Evidence map›Paper›PMID 11574686›Full record

ArticleNucleic acids research2001

Suppression of sterol 12alpha-hydroxylase transcription by the short heterodimer partner: insights into the repression mechanism.

A del Castillo-Olivares, G Gil

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
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  10. Nuclear factor-E2-related factor 2 is a major determinant of bile acid homeostasis in the liver and intestine.American journal of physiology. Gastrointestinal and liver physiology · 2012
    Article
  11. Farnesoid X receptor represses hepatic human APOA gene expression.The Journal of clinical investigation · 2011
    Article
  12. Review
  13. Article
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  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

A del Castillo-OlivaresDepartment of Biochemistry and Molecular Biophysics, Medical College of Virginia, PO Box 980614, Richmond, VA 23298-0614, USA.
G Gil
Virginia Commonwealth University Medical Center · US

Funding

TRANSCRIPTIONAL REGULATION OF STEROL 12-ALPHA-HYDROLASEP01DK038030 · NIDDK · VIRGINIA COMMONWEALTH UNIVERSITY · PI HYLEMON, PHILLIP B · 1987 to 2006
$6.9M
REGULATION OF CHOLESTEROL 7 ALPHA-HYDROXYLASER01DK044218 · NIDDK · VIRGINIA COMMONWEALTH UNIVERSITY · PI GIL, GREGORIO · 1991 to 1998
–
NIDDK NIH HHS DK 38030NIDDK NIH HHS DK44218NIDDK NIH HHS P01 DK038030
6 · The paper itself

Abstract

Cholesterol conversion to bile acids is subject to a feedback regulatory mechanism by which bile acids down-regulate their own synthesis. This regulation occurs at the level of transcription of several genes encoding enzymes in the bile acid biosynthetic pathway. One of these enzymes is sterol 12alpha-hydroxylase/CYP8B1 (12alpha-hydroxylase), the specific enzyme required for cholic acid synthesis. The levels of this enzyme determine the ratio of cholic acid to chenodeoxycholic acid and thus the hydrophobicity of the circulating bile acid pool. Previous studies from this laboratory showed that fetoprotein transcription factor (FTF) is required for 12alpha-hydroxylase promoter activity and bile acid-mediated regulation. Here, we report that the short heterodimer partner (SHP) suppresses 12alpha-hydroxylase promoter activity via an interaction with FTF. Hepatic nuclear factor-4 (HNF-4) binds and activates the 12alpha-hydroxylase promoter and is required for 12alpha-hydroxylase promoter activity. Although HNF-4 interacts with SHP, it is not involved in SHP-mediated suppression of 12alpha-hydroxylase promoter activity. FTF and not HNF-4 is the factor involved in regulation of 12alpha-hydroxylase promoter activity by bile acids through its interaction with SHP. Finally, interaction of SHP with FTF displaces FTF binding to its sites within the 12alpha-hydroxylase promoter. These results provide insights into the mechanism of action of bile acid-mediated regulation of sterol 12alpha-hydroxylase transcription.

Indexed as

Basic Helix-Loop-Helix Leucine Zipper Transcription FactorsBile Acids and SaltsBinding SitesCell LineCytochrome P-450 Enzyme SystemDNA-Binding ProteinsDown-RegulationGenes, ReporterHepatocyte Nuclear Factor 4HumansPhosphoproteinsPromoter Regions, GeneticProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearRepressor ProteinsSteroid 12-alpha-HydroxylaseBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBile Acids and SaltsCytochrome P-450 Enzyme SystemDNA-Binding Proteinsfetoprotein transcription factorHepatocyte Nuclear Factor 4MLX protein, humannuclear receptor subfamily 0, group B, member 2PhosphoproteinsReceptors, Cytoplasmic and NuclearRepressor ProteinsSteroid 12-alpha-HydroxylaseSteroid HydroxylasesTranscription Factors

Identifiers

PMID11574686
PMCPMC60248
OpenAlexW1586509449

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.