Histone deacetylase inhibitors exert anti-tumor effects on human adherent and stem-like glioma cells.


Journal

Clinical epigenetics
ISSN: 1868-7083
Titre abrégé: Clin Epigenetics
Pays: Germany
ID NLM: 101516977

Informations de publication

Date de publication:
17 01 2019
Historique:
received: 01 08 2018
accepted: 17 12 2018
entrez: 19 1 2019
pubmed: 19 1 2019
medline: 21 8 2019
Statut: epublish

Résumé

The diagnosis of glioblastoma (GBM), a most aggressive primary brain tumor with a median survival of 14.6 months, carries a dismal prognosis. GBMs are characterized by numerous genetic and epigenetic alterations, affecting patient survival and treatment response. Epigenetic mechanisms are deregulated in GBM as a result of aberrant expression/activity of epigenetic enzymes, including histone deacetylases (HDAC) which remove acetyl groups from histones regulating chromatin accessibility. Nevertheless, the impact of class/isoform-selective HDAC inhibitors (HDACi) on glioma cells, including glioma stem cells, had not been systematically determined. Comprehensive analysis of the public TCGA dataset revealed the increased expression of HDAC 1, 2, 3, and 7 in malignant gliomas. Knockdown of HDAC 1 and 2 in human GBM cells significantly decreased cell proliferation. We tested the activity of 2 new and 3 previously described HDACi with different class/isoform selectivity on human GBM cells. All tested compounds exerted antiproliferative properties on glioma cells. However, the HDACi 1 and 4 blocked proliferation of glioblastoma cells leading to G2/M growth arrest without affecting astrocyte survival. Moreover, 1 and 4 at low micromolar concentrations displayed cytotoxic and antiproliferative effects on sphere cultures enriched in glioma stem cells. We identified two selective HDAC inhibitors that blocked proliferation of glioblastoma cells, but did not affect astrocyte survival. These new and highly effective inhibitors should be considered as promising candidates for further investigation in preclinical GBM models.

Sections du résumé

BACKGROUND
The diagnosis of glioblastoma (GBM), a most aggressive primary brain tumor with a median survival of 14.6 months, carries a dismal prognosis. GBMs are characterized by numerous genetic and epigenetic alterations, affecting patient survival and treatment response. Epigenetic mechanisms are deregulated in GBM as a result of aberrant expression/activity of epigenetic enzymes, including histone deacetylases (HDAC) which remove acetyl groups from histones regulating chromatin accessibility. Nevertheless, the impact of class/isoform-selective HDAC inhibitors (HDACi) on glioma cells, including glioma stem cells, had not been systematically determined.
RESULTS
Comprehensive analysis of the public TCGA dataset revealed the increased expression of HDAC 1, 2, 3, and 7 in malignant gliomas. Knockdown of HDAC 1 and 2 in human GBM cells significantly decreased cell proliferation. We tested the activity of 2 new and 3 previously described HDACi with different class/isoform selectivity on human GBM cells. All tested compounds exerted antiproliferative properties on glioma cells. However, the HDACi 1 and 4 blocked proliferation of glioblastoma cells leading to G2/M growth arrest without affecting astrocyte survival. Moreover, 1 and 4 at low micromolar concentrations displayed cytotoxic and antiproliferative effects on sphere cultures enriched in glioma stem cells.
CONCLUSIONS
We identified two selective HDAC inhibitors that blocked proliferation of glioblastoma cells, but did not affect astrocyte survival. These new and highly effective inhibitors should be considered as promising candidates for further investigation in preclinical GBM models.

Identifiants

pubmed: 30654849
doi: 10.1186/s13148-018-0598-5
pii: 10.1186/s13148-018-0598-5
pmc: PMC6337817
doi:

Substances chimiques

Benzamides 0
Histone Deacetylase Inhibitors 0
Pyrimidines 0
mocetinostat A6GWB8T96J
HDAC1 protein, human EC 3.5.1.98
HDAC2 protein, human EC 3.5.1.98
HDAC7 protein, human EC 3.5.1.98
Histone Deacetylase 1 EC 3.5.1.98
Histone Deacetylase 2 EC 3.5.1.98
Histone Deacetylases EC 3.5.1.98
histone deacetylase 3 EC 3.5.1.98

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Pagination

11

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Auteurs

Halina Was (H)

Laboratory of Molecular Neurobiology, Neurobiology Center, The Nencki Institute of Experimental Biology, 3 Pasteur Str, 02-093, Warsaw, Poland.
Laboratory of Molecular Oncology, Military Institute of Medicine, 128 Szaserow Str, 04-141, Warsaw, Poland.

Sylwia K Krol (SK)

Laboratory of Molecular Neurobiology, Neurobiology Center, The Nencki Institute of Experimental Biology, 3 Pasteur Str, 02-093, Warsaw, Poland.

Dante Rotili (D)

Department of Drug Chemistry and Technologies, Sapienza University of Roma, P.le A. Moro 5, 00185, Rome, Italy.

Antonello Mai (A)

Department of Drug Chemistry and Technologies, Sapienza University of Roma, P.le A. Moro 5, 00185, Rome, Italy.
Pasteur Institute, Cenci-Bolognetti Foundation, Sapienza University of Rome, 00185, Rome, Italy.

Bartosz Wojtas (B)

Laboratory of Molecular Neurobiology, Neurobiology Center, The Nencki Institute of Experimental Biology, 3 Pasteur Str, 02-093, Warsaw, Poland.

Bozena Kaminska (B)

Laboratory of Molecular Neurobiology, Neurobiology Center, The Nencki Institute of Experimental Biology, 3 Pasteur Str, 02-093, Warsaw, Poland.

Marta Maleszewska (M)

Laboratory of Molecular Neurobiology, Neurobiology Center, The Nencki Institute of Experimental Biology, 3 Pasteur Str, 02-093, Warsaw, Poland. m.maleszewska@nencki.gov.pl.

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Classifications MeSH