Evidence map›Paper›PMID 31311992›Full record

ArticleScientific reports2019

Regulatory mechanisms leading to differential Acyl-CoA synthetase 4 expression in breast cancer cells.

Melina A Dattilo, Yanina Benzo, Lucía M Herrera, Jesica G Prada, Ana F Castillo, Ulises D Orlando, Ernesto J Podesta, Paula M Maloberti

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. 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
1.9field-weighted citation impact, top 16% 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, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. ACSL4-mediated H3K9 and H3K27 hyperacetylation upregulates SNAIL to drive TNBC metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  7. Article
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  15. SP and KLF Transcription Factors in Cancer Metabolism.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Targeting ferroptosis in breast cancer.Biomarker research · 2020
    Review
  19. Article
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

8 authors at 1 institution in 1 country.

Melina A DattiloBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Yanina BenzoBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Lucía M HerreraBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Jesica G PradaBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Ana F CastilloBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Ulises D OrlandoBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Ernesto J PodestaBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina.
Paula M MalobertiBiomedical Research Institute, INBIOMED, Department of Biochemistry, School of Medicine, University of Buenos Aires, CABA, Buenos Aires, Argentina. malobertipm@hotmail.com.
University of Buenos Aires · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acyl-CoA synthetase 4 (ACSL4) overexpression plays a causal role in the aggressiveness of triple negative breast cancer. In turn, a negative correlation has been established between ACSL4 and estrogen receptor alpha (ERα) expression. However, the upstream regulatory mechanisms leading to differential ACSL4 expression between triple negative breast cancer and ERα-positive cells remained unknown. We performed the characterization of the human ACSL4 promoter and the identification of transcription factors involved. Deletional analysis demonstrated the proximal 43 base pairs of the promoter are involved in overexpression. By site directed mutagenesis we describe that retinoid-related orphan receptor alpha (RORα), Sp1 and E2F elements are involved in the promoter activity. We established for the first time that estrogen-related receptor alpha (ERRα) is a transcription factor involved in the higher activation of the human ACSL4 promoter in breast cancer cells. Furthermore, a combination of inhibitors of ACSL4 and ERRα produced a synergistic decrease in MDA-MB-231 cell proliferation. We also demonstrated that ERα restoration in triple negative breast cancer cells downregulates ACSL4 expression. The results presented in this manuscript demonstrated transcriptional mechanism is involved in the different expression of ACSL4 in human breast cancer cell lines of different aggressiveness.

Indexed as

Promoter Regions, GeneticUp-RegulationCell Line, TumorCoenzyme A LigasesE2F Transcription FactorsEstrogen Receptor alphaFemaleGene Expression Regulation, NeoplasticHumansLong-Chain-Fatty-Acid-CoA LigaseMCF-7 CellsMutagenesis, Site-DirectedNuclear Receptor Subfamily 1, Group F, Member 1Sp1 Transcription FactorTriple Negative Breast NeoplasmsCoenzyme A LigasesE2F Transcription FactorsESR1 protein, humanEstrogen Receptor alphaLong-Chain-Fatty-Acid-CoA LigaseNuclear Receptor Subfamily 1, Group F, Member 1RORA protein, humanSP1 protein, humanSp1 Transcription Factor

Identifiers

PMID31311992
PMCPMC6635356
OpenAlexW2962427338

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.