Clinical significance of histone deacetylases 1, 2, 3, and 7: HDAC2 is an independent predictor of survival in HCC

Quint, Karl; Agaimy, Abbas; Fazio, Pietro Di; Montalbano, Roberta; Steindorf, C.; Jung, Rudolf; Hellerbrand, Claus; Hartmann, Arndt; Sitter, H.; Neureiter, Daniel; Ocker, Matthias

doi:10.1007/s00428-011-1103-0

Cited by 105 publications

(70 citation statements)

References 33 publications

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“…Among class 1 HDAC family members, the expression of HDAC1 was reported to be altered in liver cancers and hdac1 also regulate zebrafish liver formation (Farooq et al, 2008;Wu et al, 2010;Yang et al, 2010;Quint et al, 2011;Lachenmayer et al, 2012). This suggests a critical role of HDAC 1 in liver formation and liver carcinogenesis.…”

Section: Discussionmentioning

confidence: 99%

“…Very little is known about the possible contribution of HDAC in liver cancer progression or metastases. However, HDAC expression has been reported to be altered in liver cancer tissues (Quint et al, 2011;Wu et al, 2010). The available data on the role of HDACs in cancer indicated that there is more than one mechanism by which HDACs function in cancer development.…”

Section: Discussionmentioning

confidence: 99%

“…HDAC1 is overexpressed in prostate, gastric, colon and breast carcinomas (Halkidou et al, 2004;Zhang et al, 2005;Wilson et al, 2006;Nakagawa et al, 2007). HDAC1 and HDAC3 are specifically implicated in hepato-carcinogenesis Yang et al, 2010;Quint et al, 2011;Lachenmayer et al, 2012) and hepto-organogenesis as well (Farooq et al, 2008;Noel et al, 2008). Keeping in view the vital role of HDAC1 in hepato-organogenesis and hepato-carcinogenesis, we have tried to fish out the HDAC1 specific interacting proteins in liver cancer chosing HepG2 cells as our liver cancer model.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

Farooq

Hozzein²,

Elsayed³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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Background: Hepatocellular carcinoma is one of the leading causes of mortalities worldwide. The search for new therapeutic targets is of utmost importance for improved treatment. Altered expression of HDAC1 in hepatocellular carcinoma (HCC) and its requirement for liver formation in zebrafish, suggest that it may regulate key events in liver carcinogenesis and organogenesis. However, molecular mechanisms of HDAC1 action in liver carcinogenesis are largely unknown. The present study was conducted to identify HDAC1 interacting proteins in HepG2 cells using modified SH-double-affinity purification coupled with liquid mass spectrophotemetery. Materials and Methods: HepG2 cells were transfected with a construct containing HDAC1 with a C-terminal strepIII-HA tag as bait. Bait proteins were confirmed to be expressed in HepG2 cells by western blotting and purified by double affinity columns and protein complexes for analysis on a Thermo LTQ Orbitrap XL using a C18 nano flow ESI liquid chromatography system. Results: There were 27 proteins which showed novel interactions with HDAC1 identified only in this study, while 14 were among the established interactors. Various subunits of T complex proteins (TCP1) and prefoldin proteins (PFDN) were identified as interacting partners that showed high affinity with HDAC1 in HepG2 cells. Conclusions: The double affinity purification method adopted in this study was very successful in terms of specificity and reproducibility. The novel HDAC1 complex identified in this study could be better therapeutic target for treatment of hepatocellular carcinoma.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

Farooq

Hozzein²,

Elsayed³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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“…This acetylation equilibrium is profoundly disturbed in HCC by an imbalance between functioning of HATs and HDACs driven mainly by an abnormally high HDAC activity. Specifically, the results of several studies have demonstrated an overexpression of histone deacetylases HDAC1, HDAC2, HDAC3, HDAC5, and HDAC7 in human HCC (148)(149)(150). Additionally, it has been reported that genetic polymorphisms in the HDAC1 and HDAC3 or in the promoter of the HDAC10 genes are associated with the development or reoccurrence of HCC (151,152).…”

Section: Inhibition Of Hdacs By Bioactive Food Constituents and Prevementioning

confidence: 99%

Nutritional Epigenetics and the Prevention of Hepatocellular Carcinoma with Bioactive Food Constituents

Moreno

Heidor

Pogribny

2016

Nutrition and Cancer

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Hepatocellular carcinoma (HCC) is an aggressive and life-threatening disease often diagnosed at intermediate or advanced stages, which substantially limits therapeutic approaches to its successful treatment. This indicates that the prevention of HCC may be the most promising strategy in reducing its incidence and mortality. Emerging evidence indicates that numerous nutrients and nonnutrient dietary bioactive components can reduce the occurrence and/or delay the development of HCC through modifications of deregulated epigenetic mechanisms. This review examines the existing knowledge on the epigenetic mechanism-based studies in in vitro and in vivo models of HCC on the chemopreventive potential of epigenetic food components, including dietary methyl-group donors, epigallocatechin-3-gallate, sodium butyrate, resveratrol, curcumin, and sulforaphane, on liver carcinogenesis. Future direction and potential challenges in the effective use of bioactive food constituents in the prevention of HCC are highlighted and discussed.

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“…Hepatic carcinoma, one of the most common malignant tumor in China, was found later (Quint et al, 2011;Chen et al, 2014;Page et al, 2014;Scaggiante et al, 2014). The incidence of HCC is increasing, particularly in China, due to the high prevalence of hepatitis virus infection, which confers a high risk of HCC (Ji et al, 2014;Li et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Effect of Trichostatin A on Anti HepG2 Liver Carcinoma Cells: Inhibition of HDAC Activity and Activation of Wnt/β-Catenin Signaling

Shi

Zuo²,

Feng³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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Purpose: To investigate the effect of deacetylase inhibitory trichostatin A (TSA) on anti HepG2 liver carcinoma cells and explore the underlying mechanisms. Materials and Methods: HepG2 cells exposed to different concentrations of TSA for 24, 48, or 72h were examined for cell growth inhibition using CCK8, changes in cell cycle distribution with flow cytometry, cell apoptosis with annexin V-FTIC/PI double staining, and cell morphology changes under an inverted microscope. Expression of β-catenin, HDAC1, HDAC3, H3K9, CyclinD1 and Bax proteins was tested by Western blotting. Gene expression for β-catenin, HDAC1and HDAC3 was tested by q-PCR. β-Catenin and H3K9 proteins were also tested by immunofluorescence. Activity of Renilla luciferase (pTCF/LEF-luc) was assessed using the Luciferase Reporter Assay system reagent. The activity of total HDACs was detected with a HDACs colorimetric kit. Results: Exposure to TSA caused significant dose-and time-dependent inhibition of HepG2 cell proliferation (p<0.05) and resulted in increased cell percentages in G0/ G1 and G2/M phases and decrease in the S phase. The apoptotic index in the control group was 6.22±0.25%, which increased to 7.17±0.20% and 18.1±0.42% in the treatment group. Exposure to 250 and 500nmol/L TSA also caused cell morphology changes with numerous floating cells. Expression of β-catenin, H3K9and Bax proteins was significantly increased, expression levels of CyclinD1, HDAC1, HDAC3 were decreased. Expression of β-catenin at the genetic level was significantly increased, with no significant difference in HDAC1and HDAC3 genes. In the cytoplasm, expression of β-catenin fluorescence protein was not obvious changed and in the nucleus, small amounts of green fluorescence were observed. H3K9 fluorescence protein were increased. Expression levels of the transcription factor TCF werealso increased in HepG2 cells following induction by TSA, whikle the activity of total HDACs was decreased. Conclusions: TSA inhibits HDAC activity, promotes histone acetylation, and activates Wnt/β-catenin signaling to inhibit proliferation of HepG2 cell, arrest cell cycling and induce apoptosis.

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Clinical significance of histone deacetylases 1, 2, 3, and 7: HDAC2 is an independent predictor of survival in HCC

Cited by 105 publications

References 33 publications

Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

Nutritional Epigenetics and the Prevention of Hepatocellular Carcinoma with Bioactive Food Constituents

Effect of Trichostatin A on Anti HepG2 Liver Carcinoma Cells: Inhibition of HDAC Activity and Activation of Wnt/β-Catenin Signaling

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