Histone H3 acetylation is a conduit of gene expression perturbations in photodamaged skin

2018 ◽  
Vol 179 (1) ◽  
pp. 10-11
Author(s):  
D. A. Gunn
Keyword(s):  
Gene Expression ◽  
Histone H3 ◽  
Photodamaged Skin ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals Effects of Antipsychotic Drugs on the Epigenetic Modification of Brain-Derived Neurotrophic Factor Gene Expression in the Hippocampi of Chronic Restraint Stress Rats

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Mi Kyoung Seo ◽  
Young Hoon Kim ◽  
Roger S. McIntyre ◽  
Rodrigo B. Mansur ◽  
Yena Lee ◽  
...  
Keyword(s):  
Gene Expression ◽  
Restraint Stress ◽  
Antipsychotic Drugs ◽  
Epigenetic Modification ◽  
Histone H3 ◽  
Mrna Levels ◽  
Chronic Restraint Stress ◽  
Bdnf Gene ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Recent studies have shown that antipsychotic drugs have epigenetic effects. However, the effects of antipsychotic drugs on histone modification remain unclear. Therefore, we investigated the effects of antipsychotic drugs on the epigenetic modification of the BDNF gene in the rat hippocampus. Rats were subjected to chronic restraint stress (6 h/d for 21 d) and then were administered with either olanzapine (2 mg/kg) or haloperidol (1 mg/kg). The levels of histone H3 acetylation and MeCP2 binding at BDNF promoter IV were assessed with chromatin immunoprecipitation assays. The mRNA levels of total BDNF with exon IV, HDAC5, DNMT1, and DNMT3a were assessed with a quantitative RT-PCR procedure. Chronic restraint stress resulted in the downregulation of total and exon IV BDNF mRNA levels and a decrease in histone H3 acetylation and an increase in MeCP2 binding at BDNF promoter IV. Furthermore, there were robust increases in the expression of HDAC5 and DNMTs. Olanzapine administration largely prevented these changes. The administration of haloperidol had no effect. These findings suggest that the antipsychotic drug olanzapine induced histone modification of BDNF gene expression in the hippocampus and that these epigenetic alterations may represent one of the mechanisms underlying the actions of antipsychotic drugs.

scholarly journals Drosophila Ada2b Is Required for Viability and Normal Histone H3 Acetylation

2004 ◽  
Vol 24 (18) ◽  
pp. 8080-8089 ◽  
Author(s):  
Dai Qi ◽  
Jan Larsson ◽  
Mattias Mannervik
Keyword(s):  
Gene Expression ◽  
Transcriptional Activation ◽  
Protein Complexes ◽  
P53 Protein ◽  
Polytene Chromosomes ◽  
Histone H3 ◽  
Saga Complex ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

ABSTRACT Regulation of chromatin through histone acetylation is an important step in gene expression. The Gcn5 histone acetyltransferase is part of protein complexes, e.g., the SAGA complex, that interact with transcriptional activators, targeting the enzyme to specific promoters and assisting in recruitment of the basal RNA polymerase transcription machinery. The Ada2 protein directly binds to Gcn5 and stimulates its catalytic activity. Drosophila contains two Ada2 proteins, Drosophila Ada2a (dAda2a) and dAda2b. We have generated flies that lack dAda2b, which is part of a Drosophila SAGA-like complex. dAda2b is required for viability in Drosophila, and its deletion causes a reduction in histone H3 acetylation. A global hypoacetylation of chromatin was detected on polytene chromosomes in dAda2b mutants. This indicates that the dGcn5-dAda2b complex could have functions in addition to assisting in transcriptional activation through gene-specific acetylation. Although the Drosophila p53 protein was previously shown to interact with the SAGA-like complex in vitro, we find that p53 induction of reaper gene expression occurs normally in dAda2b mutants. Moreover, dAda2b mutant animals show excessive p53-dependent apoptosis in response to gamma radiation. Based on this result, we speculate that dAda2b may be necessary for efficient DNA repair or generation of a DNA damage signal. This could be an evolutionarily conserved function, since a yeast ada2 mutant is also sensitive to a genotoxic agent.

scholarly journals Ethylene induces combinatorial effects of histone H3 acetylation in gene expression in Arabidopsis

BMC Genomics ◽  
2017 ◽  
Vol 18 (1) ◽  
Author(s):  
Likai Wang ◽  
Fan Zhang ◽  
Siddharth Rode ◽  
Kevin K. Chin ◽  
Eun Esther Ko ◽  
...  
Keyword(s):  
Gene Expression ◽  
Histone H3 ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals Reduced Histone H3 Acetylation in CD4+T Lymphocytes: Potential Mechanism of Latent Autoimmune Diabetes in Adults

2015 ◽  
Vol 2015 ◽  
pp. 1-7 ◽  
Author(s):  
Xi-yu Liu ◽  
Jiang-feng Xu
Keyword(s):  
Gene Expression ◽  
T Lymphocytes ◽  
Histone Deacetylases ◽  
Autoimmune Diabetes ◽  
Histone H3 ◽  
Histone Acetyltransferases ◽  
Healthy Controls ◽  
Latent Autoimmune Diabetes ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Aims. Latent autoimmune diabetes in adults (LADA) is the result of gene-environment interactions. Histone acetylation regulates gene expression and maybe interpret how environmental factors modify LADA. Hence, we studied the histone acetylation patterns in CD4+T lymphocytes from LADA patients.Methods. Blood CD4+T lymphocytes from 28 patients with LADA and 28 healthy controls were obtained to detect histone H3 acetylation and H4 acetylation. The gene expression of histone acetyltransferases (P300 and CREBBP) and histone deacetylases (HDAC1, HDAC2, and HDAC7) was measured by real-time polymerase chain reaction (RT-PCR).Results. Compared to healthy controls, reduced global H3 acetylation was observed in LADA patients’ CD4+T lymphocytes (P<0.05). Global level of H4 acetylation was not statistically different. Among LADA, CD4+T lymphocytes H3 acetylation was associated with glycosylated hemoglobin (HbA1c) and GADA titer. Compared to healthy controls, the expression of histone acetyltransferases CREBBP in LADA patients was downregulated, and the expression of histone deacetylases HDAC1 and HDAC7 was upregulated.Conclusion. A concerted downregulation of histone H3 acetylation was found in CD4+T lymphocytes of LADA patients, and this might provide evidence of a novel epigenetic explanation for the pathogenesis of LADA and its complications.

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