Acetylation of histone H3 in cancer progression and prognosis
Open accessAbstract
Cancer is a multifactorial disease resulting from both genetic factors and epigenetic changes. Histone acetylation, a post-translational modification, which alters chromatin architecture and regulates gene expression is associated with cancer initiation, development and progression. Aberrations in global histone acetylation levels are observed in various cancer cells and are also associated with patients' tumor aggressiveness. Therefore, histone acetylation may have prognostic utility and serve as a potential biomarker of cancer progression and patients' prognosis. The reversible modification of histones by an acetyl group is versatile. One particular histone can be acetylated on different lysine residues, subsequently resulting in different biological outcomes. Here, we discuss recent findings on the acetylation of the highly conserved histone protein H3 in the context of cancer biology. Specifically, we review the acetylation of particular H3 residues in various cancer types. We further highlight the significance of H3 acetylation levels as a potential cancer biomarker with prognostic implications.
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Post-translational modifications predominantly occur on N-terminal histone tails and include acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns known as the histone code.
“These PTMs predominantly occur on the N-terminal histone tails and include acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns often referred to as the “histone code,” which influences transcription in a context-dependent manner (Millán-Zambrano et al., 2022; Miziak et al., 2024; Jenuwein and Allis, 2001; Lam et al., 2019).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Miziak et al., 2024
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Tachaveeraphong, W., & Phattarataratip, E. (2024) · International Dental Journal · doi:10.1016/j.identj.2024.01.011 · Cited by 13 · see citing works
SIRT1 mediates breast cancer development and tumorigenesis controlled by estrogen-related receptor β
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Epigenetic-based differentiation therapy for Acute Myeloid Leukemia
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Post-Translational Modification of Histone Proteins
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Sorted by citations
Lv, L.-Z., Wang, Z.-D., Ren, J.-J., Li, L.-H., Liu, X.-B., Li, J.-L., Zhu, H., Jiang, B., Han, Y.-P., Zhou, X.-M., et al. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2025.1722453 · Cited by 7 · see citing works
“…acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns often referred to as the “histone code,” which influences transcription in a context-dependent manner (Millán-Zambrano et al., 2022; Miziak et al., 2024; Jenuwein and Allis, 2001; Lam et al., 2019).”
- Authors
- Miziak, P., Baran, M., Borkiewicz, L., Trombik, T., & Stepulak, A.
- Affiliations
- Medical University of Lublin (PL)
- Corresponding author
- Miziak, Paulina
- Stepulak, Andrzej
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2024-10-12
- Volume
- 25
- Issue
- 20
- Pages
- 10982
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC11507103
- OpenAlex
- W4403403513
- Cited by
- 49
- References
- 101
- Citations by year
- 2026: 22 · 2025: 27
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Medical University in Lublin (DS715)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- 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
- Keywords
- histone H3 acetylation, tumor progression, cancer prognosis, prognostic factors, lysine acetylation, epigenetic regulation, chromatin structure, gene expression regulation, tumor aggressiveness
- MeSH terms
- Acetylation, Animals, Histones, Humans, Neoplasms, Prognosis, Protein Processing, Post-Translational, Biomarkers, Tumor, Disease Progression, Epigenesis, Genetic
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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