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Academic literature on the topic 'HDAC11 assay'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "HDAC11 assay"

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Bui, Hue Thi Buu, Phuong Hong Nguyen, Quan Minh Pham, Hoa Phuong Tran, De Quang Tran, Hosun Jung, Quang Vinh Hong, et al. "Target Design of Novel Histone Deacetylase 6 Selective Inhibitors with 2-Mercaptoquinazolinone as the Cap Moiety." Molecules 27, no. 7 (March 28, 2022): 2204. http://dx.doi.org/10.3390/molecules27072204.

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Epigenetic alterations found in all human cancers are promising targets for anticancer therapy. In this sense, histone deacetylase inhibitors (HDACIs) are interesting anticancer agents that play an important role in the epigenetic regulation of cancer cells. Here, we report 15 novel hydroxamic acid-based histone deacetylase inhibitors with quinazolinone core structures. Five compounds exhibited antiproliferative activity with IC50 values of 3.4–37.8 µM. Compound 8 with a 2-mercaptoquinazolinone cap moiety displayed the highest antiproliferative efficacy against MCF-7 cells. For the HDAC6 target selectivity study, compound 8 displayed an IC50 value of 2.3 µM, which is 29.3 times higher than those of HDAC3, HDAC4, HDAC8, and HDAC11. Western blot assay proved that compound 8 strongly inhibited tubulin acetylation, a substrate of HDAC6. Compound 8 also displayed stronger inhibition activity against HDAC11 than the control drug Belinostat. The inhibitory mechanism of action of compound 8 on HDAC enzymes was then explored using molecular docking study. The data revealed a high binding affinity (−7.92 kcal/mol) of compound 8 toward HDAC6. In addition, dock pose analysis also proved that compound 8 might serve as a potent inhibitor of HDAC11.
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Baumann, Philipp, Carmen Junghanns, Strobl Stefan, Fuat Oduncu, and Ralf Schmidmaier. "The Novel Pan-HDAC Inhibitor CR2408 Inhibits Multiple Myeloma Cell Growth and Proliferation." Blood 118, no. 21 (November 18, 2011): 5133. http://dx.doi.org/10.1182/blood.v118.21.5133.5133.

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Abstract Abstract 5133 Background: Myeloma (MM) is still an incurable disease, and new cytotoxic drugs are urgently needed. CR2408 is a novel pan-histon deacetylases inhibitor with promising properties and effects in MM cells. Methods: The effect of CR2408 in MM cells was characterized by multiple assays. HDAC inhibition was shown by western blotting as well as HDAC enzyme inhibition assays. Cell growth and viability was shown by the common WST-1 assay. Induction of apoptosis was detected using flow cytometry after annexin-V-FITC staining as well as caspase cleavage detected by western blotting. Basal and cytokine stimulated cell growth rates of myeloma cells were measured by the WST-1 assay. Myeloma cell proliferation was determined by the BrdU assay. Alterations of the cell cycle were determined by flow cytometry after staining with propidium iodide. Modulation of intracellular signalling was shown by western blotting. Results: We have found CR2408 to induce profound hyperacetylation of histone H4 in MM cells. Our experiments revealed that nanomolar concentrations of CR2408 abrogate HDAC activity in 11 HDAC enzymes. Comparison with SAHA shows lower IC50 values for CR2408 (HDAC1 27nM, HDAC2 76nM, HDAC3 28nM, HDAC4 151nM, HDAC5 51nM, HDAC6 13nM, HDAC7 360nM, HDAC8 522nM, HDAC9 92nM, HDAC10 77nM and HDAC11 56nM). CR2408 abrogated myeloma cell growth at nanomolar concentrations (250nM: NCI-H929: −93%; OPM-2: −85%; U266: −87%; RPMI-8226: −86%) and induced apoptosis in multiple myeloma cell lines and primary cells, as shown by the annexin V assay (500nM: NCI-H929: 75%, OPM-2: 65%, RPMI-8226: 80%, U266: 18%, primary cells: 50%). Induction of apoptosis was confirmed by showing cleavage of caspase 3, 8 and 9. Furthermore, increased cell growth induced by conditioned medium obtained from bone marrow stromal cells was abrogated by CR2408. The BrdU assay revealed that inhibition of cell growth was due to inhibition of myeloma cell proliferation (500nM: OPM-2: −50%; RPMI-8226: −58%, U266: −55%). Furthermore, we analysed cell cycle distribution and found that in contrast to other HDAC inhibitors, CD2408 does not provoke a G0/G1 cell cycle arrest but leads to immediate DNA and cell fragmentation, resulting in an accumulation of cell fragments in the subG1 phase. Inhibition of cell proliferation was accompanied by a strong downregulation of the proteins cdc25A, cdk4 and hypophosphorylation of RB. Incubation of myeloma cells with CR2408 did not alter the phosphorylation of 4E-BP-1, P70S6k, but the mitochondrial proteins Bad and Bcl-Xl were downregulated and Bim and pJNK were upregulated. Finally, CR2408 shows significant synergistic effects when combined with doxorubicin and bortezomib. Conclusions: The HDAC inhibitor CR2408 inhibits MM cell proliferation and induces apoptosis. This is accompanied by a strong perturbation of mitochondrial proteins. Since CR2408 inhibit myeloma growth and proliferation as low nanomolar levels, this study provides the rationale for the further in vivo evaluation of CR2408 in order to find a more efficient and less toxic member of this group of compounds. Disclosures: Stefan: 4SC AG: Employment.
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Kim, Jee In, Kyong-Jin Jung, Hee-Seong Jang, and Kwon Moo Park. "Gender-specific role of HDAC11 in kidney ischemia- and reperfusion-induced PAI-1 expression and injury." American Journal of Physiology-Renal Physiology 305, no. 1 (July 1, 2013): F61—F70. http://dx.doi.org/10.1152/ajprenal.00015.2013.

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Male gender and the male hormone testosterone increase susceptibility to kidney ischemia and reperfusion (I/R) injury, which is associated with inflammatory responses. Possible involvement of histone deacetylase (HDAC) in inflammatory responses has been suggested. We investigated the gender-specific role of HDACs in plasminogen activator inhibitor type-1 (PAI-1) expression and I/R injury. PAI-1 inhibition protected the kidney from I/R-induced inflammation and functional loss. Among HDACs, only HDAC11 negatively regulated PAI-1 expression in I/R-subjected kidney gender specifically and lipopolysaccharide (LPS)-stimulated mouse monocytes/macrophages. HDAC11 gene silencing increased PAI-1 expression. Chromatin immunoprecipitation assay confirmed binding of HDAC11 to the promoter region of PAI-1 and then release by I/R insult or LPS treatment. I/R-induced HDAC11 release was inhibited by orchiectomy and reversed by dihydrotestosterone treatment. Release of HDAC11 increased acetylation of histone H3. In conclusion, male gender and male hormones accelerate I/R-induced decreases in expression and binding of HDAC11, resulting in an increase in PAI-1 expression. These data provide important insight into gender dimorphism offering HDAC11 as a novel target for I/R injury.
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Chen, Jie, Fengdong Cheng, David Michael Woods, Edward Seto, Alejandro Villagra, and Eduardo M. Sotomayor. "Histone Deacetylase 11 (HDAC11) Interaction with Ikaros Represent a Novel Mechanism of Regulation of Essential Transcriptional Factors in CD4+ T Cells." Blood 128, no. 22 (December 2, 2016): 864. http://dx.doi.org/10.1182/blood.v128.22.864.864.

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Abstract Histone deacetylase 11 (HDAC11), the most recently identified histone deacetylase, is the sole member of class IV HDACs [1]. Since its discovery, no biological function was assigned to this HDAC until we demonstrated its central role in negatively regulating IL-10 production in antigen presenting cells (APCs) [2]. More recently, we have found that disruption of HDAC11 in T cells is associated with an enhanced pro-inflammatory cytokine profile and effector molecule production. Furthermore, T-cells lacking HDAC11 were less susceptible to regulatory T-cell (Treg) suppression in vitro, were refractory to tolerance induction in vivo and displayed enhanced allo-reactivity and anti-tumor responses in murine models. Of note, T-cells lacking HDAC11 expressed higher levels of the transcription factors Eomes and Tbet. Conversely, overexpression of HDAC11 in T-cells decreased the expression of both transcription factors. The molecular mechanism(s) by which HDAC11 regulates the expression of these transcription factors have remained unknown. By using chromatin immunoprecipitation (ChIP) assay we found that in resting T-cells HDAC11 is present at the Eomes and Tbet gene promoters where it maintains histone deacetylation, a compacted chromatin and gene repression. Following T-cell stimulation, HDAC11 was largely absent from both promoters, which resulted in increased histone 3 (H3) acetylation and gene transcriptional activity. These findings were confirmed in T-cells isolated from HDAC11 knock out (KO) mice which also displayed an increase in H3 acetylation at the Tbet and Eomes gene promoter regions. Conversely, H3 acetylation was decreased in both gene promoters in T-cells overexpressing HDAC11 as compared to empty-vector transfected cells. Given that HDACs do not bind to DNA, we asked next which transcription factor(s) HDAC11 might be associated with, in order to regulate Tbet and Eomes gene transcriptional activity. In prior studies we have found that HDAC11 form a molecular complex with another member of the HDAC family, HDAC6, which physically interacts with the transcription factor, STAT3 in both the cytoplasmic and nuclear compartments. However, in T-cells no direct interaction of HDAC11 with STAT3 was detected in either compartment. In contrast, we found for the first time that HDAC11 physically associates with Ikaros (Ikzf1), a member of the Ikaros zinc finger transcription factor family that has been previously implicated in the regulation of T-bet gene expression and IFN-g production in T-cells [3-5]. The protein complex HDAC11-Ikaros was mainly detected in the nuclear compartment and both proteins were present at the T-bet gene promoter. Collectively, these results point to the HDAC11-Ikaros complex as a novel epigenetic mechanism of regulation of Tbet and Eomes, transcription factors that are essential for T cell development and function. Disclosures Woods: BMS: Other: Stock; HDAC11: Patents & Royalties: Patent for targeting HDAC11; Lion Biotech: Other: Stock.
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HORIUCHI, MARIKA, AKIO MORINOBU, TAKAAKI CHIN, YOSHITADA SAKAI, MASAHIRO KUROSAKA, and SHUNICHI KUMAGAI. "Expression and Function of Histone Deacetylases in Rheumatoid Arthritis Synovial Fibroblasts." Journal of Rheumatology 36, no. 8 (June 16, 2009): 1580–89. http://dx.doi.org/10.3899/jrheum.081115.

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Objective.To explore the effects of histone deacetylases (HDAC) on rheumatoid arthritis synovial fibroblasts (RA-SF).Methods.The expression of mRNA encoding HDAC1 through HDAC11 in RA-SF and osteoarthritis-SF (OA-SF) was determined using real-time polymerase chain reactions. The functions of HDAC1 and HDAC2 in RA-SF were assessed using small interfering RNA (siRNA) technology. Cell counts and proliferation were examined by MTT assays and BrDU ELISA, respectively, and apoptosis was determined using the TUNEL assay and annexin V staining. Levels of cell cycle-related molecules and matrix metalloproteinases (MMP) were tested by Western blotting and ELISA, respectively.Results.Messenger RNA expression of HDAC1 was significantly higher in RA-SF than in OA-SF. Knockdown of HDAC1 and HDAC2 by siRNA resulted in decreased cell counts and cell proliferation, and increased apoptosis in RA-SF. Expression of p16, p21, and p53 was increased by knockdown of both HDAC1 and HDAC2. On the other hand, knockdown of HDAC1, but not of HDAC2, upregulated tumor necrosis factor-α-induced MMP-1 production by RA-SF.Conclusion.HDAC1 is overexpressed in RA-SF compared to OA-SF. HDAC1 supports cell proliferation and survival of RA-SF, but suppresses MMP-1 production. HDAC2 also plays an important role in cell proliferation and apoptosis of RA-SF. Our study provides useful information to develop new HDAC inhibitors for the treatment of RA.
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Mostofa, AGM, Allison Distler, Mark B. Meads, Eva Sahakian, John J. Powers, Tuan Nguyen, Melissa Alsina, et al. "Functional Analysis of HDAC11 in Plasma Cell Development and Multiple Myeloma Survival." Blood 132, Supplement 1 (November 29, 2018): 3223. http://dx.doi.org/10.1182/blood-2018-99-119119.

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Abstract Background: Histone deacetylases (HDACs) are potential novel therapeutic targets for multiple myeloma (MM) treatment. A pan-HDAC inhibitor (HDI) panobinostat was approved by the FDA in 2015 to treat relapsed/refractory MM patients, and several other HDIs are currently in different phases of clinical trials. However, unfavorable side-effects of the non-selective HDIs necessitate further dissection of the roles of individual HDAC isoforms to best target plasma cell malignancies with minimal toxicity. HDAC11 was recently found to regulate function in key immune cell populations including regulatory T cells, effector T cells, neutrophils, and myeloid-derived suppressor cells (MDSC). Though HDAC11 expression is confirmed in B cells and plasma cells, its functions in these cells remain largely unknown. In this study, we attempted a functional analysis of HDAC11 in plasma cell development along with its pro-tumorigenic function in MM cells. Methods: Mouse models, including a transgenic mouse strain expressing eGFP under the regulation of the HDAC11 promoter (Tg-HDAC11-eGFP), and also an HDA11-deficient mouse (B6.HDAC11-/-) were studied to establish the importance of HDAC11 in plasma cell biology. Pharmacologic inhibition of HDAC11 in MM cell lines was accomplished by using elevenostat, a new HDAC11-selective inhibitor in comparison with pan-inhibitors quisinostat and panobinostat. Impact on viability in human-derived MM cell lines was assessed using the CCK-8 assay, while induction of cell death was measured via detection of activated Caspase-3 and annexin/propidium iodide staining by flow cytometry. Synergy studies were performed by following the Chou-Talalay method for drug combinations. Post-translational modifications and subcellular localization changes induced by HDIs exposure were assessed by western blotting of fractionated cell lysates, while immunoprecipitation and proximity ligation assays (in situ PLA) were used to identify a binding partner for HDAC11. Results: Studies in Tg-HDAC11-eGFP mice reveal that HDAC11 expression in B cell lymphopoiesis is minimally detectable prior to B cell activation but demonstrates strong induction upon maturation into a plasma cell. Consistent with this, plasma cell development is markedly impaired in the absence of HDAC11. The HDAC11-selective inhibitor elevenostat showed significant cytotoxic potential in different MM cell lines that express moderate to high level of HDAC11, with IC50 values ranging 0.6-2.0 µM. Consistently, MM cell lines expressing null/very low level of HDAC11 were insensitive to elevenostat. Moreover, combining elevenostat with proteasome inhibitors bortezomib (BTZ) and carfilzomib resulted in significant synergistic effects evident from combination index (CI) and dose-reduction index (DRI) values measured by CompuSyn software. Elevenostat was also able to re-sensitize BTZ-resistant sub-clones (e.g., RPMI-8226-B25, KAS-6-V10R, and ANBL6-V10R) to BTZ and exhibited superior synergistic effects. Furthermore, elevenostat-treated cells showed a time-dependent alteration in the subcellular localization of HDAC11. HDAC11 gradually disappeared from the nuclear fractions with simultaneous upregulation in cytoplasmic fractions; similar observations were made from pan HDIs (quisinostat and panobinostat) treatment. However, unlike pan HDIs, the elevenostat treatment caused global downregulation of HDAC11 in some MM cell lines at the later time points (72 or 96 hrs), suggesting differential effects of various HDIs. Inhibition of HDAC11 also caused downstream suppression of several pro-tumorigenic factors of MM cells including IRF4 and c-Myc. Additionally, a novel interaction between HDAC11 and IRF4, an essential regulator of PC differentiation and MM survival, was identified by using PLA. HDAC11 dynamically interacts with IRF4 which can be induced by LPS stimulation and inhibited by HDIs, indicating the involvement of HDAC11 in the IRF4-mediated regulatory circuit. Conclusions: We observe that targeted inhibition of HDAC11 can impair MM cell survival and overcome acquired resistance to proteasome inhibitors. Furthermore, we identify IRF4 as a nuclear binding partner of HDAC11 and propose this interaction as a candidate mechanism regulating PC maturation and survival. Disclosures No relevant conflicts of interest to declare.
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Distler, Allison, Jason B. Brayer, Mark Meads, Eva Sahakian, John Joseph Powers, Melissa Alsina, Taiga Nishihori, et al. "HDAC11 as a candidate therapeutic target in multiple myeloma." Journal of Clinical Oncology 35, no. 15_suppl (May 20, 2017): 8029. http://dx.doi.org/10.1200/jco.2017.35.15_suppl.8029.

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8029 Background: Histone deacetylase (HDAC) inhibitors (HDI) have a therapeutic niche in multiple myeloma (MM) due to their ability to salvage proteasome inhibitor and immunomodulatory drug responsiveness in refractory patients, thus raising interest in this therapeutic class. Selective HDI may further improve therapeutic efficacy. Methods: B cell lymphopoiesis was evaluated using Tg-HDAC11-eGFP mice expressing eGFP regulated by the HDAC11 promoter and congenic mouse strains deficient in HDAC11 expression globally (B6.HDAC11-/-) or targeted to the B cell lineage (CD19Cre.HDAC11-/-). Molecular and pharmacologic means were used to impair HDAC11 in established MM cell lines. Viability was measured by activated caspase-3, Annexin/PI (A/PI) staining, and CCK-8 viability assay. Subcellular localization changes induced by HDI and identification of the novel binding partner IRF4 were assessed by proximity ligation assay (PLA). Results: Profound eGFP increases in PC of Tg-HDAC11-eGFP mice suggest HDAC11 influences late stage B cell development. In addition, HDAC11 deficiency results in dramatically reduced PC in the bone marrow and periphery. PC depletion in CD19Cre.HDAC11-/-mice suggests activity inherent in B cells rather than via externally derived signals. Quisinostat (QS), an HDI with enhanced HDAC11 selectivity, showed dose-dependent cytotoxicity in 10 MM cell lines (EC50 1-10nM). This activity was synergistic with bortezomib (BTZ) and carfilzomib (CFZ) in RPMI-8226 cells, while synergism was amplified in the BTZ-resistant RPMI-8226-B25 cell line. Exposure of RPMI-8226 cells to QS decreased detection of nuclear, but not cytosolic, HDAC11. Targeted siRNA–mediated silencing of HDAC11 in RPMI-8226 cells activated caspase-3 and reduced viability by A/PI staining. PLA of MM cell lines showed a novel interaction between HDAC11 and IRF4, an essential regulator of PC differentiation and MM survival, unmasking a potential mechanism for HDAC11-induced cytotoxicity in MM. This interaction was disrupted by QS. Conclusions: We show that HDAC11 inhibition reduces MM cell survival in vitro. Furthermore, we identify IRF4 as a binding partner for HDAC11 and propose this interaction as a candidate mechanism regulating PC maturation and MM survival.
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Kutil, Zsófia, Jana Mikešová, Matthes Zessin, Marat Meleshin, Zora Nováková, Glenda Alquicer, Alan Kozikowski, Wolfgang Sippl, Cyril Bařinka, and Mike Schutkowski. "Continuous Activity Assay for HDAC11 Enabling Reevaluation of HDAC Inhibitors." ACS Omega 4, no. 22 (November 15, 2019): 19895–904. http://dx.doi.org/10.1021/acsomega.9b02808.

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Keedy, Kara S., Nancie M. Archin, Adam T. Gates, Amy Espeseth, Daria J. Hazuda, and David M. Margolis. "A Limited Group of Class I Histone Deacetylases Acts To Repress Human Immunodeficiency Virus Type 1 Expression." Journal of Virology 83, no. 10 (March 11, 2009): 4749–56. http://dx.doi.org/10.1128/jvi.02585-08.

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ABSTRACT Silencing of the integrated human immunodeficiency virus type 1 (HIV-1) genome in resting CD4+ T cells is a significant contributor to the persistence of infection, allowing the virus to evade both immune detection and pharmaceutical attack. Nonselective histone deacetylase (HDAC) inhibitors are capable of inducing expression of quiescent HIV-1 in latently infected cells. However, potent global HDAC inhibition can induce host toxicity. To determine the specific HDACs that regulate HIV-1 transcription, we evaluated HDAC1 to HDAC11 RNA expression and protein expression and compartmentalization in the resting CD4+ T cells of HIV-1-positive, aviremic patients. HDAC1, -3, and -7 had the highest mRNA expression levels in these cells. Although all HDACs were detected in resting CD4+ T cells by Western blot analysis, HDAC5, -8, and -11 were primarily sequestered in the cytoplasm. Using chromatin immunoprecipitation assays, we detected HDAC1, -2, and -3 at the HIV-1 promoter in Jurkat J89GFP cells. Targeted inhibition of HDACs by small interfering RNA demonstrated that HDAC2 and HDAC3 contribute to repression of HIV-1 long terminal repeat expression in the HeLa P4/R5 cell line model of latency. Together, these results suggest that HDAC inhibitors specific for a limited number of class I HDACs may offer a targeted approach to the disruption of persistent HIV-1 infection.
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Wang, Dapeng, Fengdong Cheng, Yu Yu, Kenrick Semple, Lirong Peng, Elphine Telles, Noreen Luetteke, et al. "HDAC11 Inhibits T-Cell Response to Alloantigens and Reduces Gvhd In Mice." Blood 116, no. 21 (November 19, 2010): 1466. http://dx.doi.org/10.1182/blood.v116.21.1466.1466.

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Abstract Abstract 1466 Background: Histone acetyltransferases and histone deacetylases (HDAC) regulate gene expression through acetylation-deacetylation of histones. HDACs are the target of a family of compounds known as HDAC inhibitors, which have been shown to suppress pro-inflammatory cytokines and reduce acute graft-versus-host disease (GVHD) while preserving the graft-versus-leukemia (GVL) effect after allogeneic bone marrow transplantation (BMT) in mice. However, the role of individual HDAC members in the development of GVHD is not clear. Recently, HDAC11, the newest member of the HDAC family has emerged as an important transcriptional regulator of inflammatory responses in antigen-presenting cells (APCs)1. Here, we evaluated the role of HDAC11 on APCs and T cells in the allogeneic BMT setting in mice with genetic disruption of HDAC11. Method: Proliferation of wild-type (WT) and HDAC11 knock-out (KO) T cells in response to allogeneic antigens was compared by [H3] thymidine incorporation assay. Using the same method, we also tested the antigen presentation ability of WT and HDAC11 KO APCs. For in vivo studies, we used a clinical relevant mouse model of BMT: C57BL/6 (B6) ® BALB/c. To evaluate the role of HDAC11 in the function of T cells and APCs, WT and KO mice on B6 background were used as donors and recipients, respectively. Recipient survival was monitored daily and GVHD symptom was evaluated at least twice a week. HDAC11 KO mice were supplied by Merck and Co., Inc. Results: In vitro, HDAC11 KO T cells proliferated stronger than WT T cells under the stimulation of allogeneic APCs. Recipients of HDAC11 KO T cells lost significantly more body weight (p < 0.05), and died significantly sooner than those of WT T cells (p < 0.01). The pathologic score of KO recipients was higher than that of WT recipients in each of GVHD target organs including lung, liver, small intestine and colon. Mechanistically, we found that there were significantly more total and IFNγ-producing donor T cells in the recipients of KO cells than those of WT cells (p < 0.05). Collectively, HDAC11 KO T cells have higher activity in response to alloantigens in vitro and induced more severe GVHD in vivo compared to WT T cells. In contrast, KO and WT APCs had a similar ability to stimulate allogeneic T cells in vitro, and no significant difference in GVHD development was observed in WT or KO recipients after allogeneic BMT. Conclusion: HDAC11 negatively regulates T-cell function, but has no significant effect on APC function. This finding provides a rationale to promote T-cell immunity or tolerance by inhibiting or enhancing HDAC11, respectively. 1 Villagra et al. Nature Immunology, 10:92-100, 2009. Disclosures: No relevant conflicts of interest to declare.
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Dissertations / Theses on the topic "HDAC11 assay"

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Fatkins, David G. "N(EPSILON)-THIOACETYL-LYSINE AS A MULTIFACETED TOOL FOR ENZYMATIC PROTEIN LYSINE N(EPSILON)-DEACETYLATION." University of Akron / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=akron1185377018.

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Danielsson, Angelika. "Adenovirus-mediated Gene Therapy of Prostate Cancer." Doctoral thesis, Uppsala universitet, Enheten för klinisk immunologi, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-114132.

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Adenovirus-mediated gene therapy is a potential complement to standard cancer treatments. Advantages are that vectors can be used to target tumors and that replicating viruses lead to increased therapeutic dosage. In this thesis, an oncolytic serotype 5 adenovirus (Ad5), Ad[i/PPT-E1A, E3], was developed where viral replication is controlled by the insulator-shielded (i) prostate-specific PPT promoter. The adenoviral E3 region was inserted for its immune regulatory and lysis functions. Ad[i/PPT-E1A, E3] had improved cytotoxic abilities both in vitro and in a prostate cancer xenograft mouse model compared to a virus lacking the E3 region. To further improve adenoviral vectors, the histone deacetylase inhibitor (HDACi) FK228 was studied. FK228 has been proposed to enhance the effect of adenoviral therapy by upregulation of CAR, the primary receptor for Ad5 infection. In the present study, we observed that FK228 promotes transgene expression even better when administered after viral transduction, indicating a post-transductional enhancement of transgene expression. Another interesting finding was that FK228 reduced transgene expression from the PPT promoter in the prostate cancer cell line LNCaP. This is explained by the fact that different HDACi have the ability to provoke a neuroendocrine phenotype of LNCaP. A potential drawback with adenoviral gene therapy is the rapid clearance of the virus from the circulation. Viral particles have been coated with polyethylene glycol (PEG) to evade immune recognition, a strategy that works well in mouse models. However, less is known about the effects of adenoviral PEGylation in human blood. We have studied cell interactions and immune responses to PEGylated and uncoated Ad5 vectors in human whole blood using a blood loop model with constant blood flow. Limited effects of PEGylation were observed in human blood, which were associated with the neutralizing ability of the donor blood. An important finding that donors with high neutralizing ability in whole blood do not necessarily have neutralizing antibodies against the virus strongly implies that neutralization should be measured in whole blood.
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Wegener, Dennis. "Entwicklung eines HTS-geeigneten Enzymtests für Histondeacetylasen zur Entwicklung von HDAC-Inhibitoren." Doctoral thesis, 2004. http://hdl.handle.net/11858/00-1735-0000-0006-AE57-F.

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Hildmann, Christian. "Funktionelle Charakterisierung bakterieller Histondeacetylase-ähnlicher Amidohydrolasen (HDAH)." Doctoral thesis, 2005. http://hdl.handle.net/11858/00-1735-0000-0006-ABA2-E.

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Book chapters on the topic "HDAC11 assay"

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Wu, Mei-Yi, and Ray-Chang Wu. "A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity." In Methods in Molecular Biology, 3–13. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3667-0_1.

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Pons, Miriam, and Mandy Beyer. "Colony Formation Assay to Test the Impact of HDACi on Leukemic Cells." In Methods in Molecular Biology, 17–25. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2788-4_2.

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Nikolova, Teodora, Anja Göder, Ann Parplys, and Kerstin Borgmann. "DNA Fiber Spreading Assay to Test HDACi Effects on DNA and Its Replication." In Methods in Molecular Biology, 103–13. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6527-4_8.

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Conference papers on the topic "HDAC11 assay"

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Kupcho, Kevin R., Nathan J. Evans, Andrew L. Niles, Dan F. Lazar, and Thomas A. Kirkland. "Abstract 4237: Isoenzyme-selective HDAC activity assays." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4237.

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Kupcho, Kevin R., Nathan J. Evans, Andrew L. Niles, Thomas A. Kirkland, and Dan F. Lazar. "Abstract 4784: Selective bioluminogenic HDAC activity assays for profiling HDAC inhibitors." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4784.

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Kirkland, Thomas A., Andrew L. Niles, Michael A. Scurria, Tim Ugo, and Nathan Evans. "Abstract LB-94: A non-lytic, cell-based, bioluminescent HDAC assay." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-94.

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Evans, Nathan, Andrew L. Niles, and Thomas A. Kirkland. "Abstract 3028: A multiplexed, bioluminescent HDAC assay for determining target-specific, anti-cancer potency." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3028.

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Kiesel, Brian F., Robert A. Parise, Jette Tjornelund, Mette K. Christensen, Einars Loza, Edward Chu, Shivaani Kummar, and Jan H. Beumer. "Abstract 759: Quantitation of the HDAC inhibitor belinostat (PXD-101) and metabolites in human plasma by a novel LC-MS/MS assay." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-759.

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Reports on the topic "HDAC11 assay"

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HDAC6 screening dataset using tau-based substrate in an enzymatic assay yields selective inhibitors and activators. EMBL-EBI, August 2022. http://dx.doi.org/10.6019/chembl4808148.

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