Evidence map›Paper›PMID 12626711›Full record

ArticleNucleic acids research2003

Histone deacetylase inhibitors stimulate mitochondrial HMG-CoA synthase gene expression via a promoter proximal Sp1 site.

Nuria Camarero, Alícia Nadal, María José Barrero, Diego Haro, Pedro F Marrero

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 53 citations in OpenAlex.

  1. Histone deacetylases in cancer metabolic reprogramming.Experimental & molecular medicine · 2026
    Review
  2. The role of acetylation and deacetylation in cancer metabolism.Clinical and translational medicine · 2025
    Review
  3. Article
  4. Nutritional Epigenetics in Cancer.Advances in nutrition (Bethesda, Md.) · 2022
    Review
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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

5 authors at 1 institution in 1 country.

Nuria CamareroDepartment of Biochemistry and Molecular Biology, School of Pharmacy, University of Barcelona, Av. Diagonal 643, 08028 Barcelona, Spain.
Alícia Nadal
María José Barrero
Diego Haro
Pedro F Marrero
Universitat de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The expression of mitochondrial HMG-CoA synthase in the colon has been correlated with the levels of butyrate present in this tissue. We report here that the effect of butyrate on mitochondrial HMG-CoA synthase gene expression is exerted in vivo at the transcriptional level, and that trichostatin A (TSA), a specific histone deacetylase inhibitor, also induces transcriptional activity and mRNA expression of the gene in human cell lines derived from colon carcinoma. Using chromatin immunoprecipitation assays, we show that histone deacetylase 1 (HDAC1) is associated with the endogenous mitochondrial HMG-CoA synthase promoter and that TSA induction correlates with hyperacetylation of H4 histone associated with the 5' flanking region of the gene. Overexpression of HDAC1 activity leads consistently to mitochondrial HMG-CoA synthase promoter hypoacetylation and reduces its transcriptional activity. The effect of butyrate and TSA maps to a single Sp1 site present in the proximal promoter of the gene, which is able to bind Sp1 and Sp3 proteins. Interestingly, the binding affinity of Sp1 and Sp3 proteins to the Sp1 site correlates with the TSA responsiveness of the promoter. Using a one-hybrid system (GAL4-Sp1 and GAL4-Sp3), we show that both proteins can mediate responsiveness to TSA in CaCo-2 cells employing distinct mechanisms.

Indexed as

Histone Deacetylase InhibitorsAcetylationAnimalsBinding SitesButyratesCaco-2 CellsCoenzyme A LigasesDNA-Binding ProteinsEnzyme InhibitorsFemaleGene Expression Regulation, EnzymologicHistone DeacetylasesHistonesHT29 CellsHumansHydroxamic AcidsButyratesCoenzyme A LigasesDNA-Binding ProteinsEnzyme InhibitorsHistone Deacetylase InhibitorsHistone DeacetylasesHistonesHydroxamic AcidsHydroxymethylglutaryl-CoA SynthaseRecombinant Fusion ProteinsRNA, MessengerSp1 Transcription FactorSP3 protein, humanSp3 protein, mouseSp3 Transcription FactorTranscription Factorstrichostatin A

Identifiers

PMID12626711
PMCPMC152864
OpenAlexW2123822150

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.