Evidence map›Paper›PMID 23321683›Full record

ArticleEpigenetics2013

Time- and residue-specific differences in histone acetylation induced by VPA and SAHA in AML1/ETO-positive leukemia cells.

Valentina Barbetti, Antonella Gozzini, Giulia Cheloni, Ilaria Marzi, Emiliano Fabiani, Valeria Santini, Persio Dello Sbarba, Elisabetta Rovida

Erratum issuedOpen access · hybridAbstract readComparative Study
In one paragraph

Article in Epigenetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  3. Molecules (Basel, Switzerland) · 2024
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  8. Oncotarget · 2018
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  11. [Effect of histone acetylation/deacetylation imbalances on key gene of planar cell polarity pathway].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2017
    Article
  12. Article
  13. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Valentina BarbettiDipartimento di Patologia e Oncologia Sperimentali, Università degli Studi di Firenze, Istituto Toscano Tumori, Firenze, Italy.
Antonella Gozzini
Giulia Cheloni
Ilaria Marzi
Emiliano Fabiani
Valeria Santini
Persio Dello Sbarba
Elisabetta Rovida
Istituto di Ematologia di Bologna · ITUniversity of Florence · ITTumori Foundation · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We analyzed the activity of the histone deacetylase inhibitor (HDACi) suberoyl-anilide hydroxamic acid (SAHA) on Kasumi-1 acute myeloid leukemia (AML) cells expressing AML1/ETO. We also compared the effects of SAHA to those of valproic acid (VPA), a short-chain fatty acid HDACi. SAHA and VPA induced histone H3 and H4 acetylation, myeloid differentiation and massive early apoptosis. The latter effects were not determined by either drug in AML cell lines, such as NB4 or THP-1, not expressing AML1/ETO. SAHA was more rapid and effective than VPA in increasing H3 and H4 acetylation in total Kasumi-1 cell lysates and more effective than VPA in inducing acetylation of H4K8, H4K12, H4K16 residues. At the promoter of IL3, a transcriptionally-silenced target of AML1/ETO, SAHA was also more rapid than VPA in inducing total H4, H4K5, H4K8 and H3K27 acetylation, while VPA was more effective than SAHA at later times in inducing acetylation of total H4, H4K12, H4K16, as well as total H3. Consistent with these differences, SAHA induced the expression of IL3 mRNA more rapidly than VPA, while the effect of VPA was delayed. These differences might be exploited to design clinical trials specifically directed to AML subtypes characterized by constitutive HDAC activation. Our results led to include SAHA, an FDA-approved drug, among the HDACi active in the AML1/ETO-expressing AML cells.

Indexed as

AcetylationApoptosisCell DifferentiationCore Binding Factor Alpha 2 SubunitGene Expression Regulation, LeukemicHistone Deacetylase InhibitorsHistonesHumansHydroxamic AcidsLeukemia, Myeloid, AcuteLysineProto-Oncogene ProteinsRUNX1 Translocation Partner 1 ProteinTime FactorsTranscription FactorsValproic AcidCore Binding Factor Alpha 2 SubunitHistone Deacetylase InhibitorsHistonesHydroxamic AcidsLysineProto-Oncogene ProteinsRUNX1 protein, humanRUNX1T1 protein, humanRUNX1 Translocation Partner 1 ProteinTranscription FactorsValproic AcidVorinostatAcute myeloid leukemiahistone deacetylase inhibitorssuberoyl-anilide hydroxamic acidtargeted therapyvalproic acid

Identifiers

PMID23321683
PMCPMC3592907
OpenAlexW2057253428

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.