Histone deacetylase inhibitors: Anticancer compounds
Abstract
The reversible acetylation of proteins is mediated by histone acetyltransferases which acetylate proteins and histone deacetylases that remove the acetyl groups. High levels of histone acetylation are correlated with active genes, while hypoacetylation of histones corresponds with gene repression. Importantly, acetylation also occurs on non-histone proteins and this can affect the activity and stability of these proteins. Aberrant epigenetic changes are a common hallmark of tumors and imbalances in the activities of deacetylases have been associated with cancers. Accordingly, inhibitors to the histone deacetylases are in clinical trials for the treatment of several cancer types. These drugs mediate a number of molecular changes and in turn can induce cell cycle arrest, apoptosis or differentiation of cancer cells while displaying limited toxicity in normal cells.
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Broad specificity HDAC inhibitors sensitize cancer cells to DNA-damaging treatments.
“broad specificity HDAC inhibitors are promising anti-cancer drugs that sensitize cancer cells to DNA-damaging treatments24,27,28”
From Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining (2010) · cites this paper as [27]
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Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
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- Authors
- Smith, K. T., & Workman, J. L.
- Affiliations
- Stowers Institute for Medical Research (US)
- Corresponding author
- Workman, Jerry L.
- ORCID
- Workman, Jerry L.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 41
- Issue
- 1
- Pages
- 21-25
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W1968031432
- Cited by
- 90
- References
- 49
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 5 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 5 · 2016: 10 · 2015: 3 · 2014: 7 · 2013: 7 · 2012: 8
- FWCI
- 0.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r37gm047867-17)
- National Institute of General Medical Sciences (R37-GM-047867)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase inhibitors, histone acetylation, histone acetyltransferase, gene repression, non-histone protein acetylation, cell cycle arrest, apoptosis, tumor cell differentiation, anticancer agents
- MeSH terms
- Animals, Antineoplastic Agents, Cell Cycle, Cell Differentiation, Enzyme Inhibitors, Histone Deacetylases, Histones, Humans, Neoplasms, Structure-Activity Relationship, Apoptosis, Epigenesis, Genetic, Histone Deacetylase Inhibitors
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