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Journal articles on the topic 'Hyperacetylation'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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1

Sudo, Haruka, and Akira Kubo. "The Aneugenicity of Ketone Bodies in Colon Epithelial Cells Is Mediated by Microtubule Hyperacetylation and Is Blocked by Resveratrol." International Journal of Molecular Sciences 22, no. 17 (2021): 9397. http://dx.doi.org/10.3390/ijms22179397.

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Diabetes mellitus (DM) is considered to be associated with an increased risk of colorectal cancer. Recent studies have also revealed that tubulin hyperacetylation is caused by a diabetic status and we have reported previously that, under microtubule hyperacetylation, a microtubule severing protein, katanin-like (KL) 1, is upregulated and contributes to tumorigenesis. To further explore this phenomenon, we tested the effects of the ketone bodies, acetoacetate and β-hydroxybutyrate, in colon and fibroblast cells. Both induced microtubule hyperacetylation that responded differently to a histone d

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Rao, Rekha, Warren Fiskus, Yonghua Yang, et al. "HDAC6 inhibition enhances 17-AAG–mediated abrogation of hsp90 chaperone function in human leukemia cells." Blood 112, no. 5 (2008): 1886–93. http://dx.doi.org/10.1182/blood-2008-03-143644.

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Abstract Histone deacetylase 6 (HDAC6) is a heat shock protein 90 (hsp90) deacetylase. Treatment with pan-HDAC inhibitors or depletion of HDAC6 by siRNA induces hyperacetylation and inhibits ATP binding and chaperone function of hsp90. Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins. In this study, we determined the effect of hsp90 hyperacetylation on the anti-hsp90 and antileukemia activity of 17-AAG. Hyperacetylation of hsp90 increased i

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Calestagne-Morelli, Alison, and Juan Ausió. "Long-range histone acetylation: biological significance, structural implications, and mechanismsThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (2006): 518–27. http://dx.doi.org/10.1139/o06-067.

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Genomic characterization of various euchromatic regions in higher eukaryotes has revealed that domain-wide hyperacetylation (over several kb) occurs at a range of loci, including individual genes, gene family clusters, compound clusters, and more general clusters of unrelated genes. Patterns of long-range histone hyperacetylation are strictly conserved within each unique cellular system studied and they reflect biological variability in gene regulation. Domain-wide histone acetylation consists generally of nonuniform peaks of enriched hyperacetylation of specific core histones, histone isoform

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Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004-5014.1992.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of

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Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of

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Kajino, Hidetoshi, Tomomi Nagatani, Miku Oi, et al. "Synthetic hyperacetylation of nucleosomal histones." RSC Chemical Biology 1, no. 2 (2020): 56–59. http://dx.doi.org/10.1039/d0cb00029a.

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Na, Ann-Yae, Sanjita Paudel, Soyoung Choi, et al. "Global Lysine Acetylome Analysis of LPS-Stimulated HepG2 Cells Identified Hyperacetylation of PKM2 as a Metabolic Regulator in Sepsis." International Journal of Molecular Sciences 22, no. 16 (2021): 8529. http://dx.doi.org/10.3390/ijms22168529.

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Sepsis-induced liver dysfunction (SILD) is a common event and is strongly associated with mortality. Establishing a causative link between protein post-translational modification and diseases is challenging. We studied the relationship among lysine acetylation (Kac), sirtuin (SIRTs), and the factors involved in SILD, which was induced in LPS-stimulated HepG2 cells. Protein hyperacetylation was observed according to SIRTs reduction after LPS treatment for 24 h. We identified 1449 Kac sites based on comparative acetylome analysis and quantified 1086 Kac sites on 410 proteins for acetylation. Int

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Sudo, Haruka. "Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation under a Tau Deficiency in Mammary Epithelial Cells." International Journal of Molecular Sciences 19, no. 9 (2018): 2488. http://dx.doi.org/10.3390/ijms19092488.

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Enhanced microtubule acetylation has been identified as a negative prognostic indicator in breast cancer. We reported previously that primary cultured human mammary epithelial cells manifest breast cancer-related aneuploidization via the activation of severing protein katanin-like (KL)1 when tau is deficient. To address in this current study whether microtubule hyperacetylation is involved in breast carcinogenesis through mitosis, the effects of tubacin on human mammary epithelial cells were tested using immunofluorescence techniques. Tau-knockdown cells showed enhancement of KL1-dependent eve

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Wu, James T., Sonia Y. Archer, Brian Hinnebusch, Shufen Meng, and Richard A. Hodin. "Transient vs. prolonged histone hyperacetylation: effects on colon cancer cell growth, differentiation, and apoptosis." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 3 (2001): G482—G490. http://dx.doi.org/10.1152/ajpgi.2001.280.3.g482.

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The role of histone hyperacetylation in regard to growth, differentiation, and apoptosis in colon cancer cells was assessed in an in vitro model system. HT-29 cells were grown in ±10% fetal bovine serum with either 5 mM sodium butyrate or 0.3 μM trichostatin A [single dose (T) or 3 doses 8 h apart (TR)] for 24 h. Serum-starved HT-29 cells were further treated with epidermal growth factor or insulin-like growth factor I for an additional 24 h. Apoptosis was quantified with propidium iodide and characterized by electron microscopy. Northern blot analyses were performed with cDNA probes specific

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Gupta, Ramesh C., Kristina Szekely, Kefei Zhang, David E. Lanfear, and Hani N. Sabbah. "Evidence of Hyperacetylation of Mitochondrial Regulatory Proteins in Left Ventricular Myocardium of Dogs with Chronic Heart Failure." International Journal of Molecular Sciences 26, no. 8 (2025): 3856. https://doi.org/10.3390/ijms26083856.

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Increased acetylation or “hyperacetylation” of mitochondrial (MITO) proteins can lead to abnormalities of the electron transport chain (ETC) and oxidative phosphorylation. In this study we examined the levels of proteins that regulate acetylation. Studies were performed in isolated MITO fractions from left ventricular (LV) myocardium of seven healthy normal (NL) dogs and seven dogs with coronary microembolization-induced heart failure (HF, LV ejection fraction ~35%). Protein levels of drivers of hyperacetylation, namely sirtuin-3 (Sirt-3), a MITO deacetylase, and CD38, a regulator of nicotinam

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Glon, Damien, Géraldine Vilmen, Daniel Perdiz, et al. "Essential role of hyperacetylated microtubules in innate immunity escape orchestrated by the EBV-encoded BHRF1 protein." PLOS Pathogens 18, no. 3 (2022): e1010371. http://dx.doi.org/10.1371/journal.ppat.1010371.

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Innate immunity constitutes the first line of defense against viruses, in which mitochondria play an important role in the induction of the interferon (IFN) response. BHRF1, a multifunctional viral protein expressed during Epstein-Barr virus reactivation, modulates mitochondrial dynamics and disrupts the IFN signaling pathway. Mitochondria are mobile organelles that move through the cytoplasm thanks to the cytoskeleton and in particular the microtubule (MT) network. MTs undergo various post-translational modifications, among them tubulin acetylation. In this study, we demonstrated that BHRF1 i

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Natarajan, Umamaheswari, Thiagarajan Venkatesan, and Appu Rathinavelu. "Effect of the HDAC Inhibitor on Histone Acetylation and Methyltransferases in A2780 Ovarian Cancer Cells." Medicina 57, no. 5 (2021): 456. http://dx.doi.org/10.3390/medicina57050456.

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Background andObjective: Epigenetic modifications are believed to play a significant role in the development of cancer progression, growth, differentiation, and cell death. One of the most popular histone deacetylases inhibitors (HDACIs), suberoylanilide hydroxamic acid (SAHA), also known as Vorinostat, can directly activate p21WAF1/CIP1 gene transcription through hyperacetylation of histones by a p53 independent mechanism. In the present investigation, we evaluated the correlation between histone modifications and DNA methyltransferase enzyme levels following SAHA treatments in A2780 ovarian

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Schübeler, Dirk, Claire Francastel, Daniel M. Cimbora, Andreas Reik, David I. K. Martin та Mark Groudine. "Nuclear localization and histone acetylation: a pathway for chromatin opening and transcriptional activation of the human β-globin locus". Genes & Development 14, № 8 (2000): 940–50. http://dx.doi.org/10.1101/gad.14.8.940.

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We have investigated the mechanism, structural correlates, andcis-acting elements involved in chromatin opening and gene activation, using the human β-globin locus as a model. Full transcriptional activity of the human β-globin locus requires the locus control region (LCR), composed of a series of nuclease hypersensitive sites located upstream of this globin gene cluster. Our previous analysis of naturally occurring and targeted LCR deletions revealed that chromatin opening and transcriptional activity in the endogenous β-globin locus are dissociable and dependent on distinctcis-acting element

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Fromm, George, Christina de Vries, Rachel Byron та ін. "Histone hyperacetylation within the β-globin locus is context-dependent and precedes high-level gene expression". Blood 114, № 16 (2009): 3479–88. http://dx.doi.org/10.1182/blood-2009-03-210690.

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Abstract Active gene promoters are associated with covalent histone modifications, such as hyperacetylation, which can modulate chromatin structure and stabilize binding of transcription factors that recognize these modifications. At the β-globin locus and several other loci, however, histone hyperacetylation extends beyond the promoter, over tens of kilobases; we term such patterns of histone modifications “hyperacetylated domains.” Little is known of either the mechanism by which these domains form or their function. Here, we show that domain formation within the murine β-globin locus occurs

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Shepard, Blythe-D. "Alcohol-induced protein hyperacetylation: Mechanisms and consequences." World Journal of Gastroenterology 15, no. 10 (2009): 1219. http://dx.doi.org/10.3748/wjg.15.1219.

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16

Adenot, P. G., Y. Mercier, J. P. Renard, and E. M. Thompson. "Differential H4 acetylation of paternal and maternal chromatin precedes DNA replication and differential transcriptional activity in pronuclei of 1-cell mouse embryos." Development 124, no. 22 (1997): 4615–25. http://dx.doi.org/10.1242/dev.124.22.4615.

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In the mouse embryo, transcriptional activation begins during S/G2 phase of the first cell cycle when paternal and maternal chromatin are still in separate nuclear entities within the same cytoplasm. At this time, the male pronucleus exhibits greater transcriptional activity than the female pronucleus. Since acetylation of histones in the nucleosome octamer exerts a regulatory influence on gene expression, we investigated changes in histone acetylation during the remodeling of paternal and maternal chromatin from sperm entry through to minor genome activation and mitosis. We found (1) neither

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Saisomboon, Saowaluk, Ryusho Kariya, Panupong Mahalapbutr, et al. "Augmented Global Protein Acetylation Diminishes Cell Growth and Migration of Cholangiocarcinoma Cells." International Journal of Molecular Sciences 25, no. 18 (2024): 10170. http://dx.doi.org/10.3390/ijms251810170.

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We have previously shown that the overexpression of acetyl-CoA carboxylase 1 (ACC1) was associated with the poor prognosis of cholangiocarcinoma (CCA) patients, and suppression of its expression in CCA cell lines deteriorated cell growth. The present study explored the mechanism by which ACC1 inhibition affects global protein acetylation, using genetic knockdown and pharmacological inhibition with an ACC1 inhibitor ND-646 as models. Both ACC1 knockdown and ACC1-inhibitor-treated cells displayed the hyperacetylation of proteins, accompanied by impaired growth and migration. The immunoprecipitat

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Ringel, Alison E., Anne M. Cieniewicz, Sean D. Taverna, and Cynthia Wolberger. "Nucleosome competition reveals processive acetylation by the SAGA HAT module." Proceedings of the National Academy of Sciences 112, no. 40 (2015): E5461—E5470. http://dx.doi.org/10.1073/pnas.1508449112.

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The Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon histone 3 lysine 4 trimethylation (H3K4me3), a histone mark enriched at promoters of actively transcribed genes. SAGA contains a separable subcomplex known as the histone acetyltransferase (HAT) module that contains the HAT, Gcn5, bound to Sgf29, Ada2, and Ada3. Sgf29 contains a tandem Tudor domain that recognizes H3K4me3-containing peptides and is required for histone hyperacetylation in vivo. However, the mechanism by which H3K4me3 recognition leads to lysine hype

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Shepard, Blythe D., Dean J. Tuma, and Pamela L. Tuma. "Chronic Ethanol Consumption Induces Global Hepatic Protein Hyperacetylation." Alcoholism: Clinical and Experimental Research 34, no. 2 (2010): 280–91. http://dx.doi.org/10.1111/j.1530-0277.2009.01091.x.

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Niles, Lennard P., Yi Pan, Sean Kang, and Ayush Lacoul. "Melatonin induces histone hyperacetylation in the rat brain." Neuroscience Letters 541 (April 2013): 49–53. http://dx.doi.org/10.1016/j.neulet.2013.01.050.

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Párrizas, Marcelina, Miguel A. Maestro, Sylvia F. Boj та ін. "Hepatic Nuclear Factor 1-α Directs Nucleosomal Hyperacetylation to Its Tissue-Specific Transcriptional Targets". Molecular and Cellular Biology 21, № 9 (2001): 3234–43. http://dx.doi.org/10.1128/mcb.21.9.3234-3243.2001.

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ABSTRACT Mutations in the gene encoding hepatic nuclear factor 1-α (HNF1-α) cause a subtype of human diabetes resulting from selective pancreatic β-cell dysfunction. We have analyzed mice lacking HNF1-α to study how this protein controls β-cell-specific transcription in vivo. We show that HNF1-α is essential for the expression ofglut2 glucose transporter and L-type pyruvate kinase (pklr) genes in pancreatic insulin-producing cells, whereas in liver, kidney, or duodenum tissue, glut2 andpklr expression is maintained in the absence of HNF1-α. HNF1-α nevertheless occupies the endogenous glut2 and

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Blottiere, Herve M., Bruno Buecher, Jean-Paul Galmiche, and Christine Cherbut. "Molecular analysis of the effect of short-chain fatty acids on intestinal cell proliferation." Proceedings of the Nutrition Society 62, no. 1 (2003): 101–6. http://dx.doi.org/10.1079/pns2002215.

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Short-chain fatty acids (SCFA), particularly butyrate, were shown to regulate cell proliferation in vitro and in vivo. Indeed, butyrate is the major fuel for colonic epithelial cells, and it can influence cell proliferation through the release of growth factors or gastrointestinal peptides such as gastrin, or through modulation of mucosal blood flow. Lastly, SCFA can act directly on genes regulating cell proliferation, and butyrate is the main SCFA to display such an effect. Butyrate inhibits histone deacetylase, which will allow histone hyperacetylation. Such hyperacetylation leads to transcr

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Burlibaşa, Liliana, Andreea Carmen Ionescu, and Delia-Mihaela Dragusanu. "Histone hyperacetylation and DNA methylation interplay during murine spermatogenesis." Zygote 27, no. 05 (2019): 305–14. http://dx.doi.org/10.1017/s0967199419000303.

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SummaryMale germ cell development is a critical period during which epigenetic patterns are established and maintained. The progression from diploid spermatogonia to haploid spermatozoa involves the incorporation of testis-specific histone variants, mitotic and meiotic divisions, haploid gene expression, histone–protamine transitions and massive epigenetic reprogramming. Understanding the protein players and the epigenetic mark network involved in the setting of the epigenetic programme in spermatogenesis is an exciting new clue in the field of reproductive biology with translational outcomes.

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Waterborg, Jakob H., and Tamás Kapros. "Kinetic analysis of histone acetylation turnover and Trichostatin A induced hyper- and hypoacetylation in alfalfa." Biochemistry and Cell Biology 80, no. 3 (2002): 279–93. http://dx.doi.org/10.1139/o02-021.

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Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially

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Xie, Xina, Xuhong Song, Song Yuan, et al. "Histone acetylation regulates orphan nuclear receptor NR4A1 expression in hypercholesterolaemia." Clinical Science 129, no. 12 (2015): 1151–61. http://dx.doi.org/10.1042/cs20150346.

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(i) mRNA levels of orphan nuclear receptor NR4A1 positively correlate with increased total cholesterol and low-density lipoprotein cholesterol levels in plasma. (ii) Histone H3 hyperacetylation is involved in hypercholesterolaemia-induced NR4A1 expression in monocytes. (iii) NR4A1 mediates self-protection responses in hypercholesterolaemia-induced inflammation.

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Lee, Jin-Kwan, Janet Lee, Heounjeong Go, et al. "Oncogenic microtubule hyperacetylation through BEX4-mediated sirtuin 2 inhibition." Cell Death & Disease 7, no. 8 (2016): e2336-e2336. http://dx.doi.org/10.1038/cddis.2016.240.

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Sarg, Bettina, Wilfried Helliger, Heribert Talasz, Elisavet Koutzamani, and Herbert H. Lindner. "Histone H4 Hyperacetylation Precludes Histone H4 Lysine 20 Trimethylation." Journal of Biological Chemistry 279, no. 51 (2004): 53458–64. http://dx.doi.org/10.1074/jbc.m409099200.

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Libertini, L. J., J. Ausió, K. E. van Holde, and E. W. Small. "Histone hyperacetylation. Its effects on nucleosome core particle transitions." Biophysical Journal 53, no. 4 (1988): 477–87. http://dx.doi.org/10.1016/s0006-3495(88)83126-6.

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Lu, B., D. J. Antoine, K. Kwan, et al. "JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation." Proceedings of the National Academy of Sciences 111, no. 8 (2014): 3068–73. http://dx.doi.org/10.1073/pnas.1316925111.

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Ausio, Juan, and K. E. Van Holde. "Histone hyperacetylation: its effects on nucleosome conformation and stability." Biochemistry 25, no. 6 (1986): 1421–28. http://dx.doi.org/10.1021/bi00354a035.

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Li, Lin, Sriram Jayabal, Mohammad Ghorbani, et al. "ATAT1 regulates forebrain development and stress-induced tubulin hyperacetylation." Cellular and Molecular Life Sciences 76, no. 18 (2019): 3621–40. http://dx.doi.org/10.1007/s00018-019-03088-3.

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Gryder, Berkley E., Silvia Pomella, Carly Sayers, et al. "Histone hyperacetylation disrupts core gene regulatory architecture in rhabdomyosarcoma." Nature Genetics 51, no. 12 (2019): 1714–22. http://dx.doi.org/10.1038/s41588-019-0534-4.

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Granit, Avital, Nino Tetro, Miri Shmuel, Tamar Peretz, and Sara Eyal. "Lacosamide at therapeutic concentrations induces histone hyperacetylation in vitro." Epilepsia Open 3, no. 4 (2018): 535–39. http://dx.doi.org/10.1002/epi4.12269.

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Tong, Dan, Gabriele G. Schiattarella, Nan Jiang, et al. "NAD + Repletion Reverses Heart Failure With Preserved Ejection Fraction." Circulation Research 128, no. 11 (2021): 1629–41. http://dx.doi.org/10.1161/circresaha.120.317046.

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Rationale: Heart failure with preserved ejection fraction (HFpEF) is a mortal clinical syndrome without effective therapies. We recently demonstrated in mice that a combination of metabolic and hypertensive stress recapitulates key features of human HFpEF. Objective: Using this novel preclinical HFpEF model, we set out to define and manipulate metabolic dysregulations occurring in HFpEF myocardium. Methods and Results: We observed impairment in mitochondrial fatty acid oxidation associated with hyperacetylation of key enzymes in the pathway. Downregulation of sirtuin 3 and deficiency of NAD +

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Li, Xiao-Xue, Jun Lu, Yan-Mei Zhao, and Bai-Qu Huang. "Function of c-Fos-like and c-Jun-like Proteins on Trichostatin A-induced G2/M Arrest in Physarum polycephalum." Acta Biochimica et Biophysica Sinica 37, no. 11 (2005): 767–72. http://dx.doi.org/10.1111/j.1745-7270.2005.00105.x.

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Abstract The homologs of transcription factors c-Fos and c-Jun have been detected in slime mold Physarum polycephalum during progression of the synchronous cell cycle. Here we demonstrated that c-Fos-like and c-Jun-like proteins participated in G2/M transition by the regulation of the level of Cyclin B1 protein in P. polycephalum. The study of antibody neutralization revealed that interruption of the functions of c-Fos-like and c-Jun-like proteins resulted in G2/M transition arrest, implicating their functional roles in cell cycle control. When G2/M transition was blocked by histone deacetylas

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Lombard, David B., Frederick W. Alt, Hwei-Ling Cheng, et al. "Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine Acetylation." Molecular and Cellular Biology 27, no. 24 (2007): 8807–14. http://dx.doi.org/10.1128/mcb.01636-07.

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ABSTRACT Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin SIRT3 have so far been limited to cell culture systems. Here, we investigate the localization and function of SIRT3 in vivo. We show that endogenous mouse SIRT3 is a soluble mitochondrial protein. To address the function and relevance of SIRT3 in the regulation of energy metabolism, we generated and phenotypically characterized SIRT3 knockout mice. SIRT3-deficient animals exhibit striking mitochondrial protein hyperacetylation, suggesting that SIRT3 is a major m

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Fu, Qi, Robert A. McKnight, Xing Yu, Laiyi Wang, Christopher W. Callaway, and Robert H. Lane. "Uteroplacental insufficiency induces site-specific changes in histone H3 covalent modifications and affects DNA-histone H3 positioning in day 0 IUGR rat liver." Physiological Genomics 20, no. 1 (2004): 108–16. http://dx.doi.org/10.1152/physiolgenomics.00175.2004.

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Uteroplacental insufficiency and subsequent intrauterine growth retardation (IUGR) increase the risk of adult onset insulin resistance and dyslipidemia in humans and rats. IUGR rats are further characterized by postnatal alterations in hepatic PPAR-γ coactivator (PGC-1) and carnitine-palmitoyl-transferase I (CPTI) expression, as well as overall hyperacetylation of histone H3. However, it is unknown whether the histone H3 hyperacetylation is site specific or relates to the changes in gene expression previously described in IUGR rats. We therefore hypothesized that uteroplacental insufficiency c

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Jarrard, David Frazier, Jin-Hee Lee, Melissa Boersma, et al. "A personalized medicine approach to identifying dysregulated epigenetic enzymes in the development of castrate-resistant prostate cancer." Journal of Clinical Oncology 35, no. 6_suppl (2017): 237. http://dx.doi.org/10.1200/jco.2017.35.6_suppl.237.

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237 Background: Recent advances in proteomic and chromatin immunoprecipitation tools have been crucial in studying cancer epigenetics but the ability to measure directly the enzyme activities of dysregulated histone-modifiers is lacking. We utilize a novel approach to identify altered histone-modifying enzymes in the progression from hormone sensitive (HS) to castrate-resistant prostate cancer (CRPC) progression. Methods: We developed, validated and utilized a high-throughput peptide microarray assay to identify altered histone lysine (de)acetylation activity in tumor lysates. Functional assay

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Xiao, Ran, Ye Sun, Jian-Hua Ding, et al. "Splicing Regulator SC35 Is Essential for Genomic Stability and Cell Proliferation during Mammalian Organogenesis." Molecular and Cellular Biology 27, no. 15 (2007): 5393–402. http://dx.doi.org/10.1128/mcb.00288-07.

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ABSTRACT The members of the SR family of splicing regulators were initially characterized for their critical roles in constitutive and regulated splicing. They are implicated in different aspects of gene expression processes, including transcription, RNA stability, mRNA transport, and translational control. While knockout studies have demonstrated their essential functions during animal development, the pathway(s) leading to a specific cellular phenotype remains poorly understood. We report here that the SR protein SC35 controls cell proliferation during pituitary gland development but is comp

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Gueller, Saskia, Martina Komor, Julian C. Desmond, et al. "Identification of Putative New Tumor Suppressor Genes in Highly Purified CD34+ Bone Marrow Cells from Patients with Myelodysplastic Syndromes." Blood 104, no. 11 (2004): 204. http://dx.doi.org/10.1182/blood.v104.11.204.204.

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Abstract Activation of transcription of DNA by demethylation and hyperacetylation is known to cause hematologic improvement in patients with myelodysplastic syndromes (MDS). In this study we discriminated genes not expressed in CD34+ cells from untreated patients with MDS but activated by in vitro demethylation (2-aza-5-deoxycytidine, Decitabine) and hyperacetylation (suberoylanilide hydroxamic acid, SAHA). Highly purified CD34+ cells from normal individuals (n=3) and patients with low (n=3) and high (n=3) risk MDS were cultured with SCF (50 ng/ml), IL-3 (10 ng/ml) and GM-CSF (10 ng/ml). The c

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Arima, Yuichiro, Yoshiko Nakagawa, Toru Takeo, et al. "Murine neonatal ketogenesis preserves mitochondrial energetics by preventing protein hyperacetylation." Nature Metabolism 3, no. 2 (2021): 196–210. http://dx.doi.org/10.1038/s42255-021-00342-6.

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Celic, Ivana, Alain Verreault, and Jef D. Boeke. "Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage." Genetics 179, no. 4 (2008): 1769–84. http://dx.doi.org/10.1534/genetics.108.088914.

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Tomczyk, Mateusz M., Kyle G. Cheung, Bo Xiang, et al. "Mitochondrial Protein Hyperacetylation in Rodents with Doxorubicin‐Induced Cardiac Dysfunction." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04617.

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Bartling, Toni R., and Mitchell L. Drumm. "Oxidative Stress CausesIL8Promoter Hyperacetylation in Cystic Fibrosis Airway Cell Models." American Journal of Respiratory Cell and Molecular Biology 40, no. 1 (2009): 58–65. http://dx.doi.org/10.1165/rcmb.2007-0464oc.

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Mosley, Amber L., and Sabire Özcan. "Glucose Regulates Insulin Gene Transcription by Hyperacetylation of Histone H4." Journal of Biological Chemistry 278, no. 22 (2003): 19660–66. http://dx.doi.org/10.1074/jbc.m212375200.

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Perrella, Giorgio, M. Federica Consiglio, Riccardo Aiese-Cigliano, et al. "Histone hyperacetylation affects meiotic recombination and chromosome segregation in Arabidopsis." Plant Journal 62, no. 5 (2010): 796–806. http://dx.doi.org/10.1111/j.1365-313x.2010.04191.x.

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Sasaki, K., T. Ito, N. Nishino, S. Khochbin, and M. Yoshida. "Real-time imaging of histone H4 hyperacetylation in living cells." Proceedings of the National Academy of Sciences 106, no. 38 (2009): 16257–62. http://dx.doi.org/10.1073/pnas.0902150106.

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Oliva, R., D. P. Bazett-Jones, L. Locklear, and G. H. Dixon. "Histone hyperacetylation can induce unfolding of the nucleosome core particle." Nucleic Acids Research 18, no. 9 (1990): 2739–47. http://dx.doi.org/10.1093/nar/18.9.2739.

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Walley, Justin W., Zhouxin Shen, Maxwell R. McReynolds, Eric A. Schmelz, and Steven P. Briggs. "Fungal-induced protein hyperacetylation in maize identified by acetylome profiling." Proceedings of the National Academy of Sciences 115, no. 1 (2017): 210–15. http://dx.doi.org/10.1073/pnas.1717519115.

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Abstract:

Lysine acetylation is a key posttranslational modification that regulates diverse proteins involved in a range of biological processes. The role of histone acetylation in plant defense is well established, and it is known that pathogen effector proteins encoding acetyltransferases can directly acetylate host proteins to alter immunity. However, it is unclear whether endogenous plant enzymes can modulate protein acetylation during an immune response. Here, we investigate how the effector molecule HC-toxin (HCT), a histone deacetylase inhibitor produced by the fungal pathogen Cochliobolus carbon

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McLendon, Patrick M., Bradley S. Ferguson, Hanna Osinska, et al. "Tubulin hyperacetylation is adaptive in cardiac proteotoxicity by promoting autophagy." Proceedings of the National Academy of Sciences 111, no. 48 (2014): E5178—E5186. http://dx.doi.org/10.1073/pnas.1415589111.

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