Display options
Cite
Librizzi M, Chiarelli R, Bosco L, et al. The Histone Deacetylase Inhibitor JAHA Down-Regulates pERK and Global DNA Methylation in MDA-MB231 Breast Cancer Cells. Materials (Basel). 2015;8(10):7041-7047doi: 10.3390/ma8105358.
Librizzi, M., Chiarelli, R., Bosco, L., Sansook, S., Gascon, J. M., Spencer, J., Caradonna, F., & Luparello, C. (2015). The Histone Deacetylase Inhibitor JAHA Down-Regulates pERK and Global DNA Methylation in MDA-MB231 Breast Cancer Cells. Materials (Basel, Switzerland), 8(10), 7041-7047. https://doi.org/10.3390/ma8105358
Librizzi, Mariangela, et al. "The Histone Deacetylase Inhibitor JAHA Down-Regulates pERK and Global DNA Methylation in MDA-MB231 Breast Cancer Cells." Materials (Basel, Switzerland) vol. 8,10 (2015): 7041-7047. doi: https://doi.org/10.3390/ma8105358
Librizzi M, Chiarelli R, Bosco L, Sansook S, Gascon JM, Spencer J, Caradonna F, Luparello C. The Histone Deacetylase Inhibitor JAHA Down-Regulates pERK and Global DNA Methylation in MDA-MB231 Breast Cancer Cells. Materials (Basel). 2015 Oct 16;8(10):7041-7047. doi: 10.3390/ma8105358. PMID: 28793617; PMCID: PMC5455366.
Copy Download .nbib Format: NLM
Share it on

Materials (Basel). 2015 Oct 16;8(10):7041-7047. doi: 10.3390/ma8105358.

The Histone Deacetylase Inhibitor JAHA Down-Regulates pERK and Global DNA Methylation in MDA-MB231 Breast Cancer Cells.

Materials (Basel, Switzerland)

Mariangela Librizzi, Roberto Chiarelli, Liana Bosco, Supojjanee Sansook, Jose M Gascon, John Spencer, Fabio Caradonna, Claudio Luparello

Affiliations

  1. Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), Edificio 16, Università di Palermo, Viale delle Scienze, Palermo 90128, Italy. [email protected].
  2. Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), Edificio 16, Università di Palermo, Viale delle Scienze, Palermo 90128, Italy. [email protected].
  3. Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), Edificio 16, Università di Palermo, Viale delle Scienze, Palermo 90128, Italy. [email protected].
  4. Department of Chemistry, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QJ, UK. [email protected].
  5. Department of Chemistry, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QJ, UK. [email protected].
  6. Department of Chemistry, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QJ, UK. [email protected].
  7. Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), Edificio 16, Università di Palermo, Viale delle Scienze, Palermo 90128, Italy. [email protected].
  8. Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), Edificio 16, Università di Palermo, Viale delle Scienze, Palermo 90128, Italy. [email protected].

PMID: 28793617 PMCID: PMC5455366 DOI: 10.3390/ma8105358

Abstract

The histone deacetylase inhibitor N¹-(ferrocenyl)-N⁸-hydroxyoctanediamide (JAHA) down-regulates extracellular-signal-regulated kinase (ERK) and its activated form in triple-negative MDA-MB231 breast cancer cells after 18 h and up to 30 h of treatment, and to a lesser extent AKT and phospho-AKT after 30 h and up to 48 h of treatment. Also, DNA methyltransferase 1 (DNMT1), 3b and, to a lesser extent, 3a, downstream ERK targets, were down-regulated already at 18 h with an increase up to 48 h of exposure. Methylation-sensitive restriction arbitrarily-primed (MeSAP) polymerase chain reaction (PCR) analysis confirmed the ability of JAHA to induce genome-wide DNA hypomethylation at 48 h of exposure. Collective data suggest that JAHA, by down-regulating phospho-ERK, impairs DNMT1 and 3b expression and ultimately DNA methylation extent, which may be related to its cytotoxic effect on this cancer cytotype.

Keywords: AKT; DNA methyltransferase (DNMT); extracellular-signal-regulated kinase (ERK); histone deacetylase inhibitor

References

  1. Anticancer Res. 2011 Sep;31(9):2723-32 - PubMed
  2. Nat Genet. 2000 Jan;24(1):88-91 - PubMed
  3. J Leukoc Biol. 2010 Jan;87(1):137-45 - PubMed
  4. Front Oncol. 2014 May 01;4:80 - PubMed
  5. Int J Oncol. 2014 Feb;44(2):451-8 - PubMed
  6. Int J Oncol. 2012 Oct;41(4):1486-94 - PubMed
  7. Gene. 2014 Feb 15;536(1):29-39 - PubMed
  8. Tumour Biol. 2015 Jul;36(7):5051-61 - PubMed
  9. Mol Cell Biol. 2011 Oct;31(19):4119-28 - PubMed
  10. Cold Spring Harb Perspect Med. 2015 Apr 01;5(4):null - PubMed
  11. Autophagy. 2011 Sep;7(9):1028-34 - PubMed
  12. Cancer Res. 2006 Sep 1;66(17):8413-20 - PubMed
  13. Chem Res Toxicol. 2012 Nov 19;25(11):2608-16 - PubMed
  14. Clin Cancer Res. 2005 Sep 1;11(17):6382-9 - PubMed
  15. Dalton Trans. 2014 Jan 14;43(2):817-30 - PubMed
  16. Cancer Lett. 2012 Feb 28;315(2):112-21 - PubMed
  17. Chem Commun (Camb). 2015 May 14;51(39):8353-6 - PubMed
  18. Chemistry. 2013 Jul 29;19(31):10160-9 - PubMed
  19. Chem Biodivers. 2012 Sep;9(9):1849-66 - PubMed
  20. ACS Med Chem Lett. 2011 May 12;2(5):358-362 - PubMed
  21. Cancer Res. 2007 Dec 15;67(24):11481-6 - PubMed
  22. Chem Commun (Camb). 2009 Nov 28;(44):6735-7 - PubMed

Publication Types