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Systemic Lupus Erythematosus
Published in Jason Liebowitz, Philip Seo, David Hellmann, Michael Zeide, Clinical Innovation in Rheumatology, 2023
Vaneet K. Sandhu, Neha V. Chiruvolu, Daniel J. Wallace
Available evidence on histone acetylation has so far demonstrated that H3 and H4 acetylation in CD4+ T cells negatively correlates with disease activity. Acetylation of TNF has been associated with increased gene transcription. Similarly, a study with microarrays looking for H4 acetylation identified several genes that were highly acetylated and overexpressed. However, there is still a paucity of studies in this area, and the relationship between acetylation and gene expression remains unclear.50
Naturally Occurring Histone Deacetylase (HDAC) Inhibitors in the Treatment of Cancers
Published in Namrita Lall, Medicinal Plants for Cosmetics, Health and Diseases, 2022
Sujatha Puttalingaiah, Murthy V. Greeshma, Mahadevaswamy G. Kuruburu, Venugopal R. Bovilla, SubbaRao V. Madhunapantula
Since histones play an important role in the compactness of DNA, modifying these proteins through acetylation in turn modulates the expression of genes (Dong and Weng, 2013). Acetylation of histone proteins facilitates and enhances the gene transcription, whereas deacetylation suppresses the transcription by enhancing the compact packing of DNA (Park and Kim, 2020). Acetylation of histones is carried out by histone acetyltransferase (HAT), while deacetylation is performed by histone deacetylase (HDACs) enzymes (Legube and Trouche, 2003).
Food Interactions, Sirtuins, Genes, Homeostasis, and General Discussion
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
The sirtuins are a family of proteins (enzymes) that act predominantly as nicotinamide adenine dinucleotide (NAD)-dependent deacetylases, which require nicotinamide adenine dinucleotide (NAD+) as an essential co-factor (63, 66–70). Acetylation and deacetylation are two important biochemical reactions to regulate the activity of proteins. All sirtuins require the coenzyme nicotinamide adenine dinucleotide (NAD+) for their deacetylase or ADP-ribosyl transferase activity, linking their function tightly to cellular energy levels (66–70).
High levels of HDAC expression correlate with microglial aging
Published in Expert Opinion on Therapeutic Targets, 2022
Jaione Auzmendi-Iriarte, Leire Moreno-Cugnon, Ander Saenz-Antoñanzas, Daniela Grassi, Marian M de Pancorbo, Maria-Angeles Arevalo, Ian C Wood, Ander Matheu
Histone modification through acetylation of lysine residues is the primary epigenetic modification that promotes conversion into a more relaxed chromatin state and transcriptional activation [20]. Acetylation is controlled by two antagonistic enzyme families, histone acetyltransferases (HAT) and histone deacetylases (HDAC). HDACs catalyze the removal of acetyl groups from histone tails and provoke a compact chromatin status, whereas HATs have the opposite effect. Thus far, 18 human HDACs have been identified and categorized into four classes depending on their sequence similarity with yeast HDACs. Class I, II, and IV HDACs, also known as classical HDACs, depend on Zn2+ ions located in their catalytic pocket, whereas class III HDACs, known as sirtuins (SIRTs), are nicotinamide adenine dinucleotide (NAD+)-dependent enzymes [21].
Upregulation of OATP1A2 in human oesophageal squamous cell carcinoma cells via the HDAC6-GCN5/PCAF-H3K9Ac axis
Published in Xenobiotica, 2021
Xiaoli Zheng, Jian V. Zhang, Yanfeng Bai, Jiaqi Wang, Mingfeng Jiang, Su Zeng, Lvhua Wang
In cancer, epigenetic modifications are accomplished by DNA methylation, histone modifications and noncoding RNAs without changes in the DNA sequence. Alterations in epigenetic markers contribute to the inactivation of cellular factors that are involved in carcinogenesis (Liu et al. 2016; Buccarelli et al. 2020; Guerra et al. 2020). Histone acetylation is a dynamic epigenetic mediator that drives and maintains the malignant phenotype (Albrengues et al. 2015; Chen et al. 2019). Histone acetylation is mediated via histone acetyltransferases (HATs) and suppressed by histone deacetylases (HDACs). HATs such as p300/CBP, Tip60, MOZ/MORF, and GCN5/PCAF act as recruiters of acetyl groups during their interactions with HDAC complexes (Caslini et al. 2019; Wang et al. 2019). The study of epigenetic mechanism suggested that the expression of OATP1A2 was upregulated by the enrichment of H3K9Ac at promoter region of OATP1A2 in ESCC. In ESCC tumour tissues, loss of HDAC6 and enrichment of GCN5/PCAF induced H3K9Ac at the promoter region of OATP1A2. Therefore, the suppression of OATP1A2 by blocking upstream HDAC6-GCN5/PCAF-H3K9AC pathway may improve overall survival of patients with ESCC.
Neuroprotective Effect of Brazilian Green Propolis on Retinal Ganglion Cells in Ischemic Mouse Retina
Published in Current Eye Research, 2020
Jung Won Park, Mi Sun Sung, Jun Young Ha, Yue Guo, Helong Piao, Hwan Heo, Sang Woo Park
Emerging evidence has indicated that increased retinal HDAC activity contributes to retinal injury by retinal ischemia, chronic ocular hypertension, and optic nerve damage.31,52 The equilibrium between the activity of histone acetyltransferases (HATs) and HDACs is finely regulated in neurons under normal conditions. The impairment of acetylation homeostasis, shifting toward deacetylation, is a frequent molecular change in neurodegenerative diseases.53 The inhibition of HDACs, for example, through the application of valproic acid or trichostatin A, was reported to be neuroprotective in RGCs in animal models of optic nerve crushing, retina ischemia, and chronic ocular hypertension.31,52,54–57 Previously, Ishiai et al.58 reported a neuroprotective effect of BGP on Neuro 2a cells, which acts through the inhibition of histone deacetylation. In our study, BGP can effectively reduce RGC loss under oxidative stress in vivo by increasing the level of histone acetylation in the mouse retina.