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Mol Oncol. 2012 Dec;6(6):579-89. doi: 10.1016/j.molonc.2012.07.003. Epub 2012 Aug 27.

Histone deacetylases and cancer.

Author information

1
Cellular Differentiation Group, Cancer Epigenetics and Biology Program, Bellvitge Biomedical Research Institute, Av. Gran Via s/n km 2.7, 08908 L'Hospitalet, Barcelona, Spain.

Abstract

Reversible acetylation of histone and non-histone proteins is one of the most abundant post-translational modifications in eukaryotic cells. Protein acetylation and deacetylation are achieved by the antagonistic actions of two families of enzymes, histone acetyltransferases (HATs) and histone deacetylases (HDACs). Aberrant protein acetylation, particularly on histones, has been related to cancer while abnormal expression of HDACs has been found in a broad range of cancer types. Therefore, HDACs have emerged as promising targets in cancer therapeutics, and the development of HDAC inhibitors (HDIs), a rapidly evolving area of clinical research. However, the contributions of specific HDACs to a given cancer type remain incompletely understood. The aim of this review is to summarize the current knowledge concerning the role of HDACs in cancer with special emphasis on what we have learned from the analysis of patient samples.

PMID:
22963873
PMCID:
PMC5528343
DOI:
10.1016/j.molonc.2012.07.003
[Indexed for MEDLINE]
Free PMC Article

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