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Cell migration was determined in wound healing assays by means of Ibidi Culture-Insert Ibidi, Martinsried, Germany. While c5 and c6 significantly reduced the viability of all UCCs, their effect varied among the cell lines.
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- In the other UCCs no significant changes were observed Figure 9 A.
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Medizin von A-Z Patienten-Lexikon Expertensprechstunden. In human breast cancer cell lines overexpression of HDAC1, HDAC6 or HDAC8 contributes to increased invasion and metalloproteinase-9 MMP-9 expression [[ 37 ]]. A recently published analysis of HDAC expression patterns in urothelial carcinoma cell lines and tissues showed a deregulation of several HDACs in urothelial cancer. These findings include up-regulation of HDAC2 and HDAC8 and down-regulation of HDAC4, HDAC5, and HDAC7 [[ 39 ]].
Cell lines used were provided by Dr. Knowles Leeds, UK , Dr. Fogh New York, USA , Dr. Barton Grossmann Houston, USA and by the DSMZ Braunschweig, Germany.
Normal urothelial control NUC cells were isolated from ureters after nephrectomy and were cultured in keratinocyte serum-free medium Invitrogen, Life Technologies, Darmstadt, Germany supplemented with 0. C5 and c6 are investigational compounds described in [[ 41 ]] and are available on request. Inhibitors were dissolved in DMSO as a stock of 10 mM.
Control cells were treated with DMSO only. UCCs were seeded in 6-well plates and grown for 24 h before transfection. After transfection cells were incubated for 72 h before use for further experiments.
UCCs were seeded into well plates and grown for 24 h before inhibitor treatment with the indicated drug concentration or DMSO and further grown for 72 h. In another experiment, cells were plated in 6-well plates and grown for 24 h before siRNA-mediated knockdown of HDAC8. The colony forming assay was carried out 72 h after siRNA mediated HDAC8 knockdown and HDAC8 inhibitor treatment.
Then, cells were plated in 6-well plates at a density of to 1, cells per well. The colonies were stained with Giemsa Merck, Darmstadt, Germany. UCCs were transfected with HDAC8 siRNA or an irrelevant control siRNA or, in another experiment, cultured with the determined IC 50 concentrations of the HDAC8 selective inhibitors c2, c5 and c6, the pan HDAC-inhibitor SAHA 2. Cell migration was determined in wound healing assays by means of Ibidi Culture-Insert Ibidi, Martinsried, Germany.
The cell suspension was placed in both compartments allowing growth in the designated area only. The cells were treated with IC 50 concentrations of c2, c5, c6 or 2. The extent of wound closure was examined by phase contrast microscopy with the LuciaG software Laboratory Imaging s. Western blot analysis of whole-cell extracts were done as described previously [[ 39 ]]. Protein concentrations were determined by BCA protein assay Thermo Scientific, Rockford, IL. Primary antibodies were used against HDAC1 ,, C, sc; Santa Cruz Biotechnology, Heidelberg, Germany , HDAC2 ,, H, sc; Santa Cruz Biotechnology, Heidelberg, Germany , HDAC3 ,, H, sc; Santa Cruz Biotechnology, Heidelberg, Germany , HDAC8 , A; Epigentek, Brooklyn, NY , p21 , C, sc; Santa Cruz Biotechnology, Heidelberg, Germany , thymidylate synthase ,, TS, TS, Millipore, Temecula, CA , PARP poly [ADP-ribose] polymerase 1, , 46D11; Cell Signaling Technology, Inc.
Louis, Mo. Louis, MO was used as loading control in a concentration of , Secondary antibodies were HRP-conjugated goat-anti-mouse antibody sc; Santa Cruz Biotechnology, Heidelberg, Germany , HRP-conjugated goat-anti-rabbit antibody sc, Santa Cruz Biotechnology, Heidelberg, Germany and HRP-conjugated rabbit-anti-goat antibody P; DakoCytomation, Stockholm, Sweden at a concentration of , to , Bands were visualized by the ECL select chemo luminescence kit GE Healthcare, Piscataway, NJ and the WesternBright Quantum kit Biozym, Hessisch Oldendorf, Germany.
Histones were extracted following a published protocol through sulphuric acid extraction and TCA-precipitation [[ 43 ]]. The detection of acetylated and non-acetylated histones was performed with primary antibodies against acetylated histone H3 ,, , Active Motif, La Hulpe, Belgium , total histone H3 ,, , Cell Signaling Technology, Inc.
Statistical analyses were performed using SPSS 18 SPSS, Chicago, USA. IC 50 values and dose-response curves were approximated by non-linear regression analysis using Origin 8.
Urothelial bladder cancer is a heterogeneous disease with diverse clinical, pathological, genetic and epigenetic presentations. As recently published [[ 39 ]], overexpression of HDAC8 was observed in cancer tissues. In urothelial cancer cell lines, a variable expression of HDAC8 was observed both at mRNA and protein level. To cover this range, we chose a panel of cell lines representing the heterogeneity of the tumor.
In contrast, UCC RT cells showed a decreased level of HDAC8 mRNA Figure 1 A. The HDAC8 mRNA expression in UCCs was comparable to the measured HDAC8 expression in other tumor entities such as neuroblastoma and mammary carcinoma data not shown.
The HDAC8 protein levels are shown in Figure 1 B. The UCC SW indicated a strong increase of HDAC8 protein compared to NUCs. The cell lines VM-CUB1 and UM-UC-3 showed a moderate increase of HDAC8. In the cell line V, a reduction of HDAC8 protein expression was observed.
HDAC8 expression in urothelial cancer cell lines. A Relative mRNA expression of HDAC8 in eight urothelial cancer cell lines UCCs compared to two normal uroepithelial cultures NUC; mean value set as 1 measured by quantitative RT-PCR.
The HDAC8 expression values were adjusted to TBP as a reference gene and are displayed on the y-axis. The dotted line shows the average expression level of the NUC samples. B Protein expression of HDAC8 in urothelial cancer cell lines UCCs and a normal uroepithelial control NUC analyzed by western blotting. Accordingly the urothelial carcinoma cell lines SW protein level strongly increased , UM-UC-3, VM-CUB1 protein level moderately increased , RT protein level as normal and V protein level decreased were selected for further experiments.
The endogenous HDAC8 expression was reduced by transiently transfecting HDAC8 siRNA and irrelevant siRNA into RT, VM-CUB1, SW, V and UM-UC-3 cells.
The knockdown efficacy 72 h after transfection was shown by RT-PCR Figure 2 A and western blot analysis Figure 2 B. Efficiency of HDAC8 knockdown by a specific siRNA in the urothelial cancer cell lines. A Relative HDAC8 expression after siRNA mediated knockdown in urothelial carcinoma cell lines compared to irrelevant control as examined by quantitative RT-PCR analysis 72 h.
The HDAC8 expression values were normalized to TBP as a reference gene and are displayed on the y-axis. B Western blot analysis confirmed the effects of HDAC8-siRNA mediated knockdown at the HDAC8 protein level in comparison to normal and irrelevant siRNA controls 72 h. To investigate the impact of HDAC8 on cell proliferation of UCCs we performed viability assays after 72 h of transfection.
Colony forming assays were performed to evaluate the role of HDAC8 for anchorage-dependent clonal growth capability. The siRNA mediated HDAC8 knockdown inhibited clonogenic growth of UCCs Figure 3 B. The relative size of the HDAC8 siRNA transfected colonies is reduced in V in comparison to irrelevant siRNA. In VM-CUB1, SW, RT and UM-UC-3 cells the colony size remains constant between irrelevant control and HDAC8 siRNA transfection data not shown.
Proliferation and clonogenicity in urothelial cancer cells after siRNA mediated knockdown of HDAC8. A Relative cell viability in several urothelial carcinoma cell lines after siRNA mediated knockdown of HDAC8 compared to irrelevant control 72 h.
B Giemsa-staining of colonies from irrelevant siRNA and HDAC8 siRNA transfected RT, VM-CUB1, SW, V and UM-UC-3 cells compared to an untreated control 72 h.
To characterize the effect of the HDAC8 knockdown on UCCs, we investigated downstream targets of HDAC8 known from other cancers: the proliferation marker thymidylate synthase TS , cleavage of PARP and expression of p The expression of TS 72 h after HDAC8 knockdown was only slightly reduced in SW, V and UM-UC-3 cells.
In RT and VM-CUB1 cells no effects were observed. Effects on cleavage of PARP could only be detected in UM-UC-3 cells after HDAC8 knockdown. There a decrease can be observed. The expression level of p21 indicates a decreased expression in comparison to irrelevant control in the cell lines RT, VM-CUB1, V and UM-UC-3 after HDAC8 knockdown. In the cell line SW no altered p21 expression could be observed. Effects of siRNA mediated HDAC8 knockdown on target proteins.
Based on the observation that the HDAC8 knockdown inhibited proliferation of urothelial carcinoma cells we investigated the sensitivity of several UCCs to three different HDAC8 inhibitors [[ 41 ]]. The treatment with the HDAC8 selective small molecule inhibitors c2, c5 and c6 inhibited the cell proliferation of all UCCs in a concentration dependent manner, with stronger effects of the higher affinity compounds c5 and c6 Table 1. Dose-dependent effects of three different HDAC8 specific inhibitors on viability of urothelial cancer cell lines.
A Several urothelial cancer cell lines were treated with different concentrations of HDAC8 inhibitors. B Sensitivity of urothelial cancer cell lines and one representative normal uroepithelial control to compound 5 and compound 6 after 72 h of treatment. The cell lines outlined by bold letters were used for the functional experiments.
While c5 and c6 significantly reduced the viability of all UCCs, their effect varied among the cell lines. It is noticeable that cells with an epithelial phenotype e. The influence of the inhibitors on clonogenic growth after a 72 h treatment at the determined IC 50 concentrations is illustrated in Figure 6. Compound 2 inhibited clonogenicity only in VM-CUB1 cells. Treatment with compound 5 resulted in a moderate reduction of colony numbers in RT, UM-UC-3 and V cells, whereas in VM-CUB1 cells, clonogenic growth was completely abolished.
In contrast, c5 had no effect on SW cells. Effect of HDAC8 specific inhibitor treatment on clonogenic growth of urothelial cancer cells. Giemsa-staining of grown colonies from inhibitor treated RT, VM-CUB1, SW, V and UM-UC-3 cells is compared to DMSO solvent control compound 2, compound 5, compound 6; IC 50 , 72 h. As the effect of pharmacological HDAC8 inhibition was stronger than the effect of HDAC8 knock-down, wound healing assays of UCCs after HDAC8 inhibitor treatment were additionally performed Figure 7 A.
A clear difference was observed in VM-CUB1 and UM-UC-3 cells, respectively, comparing DMSO controls to cells treated with c5 and c6, especially after 6 - 12 h Figure 7 B.
Migration assay of urothelial cancer cells after HDAC8 inhibitor treatment. A Representative photographs of wound healing assay at 0 and 12 hours from inhibitor treated RT, VM-CUB1, SW, V and UM-UC-3 cells compound 2, compound 5, compound 6; IC50, 72 h in comparison to a DMSO solvent control co. B Relative scratch size after 3, 6, 9 and 12 h of migration in comparison to the starting point 0 h. The relative scratch size is displayed on the y-axis.
The calculated significances refer to the DMSO solvent control. The impact of the HDAC8 inhibitor treatment was further analyzed by western blot analysis of different target proteins Figure 8. The expression of thymidylate synthase TS in VM-CUB1, SW and UM-UC-3 cells was weakly reduced after 72 h of c5 and c6 treatment.
No effects were observed in V and RT cells. Increased cleavage of PARP after c6 treatment could be only detected in the UCC SW Effects on p21 were divergent.
In RT and VM-CUB1 cells an increase of p21 protein level could be observed. Expression decreased in the cell lines SW, V and UM-UC-3 after c6 treatment and in the two former cell lines also after c5 treatment Figure 8. Effects of specific HDAC8 inhibition on target proteins. To further characterize the impact of HDAC8 on cell cycle distribution UCCs were analyzed by flow cytometry after either knockdown or inhibitor treatment Figure 9.
Knockdown of HDAC8 resulted in a significant shift in cell cycle distribution only in SW cells, showing an S-phase-decrease. In the other UCCs no significant changes were observed Figure 9 A. In contrast, pharmacological inhibition of HDAC8 by c5 and c6 resulted in a significant increase of the sub-G1 fraction in the UCCs VM-CUB1 and SW and a significant decrease of the G1-fraction in VM-CUB1, SW, V and UM-UC-3 cells Figure 9 B.
Effects of HDAC8 knockdown and HDAC8 inhibitor treatment on cell cycle distribution. Changes in cell cycle distribution and amount of apoptotic cells as sub-G1 fraction after A siRNA mediated HDAC8 knockdown 72 h and B HDAC8 inhibitor treatment compound 2, compound 5, compound 6; IC 50 , 72 h were measured by cell cycle analysis using flow cytometry.
DMSO served as a solvent control. The relative distribution of the fractions is displayed on the y-axis. Following HDAC8 knockdown or pharmacological inhibition, no effects on the acetylation status of histone H3 were observed Figure In contrast, acetylation of H4 increased after inhibitor treatment in RT Figure 10 B.
In addition, a slight increase of H4 acetylation was observed after c5 and c6 treatment in the cell line V Figure 10 B. No effects on the acetylation status of H4 were seen following HDAC8 knockdown Figure 10 A. Western blot analysis of histone H3 and H4 acetylation in urothelial cancer cell lines after HDAC8 knockdown and HDAC8 inhibitor treatment. Amounts of acetylated and total histone H3 and H4 were analyzed by western blotting.
The modifications are determined in the urothelial cancer cell lines RT, VM-CUB1, SW, V and UM-UC-3 after A siRNA mediated HDAC 8 knockdown 72 h in comparison to untreated and irrelevant control and B pharmacological HDAC8 treatment compound 2, compound 5, compound 6; IC 50 , 72 h.
To investigate whether inhibition of HDAC8 might be counteracted by concomitant upregulation of other class I-HDACs HDAC1, HDAC2 and HDAC3 their expression levels were compared by real-time PCR and western blot analysis Figures 11 and In brief, HDAC1, HDAC2 and HDAC3 mRNA levels exhibited variable changes after siRNA-mediated knockdown of HDAC8.
Both significant up-and downregulation of specific HDACs were observed. In particular, either HDAC1 or HDAC2 seems to become upregulated after HDAC8 knockdown Figure 11 A.
Western blot analysis shown in Figure 11 B revealed a decrease of HDAC2 protein in RT cells and HDAC3 protein in UM-UC-3 cells after siRNA mediated HDAC8 knockdown. No significant deregulation of other class I-HDACs took place Figure 11 B. Compensation mechanism after HDAC8 knockdown in RT, VM-CUB1, SW, V and UM-UC-3 cells. Effects of siRNA mediated HDAC8 knockdown on A mRNA and B protein expression levels of the class I histone deacetylase HDAC8, HDAC1, HDAC2 and HDAC3 72 h in comparison to untreated and irrelevant control.
The mRNA expression values were measured by quantitative RT-PCR analysis and were normalized to TBP as a reference gene. Compensation mechanism after specific HDAC8 inhibition in RT, VM-CUB1, SW, V and UM-UC-3 cells. Effects of HDAC8 inhibitor treatment on A mRNA and B protein expression of the class I histone deacetylases HDAC8, HDAC1, HDAC2 and HDAC3, compared to DMSO solvent control compound 2, compound 5, compound 6; IC 50 , 72 h. The calculated significances of the treated value refer to the DMSO solvent control.
Measurements of mRNA expression after pharmacological inhibition of HDAC8 showed significant, but overall slight decreases or increases of the expression of several HDACs in the UCC Figure 12 A. In this study we present the first systematic analysis of HDAC8 expression and function in urothelial cancer using a set of bladder cancer cell lines representative for the heterogeneity of this tumor.
The aim of our study was to evaluate the potential of HDAC8 as a therapeutic target. Overexpression of HDAC8 has been reported in a considerable number of different cancer entities [[ 26 ],[ 34 ],[ 36 ],[ 37 ]]. In neuroblastoma, in particular, HDAC8 expression was significantly correlated with further poor prognostic markers as well as poor overall and progression-free survival.
SiRNA-mediated knockdown and pharmacological inhibition of HDAC8 in neuroblastoma significantly decreased proliferation rate and reduced clonogenic growth, cell cycle arrest, and differentiation [[ 34 ]].
In hepatocellular carcinoma HDAC8 knockdown also suppresses cell proliferation and enhances apoptosis via elevated expression of p53 and acetylation of p53 at Lys [[ 36 ]]. As there were indications from our own and other data that HDAC8 is often upregulated in urothelial carcinoma as well [[ 39 ],[ 44 ]], the question arose whether HDAC8 might be a potential target for anticancer treatment in this tumor.
In urothelial cancer cell lines, a variable expression of HDAC8 was observed both at mRNA and protein level [[ 39 ]]. Importantly, mRNA expression levels were comparable to neuroblastoma and breast cancer cells data not shown. An according variability has also been reported from investigations in further malignomas, e.
Differences between mRNA and protein expression indicate that HDAC8 expression and activity in UCCs may be regulated both transcriptionally and on the protein level, e. In addition, in our UCC panel, a low HDAC8 expression was predominantly observed in UCCs with an epithelial phenotype. Therefore, to cover this range both on protein and mRNA level, we chose to apply a panel of 6 cell lines representing the heterogeneity of the HDAC8 expression instead of focusing on one urothelial cancer cell line.
In these cells, the HDAC8 inhibitor c2 yielded an similar phenotype at a concentration similar to the in vitro IC 50 of c2 against HDAC8 [[ 41 ]]. None of the UCCs was inhibited substantially at this concentration by pharmacological treatment with c2. The inhibitors c5 and c6 significantly reduced the viability of all UCCs, with half inhibitory concentrations between 9 and These differences follow the order of the affinity of the inhibitors for HDAC8 in vitro [[ 41 ]].
Though in vitro affinity of c5 and c6 is 20 - 50 fold higher compared to c2, in vivo effects on UCC were not as strong as expected.
Specifically, SW cells mesenchymal, elevated HDAC8 expression were least sensitive to the inhibitors c5 and c6 while RT cells epithelial, lowest HDAC8 expression responded to treatment with c5 and c6 already at low concentrations. As recently shown in endometrial stroma sarcoma cells, HDAC inhibition may be counteracted by increased activity of the PI3K pathway in PTEN-deficient cells [[ 45 ]].
In our cell line panel, UM-UC-3 are PTEN-deficient, resulting in increased PI3K activity. However, this cell line was not exceptionally resistant either in our previous study using pan-HDAC inhibition [[ 39 ]] or in the present study with HDAC8-specific inhibitors. Accordingly, at least in urothelial cancer, PTEN deficiency does not seem to have a decisive impact on the efficacy of HDAC inhibitors.
Effects of siRNA mediated downregulation and pharmacological inhibition on urothelial cancer cell lines were not thoroughly consistent. Differences might be explained by several factors. For example, knockdown depletes the protein thereby not only affecting enzymatic but also other protein functions for example complex assembly.
Inhibitor treatment ideally only suppresses the enzymatic activity while further protein functions should not be affected. Accordingly, also compensatory mechanisms might be different in both conditions. Comparing expression levels of further class I HDACs after knockdown of HDAC8 as well as after pharmacological inhibition, only minor changes were observed.
Neither HDAC8 knockdown nor pharmacological treatment with any compound except the SAHA control led to a change in histone H3 or H4 acetylation, a widely used surrogate marker for intracellular HDAC inhibition. This finding suggests that HDAC8, as expected, does not substantially affect overall histone acetylation.
In addition, this does also indicate that inhibitor treatment seems to be iso-enzyme specific as other class I HDACs seemed to be not affected.
This was also observed in neuroblastoma cell lines after treatment of HDAC8. Global Histone H4 acetylation was not affected by HDAC8 knockdown or by selective inhibitor treatment [[ 34 ]]. The latter finding is in accord with previous findings in HeLa and HEK cells [[ 45 ]].
In vitro , c5 and c6 do not inhibit HDAC6 efficiently. Similar discrepancies between in vitro and in vivo activity of an isoenzyme-selective HDAC inhibitor on tubulin acetylation have been observed by others for valproic acid [[ 47 ]]. However, inhibition of HDAC6 as such does not inhibit migration of UCC as efficiently as the HDAC8 inhibitors c5 and c6 [[ 48 ]].
The effects of siRNA mediated knockdown of HDAC8 on cell cycle and apoptosis were limited and few significant effects were seen, such as a decreased S-phase fraction in VM-CUB1 and small changes in thymidylate synthase and p21 expression. In contrast, no effect on the cell cycle was observed in the hepatocellular carcinoma cell lines BEL and Hep-G2 [[ 36 ]].
This observation fits with our own marginal effects after siRNA-mediated HDAC8 knockdown. The level of apoptosis induction in BEL and Hep-G2 cells after siRNA-mediated targeting of HDAC8 were comparable to the increase of the subG1-fraction in individual urothelial carcinoma cell lines after targeting of HDAC8 [[ 36 ]]. Concerning the use of inhibitors, effects of pharmacological inhibition on cell cycle distribution by c2 were, as expected, only minor.
Consequently, p21 increased in two cell lines and thymidylate synthase decreased in all but one. HDAC8 is deregulated in UCCs resulting in variable mRNA and protein expression levels. Suppression and pharmacological inhibition of HDAC8 had significant, but overall minor impacts on cell proliferation, clonogenic growth and migration. These effects were comparable to findings in other cancer entities.
However, those effects were observed only at drug concentrations probably not appropriate for the use in patients. Neither HDAC8 mRNA nor protein expression levels were reliable predictive marker for sensitivity to HDAC8 inhibition. In summary, HDAC8 on its own does not seem to constitute a promising drug target in bladder cancer. Whether selective HDAC8 inhibition may synergize with either conventional chemotherapeutics or further targeted antitumoral compounds remains to be further explored.
Interestingly, in this respect, the compounds c5 and c6 which are efficient inhibitors of HDAC8 may have additional cellular targets which need to be further elucidated. Ferlay J, Shin HR, Bray F, Forman D, Mathers C, Parkin DM: Estimates of worldwide burden of cancer in GLOBOCAN Int J Cancer. CAS Article PubMed Google Scholar. Witjes JA, Comperat E, Cowan NC, De Santis M, Gakis G, Lebret T, Ribal MJ, Van der Heijden AG, Sherif A: EAU Guidelines on Muscle-invasive and Metastatic Bladder Cancer: Summary of the Guidelines.
Histone deacetylase 8 is deregulated in urothelial cancer but not a …
2014/7/10 · Background Previous studies have shown that class-I histone deacetylase (HDAC) 8 mRNA is upregulated in urothelial cancer tissues and urothelial cancer cell lines compared to benign controls. Using urothelial cancer cell lines we evaluated whether specific targeting of HDAC8 might be a therapeutic option in bladder cancer treatment. Methods We conducted siRNA-mediated knockdown …
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