Cited by 1,069Histone Deacetylase Inhibitors ResearchEpigenetics and DNA MethylationGenomics and Chromatin Dynamics

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HDAC family: What are the cancer relevant targets?

Witt, Olaf, Deubzer, Hedwig E., Milde, Till, Oehme, Ina·2009·Cancer Letters

DOI 10.1016/j.canlet.2008.08.016

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Abstract

Histone deacetylases comprise a family of 18 genes, which are grouped into classes I-IV based on their homology to their respective yeast orthologues. Classes I, II, and IV consist of 11 family members, which are referred to as "classical" HDACs, whereas the 7 class III members are called sirtuins. Classical HDACs are a promising novel class of anti-cancer drug targets. First HDAC inhibitors have been evaluated in clinical trials and show activity against several cancer diseases. However, these compounds act unselectively against several or all 11 HDAC family members. As a consequence, clinical phase I trials document a wide range of side effects. Therefore, the current challenge in the field is to define the cancer relevant HDAC family member(s) in a given tumor type and to design selective inhibitors, which target cancer cells but leave out normal cells. Knockout of single HDAC family members in mice produces a variety of phenotypes ranging from early embryonic death to viable animals with only discrete alterations, indicating that potential side effects of HDAC inhibitors depend on the selectivity of the compounds. Recently, several studies have shown that certain HDAC family members are aberrantly expressed in several tumors and have non-redundant function in controlling hallmarks of cancer cells. The aim of this review is to discuss individual HDAC family members as drug targets in cancer taking into consideration their function under physiological conditions and their oncogenic potential in malignant disease.

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Inhibition of Histone Deacetylase Activity Promotes Invasion of Human Cancer Cells through Activation of Urokinase Plasminogen Activator
Pulukuri, S. M. K., Gorantla, B., & Rao, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705867200 · Cited by 51
Retracted
The Consensus Coding Sequences of Human Breast and Colorectal Cancers
Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529

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Li, 2008, HDAC6 is required for EGF-induced β-catenin nuclear localization, J. Biol. Chem.

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Wang, L., Hou, X., Fu, H., Pan, X., Xu, W., Tang, W., & Fang, H. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.06.024 · Cited by 47
Small-molecular modulators of cancer-associated epigenetic mechanisms
Itoh, Y., Suzuki, T., & Miyata, N. (2013) · Molecular BioSystems · doi:10.1039/c3mb25410k · Cited by 46
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Hieu, D. T., Anh, D. T., Nguyen, T. M., Pham‐The, H., Le‐Thi‐Thu, H., Kim, J., Kang, J. S., Vu, T. K., Dung, P. T. P., Han, S., et al. (2017) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2017.12.007 · Cited by 46
Melittin Restores PTEN Expression by Down-Regulating HDAC2 in Human Hepatocelluar Carcinoma HepG2 Cells
Zhang, H., Zhao, B., Huang, C., Meng, X., Bian, E., & Li, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095520 · Cited by 46
Small molecules targeting HDAC6 for cancer treatment: Current progress and novel strategies
Huang, Z., Li, L., Cheng, B., & Li, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117218 · Cited by 46
The inhibition of histone deacetylase 8 suppresses proliferation and inhibits apoptosis in gastric adenocarcinoma
Song, S., Wang, Y., Xu, P., Yang, R., Ma, Z., Liang, S., & Zhang, G. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3182 · Cited by 45
Sonic Hedgehog-Induced Histone Deacetylase Activation Is Required for Cerebellar Granule Precursor Hyperplasia in Medulloblastoma
Lee, S. J., Lindsey, S. C., Graves, B., Yoo, S., Olson, J. M., & Langhans, S. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071455 · Cited by 45
HDAC1 and HDAC2 collectively regulate intestinal stem cell homeostasis
Zimberlin, C., Lancini, C., Sno, R., Rosekrans, S. L., McLean, C. M., Vlaming, H., van den Brink, G. R., Bots, M. L., Medema, J. P., & Dannenberg, J. (2015) · The FASEB Journal · doi:10.1096/fj.14-257931 · Cited by 49
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Hamberg, P., Woo, M. M., Chen, L., Verweij, J., Porro, M. G., Zhao, L., Li, W., van der Biessen, D. A. J., Sharma, S., Hengelage, T., et al. (2011) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-011-1693-x · Cited by 45
Clinico-Pathological Association of Delineated miRNAs in Uveal Melanoma with Monosomy 3/Disomy 3 Chromosomal Aberrations
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Retracted
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Krieger, V., Hamacher, A., Gertzen, C. G. W., Senger, J., Zwinderman, M. R. H., Marek, M., Romier, C., Dekker, F. J., Kurz, T., Jung, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00197 · Cited by 46
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Li, S., Chen, X., Mao, L., Zahid, K. R., Wen, J., Zhang, L., Zhang, M., Duan, J., Duan, J., Yin, X., et al. (2018) · Brain Research · doi:10.1016/j.brainres.2018.05.023 · Cited by 45
Design, synthesis and anticancer activities of novel dual poly(ADP-ribose) polymerase-1/histone deacetylase-1 inhibitors
Tian, Y., Xie, Z., & Liao, C. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127036 · Cited by 45
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Swierczynski, S., Klieser, E., Illig, R., Alinger-Scharinger, B., Kiesslich, T., & Neureiter, D. (2015) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2015.1025047 · Cited by 44
Current Limitations And Future Opportunities For Epigenetic Therapies
Cherblanc, F., Chapman‐Rothe, N., Brown, R. E., & Fuchter, M. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.7 · Cited by 44
Synergistic Interaction between the HDAC Inhibitor, MPT0E028, and Sorafenib in Liver Cancer Cells In Vitro and In Vivo
Chen, C.-H., Chen, M.-C., Wang, J.-C., Tsai, A.-C., Chen, C., Liou, J., Pan, S., & Teng, C. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-3909 · Cited by 44
Emerging targets for glioblastoma stem cell therapy
Ahmad, R., Mohammad, R., Aaron, A., Karen, E., & Bijangi‐Vishehsaraei, K. (2016) · Journal of Biomedical Research · doi:10.7555/jbr.30.20150100 · Cited by 44
Emerging drugs and combinations to treat multiple myeloma
Larocca, A., Mina, R., Gay, F., Bringhen, S., & Boccadoro, M. (2017) · Oncotarget · doi:10.18632/oncotarget.19269 · Cited by 44
A novel class of anthraquinone-based HDAC6 inhibitors
Song, Y., Lim, J., & Seo, Y. H. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.12.056 · Cited by 44
Design and biological evaluation of tetrahydro-β-carboline derivatives as highly potent histone deacetylase 6 (HDAC6) inhibitors
Leonhardt, M., Sellmer, A., Krämer, O. H., Dove, S., Elz, S., Kraus, B., Beyer, M., & Mahboobi, S. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.04.046 · Cited by 44
Curriculum vitae of HDAC6 in solid tumors
Zheng, Y., Kang, H., Wang, B., Zhu, Y.-Z., Mamun, M., Zhao, L., Nie, H., Liu, Y., Zhao, L., Zhang, X., et al. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123219 · Cited by 43
The application of PROTAC in HDAC
Chen, S., Zheng, Y., Liang, B., Yin, Y., Yao, J., Wang, Q., Liu, Y., & Neamati, N. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115746 · Cited by 45
Maspin Reprograms the Gene Expression Profile of Prostate Carcinoma Cells for Differentiation
Bernardo, M. M., Meng, Y., Lockett, J., Dyson, G. E., Dombkowski, A. A., Kaplun, A., Li, X., Yin, S., Dzinic, S. H., Olive, M., et al. (2011) · Genes & Cancer · doi:10.1177/1947601912440170 · Cited by 43
Macro domains as metabolite sensors on chromatin
Marjanović, M. P., Timinszky, G., & Buschbeck, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1294-4 · Cited by 43
miR-155 downregulates ErbB2 and suppresses ErbB2-induced malignant transformation of breast epithelial cells
He, X.-H., Zhu, W., Yuan, P., Jiang, S., Li, D., Zhang, H.-W., & Liu, M.-F. (2016) · Oncogene · doi:10.1038/onc.2016.132 · Cited by 43
TOPK Promotes Microglia/Macrophage Polarization towards M2 Phenotype via Inhibition of HDAC1 and HDAC2 Activity after Transient Cerebral Ischemia
Han, Z., Zhao, H., Tao, Z., Wang, R., Fan, Z., Luo, Y., Luo, Y., & Ji, X. (2018) · Aging and Disease · doi:10.14336/ad.2017.0328 · Cited by 43
One-pot, multi-component synthesis and structure-activity relationships of peptoid-based histone deacetylase (HDAC) inhibitors targeting malaria parasites
Diedrich, D., Stenzel, K., Hesping, E., Antonova‐Koch, Y., Gebru, T., Duffy, S., Fisher, G. M., Schöler, A., Meister, S., Kurz, T., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.018 · Cited by 44
Epigenetics in Intestinal Epithelial Cell Renewal
Roostaee, A., Benoit, Y. D., Boudjadi, S., & Beaulieu, J. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25401 · Cited by 44
Deregulated expression of HDAC9 in B-cells promotes development of lymphoproliferative disease and lymphoma
Gil, V., Bhagat, G., Howell, L., Zhang, J., Kim, C., Stengel, S., Vega, F., Zelent, A., & Petrie, K. R. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.023366 · Cited by 42

Authors: Witt, O., Deubzer, H. E., Milde, T., & Oehme, I.
Affiliations: German Cancer Research Center (DE)
Corresponding author: Witt, Olaf
ORCID: Witt, Olaf
Deubzer, Hedwig E.
Milde, Till
Oehme, Ina
Venue: Cancer Letters
Publisher: Elsevier BV
Published: 2009-05
Volume: 277
Issue: 1
Pages: 8-21
ISSN: 0304-3835 (ISSN-L)
DOI: 10.1016/j.canlet.2008.08.016
OpenAlex: W2029148944
Cited by: 1,069
References: 131
Citations by year: 2026: 25 · 2025: 55 · 2024: 56 · 2023: 67 · 2022: 52 · 2021: 54 · 2020: 65 · 2019: 53 · 2018: 64 · 2017: 61 · 2016: 86 · 2015: 75 · 2014: 79 · 2013: 94 · 2012: 73
FWCI: 2.83
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cancer Letters (publishedVersion)
PubMed (publishedVersion)
MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
Funders: Bundesministerium für Bildung und Forschung
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, histone deacetylase inhibitors, sirtuins, class I HDACs, class II HDACs, cancer drug targets, selective inhibitors, oncogenicity
MeSH terms: Animals, Antineoplastic Agents, Enzyme Inhibitors, Histone Deacetylases, Humans, Neoplasms, Polymorphism, Genetic, Histone Deacetylase Inhibitors

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HDAC family: What are the cancer relevant targets?

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