarily responsible for making the resource
Li Y C; Wang D P; Chiang J Y
Description
An account of the resource
Monospecific antibody against purified rat liver cholesterol 7 alpha-hydroxylase cytochrome P-450 was used to screen a lambda gt11 cDNA library constructed from immuno-enriched polysomal RNA of cholestyramine-treated female rat liver. Two types of cDNA clones differing in the length of the 3'-untranslated region were identified, and DNA sequences were determined. The full length clone contains 3561 base pairs plus a long poly(A) tail. The amino acid sequence deduced from the open reading frame revealed a unique P-450 protein containing 503 amino acid residues which belonged to a new gene family designated family VII or CYP7. Southern blot hybridization experiments indicated that the minimal size of P-450 VII gene was 11 kilobase pairs (kb), and there was probably only one gene in this new family. Northern blot hybridization using specific cDNA probes revealed at least two major mRNA species of about 4.0 kb and 2.1 kb, respectively. These two mRNA species may be derived from the use of different polyadenylation signals and reverse-transcribed to two types of cDNA clones. Cholesterol 7 alpha-hydroxylase mRNAs were induced 2- to 3-fold in rat liver by cholestyramine treatment. The mRNA level was rapidly reduced upon the removal of the inducer. Similarly, cholesterol feeding induced enzyme activity, protein, and mRNA levels in the rat by 2-fold, suggesting that cholesterol is an important regulator of cholesterol 7 alpha-hydroxylase in the liver. On the other hand, dexamethasone and pregnenolone-16 alpha-carbonitrile drastically reduced the activity, protein, and mRNA levels. These experiments suggest that the induction of cholesterol 7 alpha-hydroxylase activity by cholestyramine or cholesterol and inhibition of cholesterol 7 alpha-hydroxylase activity by bile acid feedback are results of the rapid turnover of cholesterol 7 alpha-hydroxylase enzyme and mRNA levels.
Rights
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Gene Expression Regulation
1990
Amino Acid Sequence
Animals
Base Sequence
Cell Fractionation
Centrifugation
Chiang J Y
Cholesterol 7-alpha-Hydroxylase/biosynthesis/*genetics/immunology
Cholestyramine Resin/pharmacology
Circadian Rhythm
Cloning
Cytochrome P-450 Enzyme System/genetics
Density Gradient
Department of Integrative Medical Sciences
DNA/genetics/isolation & purification
Enzyme Induction
Enzymologic
Epitopes/analysis
Female
Immunoblotting
Inbred Strains
Kinetics
Li Y C
Liver/drug effects/*enzymology
Messenger/*genetics
Molecular Sequence Data
Molecular/methods
NEOMED College of Medicine
Nucleic Acid
Polyribosomes/metabolism/ultrastructure
Rats
Restriction Mapping
RNA
Sequence Homology
Steroid Hydroxylases/*genetics
The Journal of biological chemistry
Wang D P
-
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
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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
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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
9833–9839
Issue
15
Volume
272
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
Orphan receptors chicken ovalbumin upstream promoter transcription factor II (COUP-TFII) and retinoid X receptor (RXR) activate and bind the rat cholesterol 7alpha-hydroxylase gene (CYP7A).
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
1997
1997-04
Subject
The topic of the resource
Animals; Rats; *Gene Expression Regulation; Cholesterol 7-alpha-Hydroxylase/*genetics/metabolism; Nuclear Proteins/*metabolism; Chickens; Transcription Factors/*metabolism; DNA-Binding Proteins/*metabolism; Retinoid X Receptors; COUP Transcription Factor II; COUP Transcription Factors; Circadian Rhythm; COUP Transcription Factor I; Recombinant Proteins/genetics/metabolism; Receptors; Models; Genetic; Enzymologic; Molecular; Electrophoresis; Polyacrylamide Gel; Promoter Regions; *Receptors; Steroid; Glucocorticoid/*genetics; Retinoic Acid/*metabolism
Creator
An entity primarily responsible for making the resource
Stroup D; Crestani M; Chiang J Y
Description
An account of the resource
The cholesterol 7alpha-hydroxylase gene (CYP7A) is transcriptionally regulated by a number of factors, including hormones, bile acids, and diurnal rhythm. Previous studies have identified a region from nucleotides (nt) -74 to -55 of the rat CYP7A promoter that enhanced bile acid repression of the SV40 early promoter, as assayed with a luciferase reporter gene in transiently transfected HepG2 cells. The rat CYP7A promoter/reporter activity was strongly stimulated by cotransfection with an expression plasmid encoding the nuclear hormone receptor chicken ovalbumin upstream promoter transcription factor II (COUP-TFII) in a dose-dependent manner. Site-directed mutagenesis in the region of nt -74 to -55 altered this stimulation. Recombinant COUP-TFII expressed in HepG2 or COS-1 cells were found to bind to nt -74 -55 and nt -149 -128 probes by electrophoretic mobility shift assay (EMSA) and by supershifting the corresponding band with
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).
*Gene Expression Regulation
*Receptors
1997
Animals
Chiang J Y
Chickens
Cholesterol 7-alpha-Hydroxylase/*genetics/metabolism
Circadian Rhythm
COUP Transcription Factor I
COUP Transcription Factor II
COUP Transcription Factors
Crestani M
Department of Integrative Medical Sciences
DNA-Binding Proteins/*metabolism
Electrophoresis
Enzymologic
Genetic
Glucocorticoid/*genetics
Models
Molecular
NEOMED College of Medicine
Nuclear Proteins/*metabolism
Polyacrylamide Gel
Promoter Regions
Rats
Receptors
Recombinant Proteins/genetics/metabolism
Retinoic Acid/*metabolism
Retinoid X Receptors
Steroid
Stroup D
The Journal of biological chemistry
Transcription Factors/*metabolism
-
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
191–197
Issue
1
Volume
272
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 human oxysterol 7 alpha-hydroxylase gene (CYP7B1) by Sp1.
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
2001
2001-07
Subject
The topic of the resource
Humans; Protein Binding; Gene Expression Regulation; Cell Line; Transfection; Base Sequence; Binding Sites/genetics; Molecular Sequence Data; Cytochrome P450 Family 7; Mutagenesis; Luciferases/genetics/metabolism; Recombinant Fusion Proteins/genetics/metabolism; CpG Islands/genetics; Cytochrome P-450 Enzyme System/*genetics/metabolism; DNA/genetics; Sequence Deletion; Sp1 Transcription Factor/metabolism/*physiology; Steroid Hydroxylases/*genetics/metabolism; Cultured; Binding; Competitive; Transcription; Genetic; Enzymologic; Tumor Cells; Site-Directed; Regulatory Sequences; Nucleic Acid/genetics
Creator
An entity primarily responsible for making the resource
Wu Z; Chiang J Y
Description
An account of the resource
Oxysterol 7 alpha-hydroxylase catalyzes hydroxylation of oxysterols and neurosterols and plays a role in the alternative bile acid synthesis pathway. This gene is widely expressed in many organs and peripheral tissues and may protect tissues from the toxicity of oxysterols. Mutation in CYP7B1 caused neonatal cholestasis. To examine the regulatory mechanisms governing CYP7B1 expression, the 5' flanking sequence of the CYP7B1 was analyzed and revealed a CpG island of about 1.2 kb. Transient transfection assays of deletion mutants of the CYP7B1 promoter-luciferase reporter gene in human liver-derived HepG2, fibroblast NT1088, and human embryonic kidney 293 cell lines revealed that the region from -291 to +189 was critical for gene transcription. Three GC box sequences located between -25 and +10 were essential for basal transcription because mutations of these sequences markedly reduced promoter activity. Sp1 and Sp3 bound to these sequences as demonstrated by DNase I footprinting assays and electrophoretic mobility shift assay. Thus, regulation of CYP7B1 transcription by Sp1 may play a pivotal role in regulating oxysterol levels, which regulate cholesterol metabolism.
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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).
2001
Base Sequence
Binding
Binding Sites/genetics
Cell Line
Chiang J Y
Competitive
CpG Islands/genetics
Cultured
Cytochrome P-450 Enzyme System/*genetics/metabolism
Cytochrome P450 Family 7
Department of Integrative Medical Sciences
DNA/genetics
Enzymologic
gene
Gene Expression Regulation
Genetic
Humans
Luciferases/genetics/metabolism
Molecular Sequence Data
Mutagenesis
NEOMED College of Medicine
Nucleic Acid/genetics
Protein Binding
Recombinant Fusion Proteins/genetics/metabolism
Regulatory Sequences
Sequence Deletion
Site-Directed
Sp1 Transcription Factor/metabolism/*physiology
Steroid Hydroxylases/*genetics/metabolism
Transcription
Transfection
Tumor Cells
Wu Z