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Journal of Education, Health and Sport

Histone deacetylase inhibitors
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Histone deacetylase inhibitors

Authors

  • Marzena Baran Chair and Department of Biochemistry and Molecular Biology, Medical University of Lublin
  • Paulina Anna Miziak Chair and Department of Biochemistry and Molecular Biology, Medical University of Lublin https://orcid.org/0000-0001-7022-6927
  • Katarzyna Bonio Department of Cell Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin

DOI:

https://doi.org/10.12775/JEHS.2020.10.08.043

Keywords

inhibitors, histone deacetylase, cancer

Abstract

The human genome is contained in chromatin, which is a complex macromolecular complex. It is made of DNA, histones and non-histone proteins. The structure of chromatin and the process of its rearrangement regulate the process of transcription, and hence gene expression.  Deacetylase (HDAC) is a group of enzymes that catalyzes the cleavage of acetyl groups from lysine residues in histone and nonhistone proteins. This reaction is catalyzed by zinc or NAD + ions [3]. Histone deacetylases are present in the cytoplasm or nucleus of eukaryotes [4, 5]. These enzymes have been divided into 5 classes (I, IIa, IIb, III and IV) due to the similarity in structure and origin. Vorinostat is one of the most studied HDAC inhibitors. It belongs to the second generation polar-planar hydroxamic acid derivatives that inhibit class I and II histone deacetylases. Panobinostat and belinostat are HDAC inhibitors derived from hydroxamic acid that have also entered clinical trials. Valproic acid, from the group of aliphatic acids, belongs to inhibitors of class I and IIα deacetylases and is an established drug anticonvulsants. Histone deacetylase inhibitors may be useful in the treatment of neoplasms because they influence the action of factors related to cell proliferation, may cause cell cycle arrest, and coordinate the action of apoptotic factors and induce apoptosis. There are several deacetylase inhibitors available as drugs and are in different phases of clinical trials. They differ in potency and enzyme specificity. However, it is still unknown which deacetylases are essential for initiating and sustaining metabolic pathways leading to tumor development.

References

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. Qiu X i inni, Histone deacetylases inhibitors (HDACis) as novel therapeutic application in various clinical diseases, Progress in Neuro-Psychopharmacology and Biological Psychiatry, 2017, Vol. 72

. Seto E., Yoshida M., Erasers of histone acetylation: the histone deacetylase enzymes,

Cold Spring Harb Perspect Biol., 2014,6(4)

. Seidel C. i inni, , Histone deacetylase 6 in health and disease,

Epigenomics, 2015, 7(1), 103-18

. Wawruszak A i inni., Histone Deacetylase Inhibitors and Phenotypical Transformation of Cancer Cells, Cancers., 2019, 11(2), 148

. Grabarska A, Dmoszyńska-Graniczka M, Nowosadzka E, Stepulak A. Inhibitory deacetylaz histonów - mechanizmy działania na poziomie molekularnym i zastosowania kliniczne [Histone deacetylase inhibitors - molecular mechanisms of actions and clinical applications]. Postepy Hig Med Dosw (Online). 2013 Aug 2;67:722-35. Polish. doi: 10.5604/17322693.1061381. PMID: 24018438.

. Kuendgen A., Knipp S., Fox F., Strupp C., Hildebrandt B., Steidl C., Germing U., Haas R., Gattermann N.: Results of a phase 2 study of valproic acid alone or in combination with all-trans retinoic acid in 75 patients with myelodysplastic syndrome and relapsed or refractory acute myeloid leukemia. Ann. Hematol., 2005; 84, Suppl 1: 61-66

. Eckschlager T, Plch J, Stiborova M, Hrabeta J. Histone Deacetylase Inhibitors as Anticancer Drugs. Int J Mol Sci. 2017 Jul 1;18(7):1414. doi: 10.3390/ijms18071414. PMID: 28671573; PMCID: PMC5535906.

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Published

2020-08-23

How to Cite

1.
BARAN, Marzena, MIZIAK, Paulina Anna and BONIO, Katarzyna. Histone deacetylase inhibitors. Journal of Education, Health and Sport. Online. 23 August 2020. Vol. 10, no. 8, pp. 361-364. [Accessed 6 July 2025]. DOI 10.12775/JEHS.2020.10.08.043.
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Issue

Vol. 10 No. 8 (2020)

Section

Review Articles

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The periodical offers access to content in the Open Access system under the Creative Commons Attribution-NonCommercial-ShareAlike 4.0

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