p53-dependent and p53-independent anticancer effects of different histone deacetylase inhibitors

Sonnemann, Jürgen; Marx, Christian; Becker, Sabine; Wittig, Susan; Palani, Chithra D.; Krämer, Oliver H.; Beck, James F.

doi:10.1038/bjc.2013.742

Cited by 76 publications

(65 citation statements)

References 47 publications

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“…S5F). These findings are consistent with a recent report from Sonnemann et al (2014), showing that HDAC inhibition in HCT116 cells is partially dependent on p53.…”

Section: Direct Effects Of Hdac Inhibition On Cell Growth and Survivalsupporting

confidence: 94%

Histone deacetylase 1 and 2 regulate Wnt and p53 pathways in the ureteric bud epithelium

Chen

Xiao

et al. 2015

Development

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Histone deacetylases (HDACs) regulate a broad range of biological processes through removal of acetyl groups from histones as well as non-histone proteins. Our previous studies showed that Hdac1 and Hdac2 are bound to promoters of key renal developmental regulators and that HDAC activity is required for embryonic kidney gene expression. However, the existence of many HDAC isoforms in embryonic kidneys raises questions concerning the possible specificity or redundancy of their functions. We report here that targeted deletion of both the Hdac1 and Hdac2 genes from the ureteric bud (UB) cell lineage of mice causes bilateral renal hypodysplasia. One copy of either Hdac1 or Hdac2 is sufficient to sustain normal renal development. In addition to defective cell proliferation and survival, genome-wide transcriptional profiling revealed that the canonical Wnt signaling pathway is specifically impaired in UB Hdac1,2−/− kidneys. Our results also demonstrate that loss of Hdac1 and Hdac2 in the UB epithelium leads to marked hyperacetylation of the tumor suppressor protein p53 on lysine 370, 379 and 383; these post-translational modifications are known to boost p53 stability and transcriptional activity. Genetic deletion of p53 partially rescues the development of UB Hdac1,2−/− kidneys. Together, these data indicate that Hdac1 and Hdac2 are crucial for kidney development. They perform redundant, yet essential, cell lineage-autonomous functions via p53-dependent and -independent pathways.

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“…S5F). These findings are consistent with a recent report from Sonnemann et al (2014), showing that HDAC inhibition in HCT116 cells is partially dependent on p53.…”

Section: Direct Effects Of Hdac Inhibition On Cell Growth and Survivalsupporting

confidence: 94%

Histone deacetylase 1 and 2 regulate Wnt and p53 pathways in the ureteric bud epithelium

Chen

Xiao

et al. 2015

Development

View full text Add to dashboard Cite

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“…Likewise, we have recently observed that the SIRT1/2 inhibitor tenovin-1 effectively killed p53 +/+ , but not p53 −/− cancer cells (Sonnemann et al 2014), further substantiating that the effects of sirtuin modulators can depend on p53. To consider a potential impact of p53 on the response of ES cells to STACs, we used three ES cell lines differing in their p53 status, viz.…”

Section: Single-agent Activity Of Resveratrol and Srt1720 Against Ewisupporting

confidence: 58%

Reverse chemomodulatory effects of the SIRT1 activators resveratrol and SRT1720 in Ewing’s sarcoma cells: resveratrol suppresses and SRT1720 enhances etoposide- and vincristine-induced anticancer activity

Sonnemann

Kahl

Siranjeevi

et al. 2015

J Cancer Res Clin Oncol

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“…HDACi activated P53, and entinostatinduced cytotoxic effects partially depended on P53 in colon cancer cell lines (25). Valproic acid and TSA affect acetylation status of p53 and induce apoptosis in ERG-positive prostate cancer cells (26).…”

Section: Discussionmentioning

confidence: 99%

Histone deacetylase 3 promotes pancreatic cancer cell proliferation, invasion and increases drug-resistance through histone modification of P27, P53 and Bax

Jiao

Yuan

et al. 2014

International Journal of Oncology

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Abstract. Pancreatic cancer is one of the most aggressive solid malignancies with a dismal survival rate. Recent studies have shown that high expression levels of histone deacetylase 3 (HDAC3) correlate with malignant phenotype. However, the expression patterns and biological role of HDAC3 in pancreatic cancer remain unclear. In this study, our data showed that a higher level of HDAC3 protein expression was found in pancreatic cancer as compared to paired paracancerous tissues. Consistently, higher expression level of HDAC3 was found in all of the eight pancreatic cancer cell lines relative to human pancreatic ductal epithelial cells (HPDE). In addition, further function analysis revealed that HDAC3 can function as oncogenic protein, which could promote pancreatic cancer cell proliferation, migration and invasion, and may increase drug resistance. Moreover, the functional involvement of HDAC3 was partially correlated with post-induction repression of P53, P27 and Bax gene transcription, acting via H3K9 deacetylation. Taken together, our data suggest that HDAC3 participates in the pathogenesis and progression of pancreatic cancer through histone modification, which might be a pivotal epigenetic target against this devastating disease.

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p53-dependent and p53-independent anticancer effects of different histone deacetylase inhibitors

Cited by 76 publications

References 47 publications

Histone deacetylase 1 and 2 regulate Wnt and p53 pathways in the ureteric bud epithelium

Histone deacetylase 1 and 2 regulate Wnt and p53 pathways in the ureteric bud epithelium

Reverse chemomodulatory effects of the SIRT1 activators resveratrol and SRT1720 in Ewing’s sarcoma cells: resveratrol suppresses and SRT1720 enhances etoposide- and vincristine-induced anticancer activity

Histone deacetylase 3 promotes pancreatic cancer cell proliferation, invasion and increases drug-resistance through histone modification of P27, P53 and Bax

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