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Relevant bibliographies by topics / Jumonji Domain-Containing Histone Demethylases

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Academic literature on the topic 'Jumonji Domain-Containing Histone Demethylases'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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Journal articles on the topic "Jumonji Domain-Containing Histone Demethylases"

1

Leon, Kelly E., and Katherine M. Aird. "Jumonji C Demethylases in Cellular Senescence." Genes 10, no. 1 (January 9, 2019): 33. http://dx.doi.org/10.3390/genes10010033.

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Senescence is a stable cell cycle arrest that is either tumor suppressive or tumor promoting depending on context. Epigenetic changes such as histone methylation are known to affect both the induction and suppression of senescence by altering expression of genes that regulate the cell cycle and the senescence-associated secretory phenotype. A conserved group of proteins containing a Jumonji C (JmjC) domain alter chromatin state, and therefore gene expression, by demethylating histones. Here, we will discuss what is currently known about JmjC demethylases in the induction of senescence, and how these enzymes suppress senescence to contribute to tumorigenesis.

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Liu, Haolin, Chao Wang, Schuyler Lee, Yu Deng, Matthew Wither, Sangphil Oh, Fangkun Ning, et al. "Clipping of arginine-methylated histone tails by JMJD5 and JMJD7." Proceedings of the National Academy of Sciences 114, no. 37 (August 28, 2017): E7717—E7726. http://dx.doi.org/10.1073/pnas.1706831114.

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Two of the unsolved, important questions about epigenetics are: do histone arginine demethylases exist, and is the removal of histone tails by proteolysis a major epigenetic modification process? Here, we report that two orphan Jumonji C domain (JmjC)-containing proteins, JMJD5 and JMJD7, have divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD5 and JMJD7, acting as aminopeptidases, progressively digest the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones. Furthermore, depletion of JMJD7 in breast cancer cells greatly decreases cell proliferation. The protease activities of JMJD5 and JMJD7 represent a mechanism for removal of histone tails bearing methylated arginine residues and define a potential mechanism of transcription regulation.

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Pollard, Patrick J., Christoph Loenarz, David R. Mole, Michael A. McDonough, Jonathan M. Gleadle, Christopher J. Schofield, and Peter J. Ratcliffe. "Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1α." Biochemical Journal 416, no. 3 (November 26, 2008): 387–94. http://dx.doi.org/10.1042/bj20081238.

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The transcription factor HIF (hypoxia-inducible factor) mediates a highly pleiotrophic response to hypoxia. Many recent studies have focused on defining the extent of this transcriptional response. In the present study we have analysed regulation by hypoxia among transcripts encoding human Fe(II)- and 2-oxoglutarate-dependent oxygenases. Our results show that many of these genes are regulated by hypoxia and define two groups of histone demethylases as new classes of hypoxia-regulated genes. Patterns of induction were consistent across a range of cell lines with JMJD1A (where JMJD is Jumonji-domain containing) and JMJD2B demonstrating robust, and JMJD2C more modest, up-regulation by hypoxia. Functional genetic and chromatin immunoprecipitation studies demonstrated the importance of HIF-1α in mediating these responses. Given the importance of histone methylation status in defining patterns of gene expression under different physiological and pathophysiological conditions, these findings predict a role for the HIF system in epigenetic regulation.

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Cui, Xiaoyun, Yu Zheng, Yue Lu, Emmanuelle Issakidis-Bourguet, and Dao-Xiu Zhou. "Metabolic control of histone demethylase activity involved in plant response to high temperature." Plant Physiology 185, no. 4 (January 28, 2021): 1813–28. http://dx.doi.org/10.1093/plphys/kiab020.

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Abstract Jumonji C (JmjC) domain proteins are histone lysine demethylases that require ferrous iron and alpha-ketoglutarate (or α-KG) as cofactors in the oxidative demethylation reaction. In plants, α-KG is produced by isocitrate dehydrogenases (ICDHs) in different metabolic pathways. It remains unclear whether fluctuation of α-KG levels affects JmjC demethylase activity and epigenetic regulation of plant gene expression. In this work, we studied the impact of loss of function of the cytosolic ICDH (cICDH) gene on the function of histone demethylases in Arabidopsis thaliana. Loss of cICDH resulted in increases of overall histone H3 lysine 4 trimethylation (H3K4me3) and enhanced mutation defects of the H3K4me3 demethylase gene JMJ14. Genetic analysis suggested that the cICDH mutation may affect the activity of other demethylases, including JMJ15 and JMJ18 that function redundantly with JMJ14 in the plant thermosensory response. Furthermore, we show that mutation of JMJ14 affected both the gene activation and repression programs of the plant thermosensory response and that JMJ14 and JMJ15 repressed a set of genes that are likely to play negative roles in the process. The results provide evidence that histone H3K4 demethylases are involved in the plant response to elevated ambient temperature.

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Hickok, Jason R., Divya Vasudevan, William E. Antholine, and Douglas D. Thomas. "Nitric Oxide Modifies Global Histone Methylation by Inhibiting Jumonji C Domain-containing Demethylases." Journal of Biological Chemistry 288, no. 22 (April 1, 2013): 16004–15. http://dx.doi.org/10.1074/jbc.m112.432294.

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Hickok, Jason R., Divya Vasudevan, and Douglas D. Thomas. "Nitric Oxide Modifies Histone Methylation Patterns by Inhibiting Jumonji C Domain Containing Demethylases." Free Radical Biology and Medicine 53 (November 2012): S181. http://dx.doi.org/10.1016/j.freeradbiomed.2012.10.499.

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Chopra, Anand, Hemanta Adhikary, William G. Willmore, and Kyle K. Biggar. "Insights into The Function and Regulation of Jumonji C Lysine Demethylases as Hypoxic Responsive Enzymes." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 642–54. http://dx.doi.org/10.2174/1389203721666191231104225.

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Cellular responses to hypoxia (low oxygen) are governed by oxygen sensitive signaling pathways. Such pathways, in part, are controlled by enzymes with oxygen-dependent catalytic activity, of which the role of prolyl 4-hydroxylases has been widely reviewed. These enzymes inhibit hypoxic response by inducing the oxygen-dependent degradation of hypoxia-inducible factor 1α, the master regulator of the transcriptional hypoxic response. Jumonji C domain-containing lysine demethylases are similar enzymes which share the same oxygen-dependent catalytic mechanism as prolyl 4- hydroxylases. Traditionally, the role of lysine demethylases has been studied in relation to demethylation activity against histone substrates, however, within the past decade an increasing number of nonhistone protein targets have been revealed, some of which have a key role in survival in the hypoxic tumor microenvironment. Within this review, we highlight the involvement of methyllysine in the hypoxic response with a focus on the HIF signaling pathway, the regulation of demethylase activity by oxygen, and provide insights into notable areas of future hypoxic demethylase research.

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Xu, Xin, Wilhelm G. Dirks, Hans G. Drexler, and Zhenbo Hu. "Small Molecular Modulators of Histone Demethylases Selectively Inhibits Growth of Hematopoietic Malignancies." Blood 132, Supplement 1 (November 29, 2018): 3941. http://dx.doi.org/10.1182/blood-2018-99-112376.

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Abstract Background: About 10% of acute leukemia (AL) patients harbor MLL-r(earrangements). MLLr acute myeloid leukemia (AML) mainly occurs in young-to-middle-aged adults whereas MLLr acute lymphoblastic leukemia (ALL) mainly occurs in patients younger than 1 year at diagnosis. AML with MLL fusion to MLLT3 via t(9;11)(p22;q23) predicts intermediate prognosis whereas MLL fusion to other partners predicts adverse prognosis. By contrast, in infants with ALL MLLr invariably confers poor prognosis. Much efforts have been made to identify and target proteins required for initiation and maintenance of MLLr AL, with an aim to improve the prognosis of this aggressive AL subtype. Multiple writers, erasers, and readers of histone post-translational modifications (PTMs) have been identified to be fundamental for the initiation and maintenance of MLLr AL. Small molecular inhibitors of some of these chromatin-associated proteins have been identified, such as EPZ004777 against DOT1L, JQ1 and I-BET151 against BRD4, and so on which are also under clinical trials for AL treatment. Among histone modification erasers essential for MLLr AL, JMJD1C and KDM4C that share Jumonji catalytic domain are fundamental for MLLr AL maintenance. Histone H3 lysine 9 (H3K9) demethylase JMJD1C is one of the most promising MLLr AL targets. Multiple independent studies identified JMJD1C as required for MLLr AML, RUNX1(AML1)/RUNX1T1(ETO) AML and even chronic myeloid leukemia and lymphoma cells but not normal hematopoiesis. KDM4C Is essential for Initiation and maintenance of MLLr AL transcriptional profiling of which is dependent on KDM4C. Moreover, pharmacological inhibition of KDM4C blocks leukemia development in syngeneic mouse model and human AML xenograft model. Although a large number of special inhibitors of histone demethylases have been developed, no special inhibitors against KDM3 family member like JMJD1C have been reported. Results: Here we focused on Jumonji domain that is responsible for enzymatic activities of histone demethylases for identifying potential small molecule modulators of histone demethylases. We selected Jumonji domain of histone H3 lysine (H3K9) demethylase JMJD1C with KDM4C as reference to screen for potential small molecular modulators from 149,519 natural products and 33,765 Chinese medicine components through virtual screening method. Although identified independently from each other, compound #4 and #12 both share a common structural backbone and surface plasmon resonance analysis showed that #4 and #12 bind to JMJD1C, KDM3 family member KDM3B, and KDM4 family member KDM4C with modest affinity. In vivo demethylation assay showed that #4 induces global increase of H3K9 methylation. In vitro demethylation assay showed that #4 is able to reverse H3K9 demethylation conferred by KDM3B and KDM4C. We thus named #4 and #12 as JI-4 and JI-12 (JI, Jumonji inhibitor). Cell proliferation and colony formation assays showed that JI-4 and JI-12 predominantly kill MLLr AL. To increase evidence, multiple similar compounds to JI-4 and JI-12 were tested for cell proliferation repression and JI-16 was found to show superior killing activities against hematopoietic malignant cells compared to JI-4 and JI-12. Mechanistically, JI-16 not only induces apoptosis but also differentiation of MLLr AL cells. Transcriptome analysis and quantitative PCR (QPCR) showed that JI-16 induced gene expression profiling is especially enriched in gene sets involved in metabolism. Conclusion: To sum up, we identified potential pan-inhibitors of the Jumonji domain of histone demethylases. Binding in-vivo is followed by selective killing of MLLr AL cells. Disclosures. No relevant conflicts of interest to declare. Disclosures No relevant conflicts of interest to declare.

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Hastar, N., D. Koca, and Y. Baran. "PP-074 INHIBITION OF JUMONJI C DOMAIN CONTAINING HISTONE DEMETHYLASES IN ACUTE MYELOID LEUKEMIA." Leukemia Research 38 (October 2014): S50. http://dx.doi.org/10.1016/s0145-2126(14)70128-6.

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Cho, Yumi, Ki Hyun Kim, Yoon Sun Cho, Wenqing Xu, Xiang Wang, and Ho Jeong Kwon. "A histone demethylase inhibitor, methylstat, inhibits angiogenesis in vitro and in vivo." RSC Adv. 4, no. 72 (2014): 38230–33. http://dx.doi.org/10.1039/c4ra07154a.

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Histone methylation has been highlighted in the regulation of gene expression. Methylstat, a Jumonji C domain containing histone demethylase inhibitor, inhibitedin vitroandin vivoangiogenesis at nontoxic dose. Collectively, methylstat could be a promising chemical probe for addressing its role in angiogenesis

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Dissertations / Theses on the topic "Jumonji Domain-Containing Histone Demethylases"

1

Wenzler, Sandra [Verfasser], and Manfred [Akademischer Betreuer] Jung. "Synthesis and testing of inhibitors for jumonjiC domain-containing histone demethylases." Freiburg : Universität, 2020. http://d-nb.info/1238016022/34.

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Roatsch, Martin [Verfasser], and Manfred [Akademischer Betreuer] Jung. "Assays and Inhibitors for JumonjiC Domain-Containing Histone Demethylases as Epigenetic Regulators." Freiburg : Universität, 2016. http://d-nb.info/1136263446/34.

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Hu, Yu-Jie. "Roles of Protein Arginine Methyltransferase 7 and Jumonji Domain-Containing Protein 6 in Adipocyte Differentiation: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/797.

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Regulation of gene expression comprises a wide range of mechanisms that control the abundance of gene products in response to environmental and developmental changes. These biological processes can be modulated by posttranslational modifications including arginine methylation. Among the enzymes that catalyze the methylation, protein arginine methyltransferase 7 (PRMT7) is known to modify histones to repress gene expression. Jumonji domain-containing protein 6 (JMJD6) is a putative arginine demethylase that potentially antagonize PRMT7. However, the biological significance of these enzymes is not well understood. This thesis summarizes the investigation of both PRMT7 and JMJD6 in cell culture models for adipocyte differentiation. The results suggest that PRMT7 is not required for the differentiation, whereas JMJD6 is necessary for the differentiation by promoting the expression of the lineage determining transcription factors peroxisome proliferator-activated receptor γ (PPARγ) and CCAAT/enhancerbinding proteins (C/EBPs). The underlying mechanisms by which JMJD6 regulate differentiation involve transcriptional and post-transcriptional control of gene expression. Unexpectedly, the adipogenic function of JMJD6 is independent of its enzymatic activity. Collectively, the present research reveals a novel role of JMJD6 in gene regulation during the differentiation of adipocytes.

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Hu, Yu-Jie. "Roles of Protein Arginine Methyltransferase 7 and Jumonji Domain-Containing Protein 6 in Adipocyte Differentiation: A Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/797.

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Regulation of gene expression comprises a wide range of mechanisms that control the abundance of gene products in response to environmental and developmental changes. These biological processes can be modulated by posttranslational modifications including arginine methylation. Among the enzymes that catalyze the methylation, protein arginine methyltransferase 7 (PRMT7) is known to modify histones to repress gene expression. Jumonji domain-containing protein 6 (JMJD6) is a putative arginine demethylase that potentially antagonize PRMT7. However, the biological significance of these enzymes is not well understood. This thesis summarizes the investigation of both PRMT7 and JMJD6 in cell culture models for adipocyte differentiation. The results suggest that PRMT7 is not required for the differentiation, whereas JMJD6 is necessary for the differentiation by promoting the expression of the lineage determining transcription factors peroxisome proliferator-activated receptor γ (PPARγ) and CCAAT/enhancerbinding proteins (C/EBPs). The underlying mechanisms by which JMJD6 regulate differentiation involve transcriptional and post-transcriptional control of gene expression. Unexpectedly, the adipogenic function of JMJD6 is independent of its enzymatic activity. Collectively, the present research reveals a novel role of JMJD6 in gene regulation during the differentiation of adipocytes.

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"JMJD3 acts as a tumor suppressor by disrupting cytoskeleton in pancreatic ductal adenocarcinoma cells." 2013. http://library.cuhk.edu.hk/record=b5884440.

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Xiao, Zhangang.
Thesis (Ph.D.)--Chinese University of Hong Kong, 2013.
Includes bibliographical references (leaves 118-131).
Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web.
Abstracts also in Chinese.

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Book chapters on the topic "Jumonji Domain-Containing Histone Demethylases"

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Staller, Peter. "Inhibitors of Jumonji C-Domain Histone Demethylases." In Epigenetic Cancer Therapy, 439–69. Elsevier, 2015. http://dx.doi.org/10.1016/b978-0-12-800206-3.00020-3.

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Conference papers on the topic "Jumonji Domain-Containing Histone Demethylases"

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Muecke, Christian, Swati Dabral, Werner Seeger, and Soni Savai Pullamsetti. "Role and regulation of Jumonji C domain-containing histone demethylases 1A and 2B in pulmonary hypertension." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa5092.

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Alves, Juliano, Said Goueli, and Hicham Zegzouti. "Abstract 362: A homogeneous bioluminescent succinate assay for detection of jumonjiC domain-containing histone demethylase activities." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-362.

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