OsHDA710-Mediated Histone Deacetylation Regulates Callus Formation of Rice Mature Embryo

2020 ◽  
Vol 61 (9) ◽  
pp. 1646-1660
Author(s):  
Haidao Zhang ◽  
Fu Guo ◽  
Peipei Qi ◽  
Yizi Huang ◽  
Yongyao Xie ◽  
...  
Keyword(s):  
Histone Deacetylases ◽  
Callus Formation ◽  
Trichostatin A ◽  
Expression Patterns ◽  
Histone H3 ◽  
Mature Embryo ◽  
Histone Deacetylation ◽  
Auxin Response ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Abstract Histone deacetylases (HDACs) play important roles in the regulation of eukaryotic gene expression. The role of HDACs in specialized transcriptional regulation and biological processes is poorly understood. In this study, we evaluated the global expression patterns of genes related to epigenetic modifications during callus initiation in rice. We found that the repression of HDAC activity by trichostatin A (TSA) or by OsHDA710 mutation (hda710) results in impaired callus formation of rice mature embryo and increased global histone H3 acetylation levels. The HDAC inhibition decreased auxin response and cell proliferation in callus formation. Meanwhile, the transcriptional repressors OsARF18 and OsARF22 were upregulated in the callus of hda710. The chromatin immunoprecipitation-quantitative PCR (ChIP-qPCR) analysis demonstrated that the callus of hda710 exhibited enhanced histone H3 acetylation levels at the chromatin regions of OsARF18 and OsARF22. Furthermore, we found that OsARF18 and OsARF22 were regulated through OsHDA710 recruitment to their target loci. In addition, overexpression of OsARF18 decreased the transcription of downstream genes PLT1 and PLT2 and inhibited callus formation of the mature embryo. These results demonstrate that OsHDA710 regulates callus formation by suppressing repressive OsARFs via histone deacetylation during callus formation of rice mature embryo. This indicates that OsHDA710-mediated histone deacetylation is an epigenetic regulation pathway for maintaining auxin response during cell dedifferentiation.

scholarly journals Role of Salt-Induced Kinase 1 in Androgen Neuroprotection against Cerebral Ischemia

2010 ◽  
Vol 31 (1) ◽  
pp. 339-350 ◽  
Author(s):  
Jian Cheng ◽  
Masayoshi Uchida ◽  
Wenri Zhang ◽  
Marjorie R Grafe ◽  
Paco S Herson ◽  
...  
Keyword(s):  
Cerebral Ischemia ◽  
Cortical Neurons ◽  
Trichostatin A ◽  
Histone H3 ◽  
Glucose Deprivation ◽  
Artery Occlusion ◽  
Histone Deacetylation ◽  
Small Interference Rna ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Androgens within physiological ranges protect castrated male mice from cerebral ischemic injury. Yet, underlying mechanisms are unclear. Here, we report that, after middle cerebral artery occlusion (MCAO), salt-induced kinase 1 (SIK1) was induced by a potent androgen—dihydrotestosterone (DHT) at protective doses. To investigate whether SIK1 contributes to DHT neuroprotection after cerebral ischemia, we constructed lentivirus-expressing small interference RNA (siRNA) against SIK1. The SIK1 knockdown by siRNA exacerbated oxygen–glucose deprivation (OGD)-induced cell death in primary cortical neurons, suggesting that SIK1 is an endogenous neuroprotective gene against cerebral ischemia. Furthermore, lentivirus-mediated SIK1 knockdown increased both cortical and striatal infarct sizes in castrated mice treated with a protective dose of DHT. Earlier studies show that SIK1 inhibits histone deacetylase (HDAC) activities by acting as a class IIa HDAC kinase. We observed that SIK1 knockdown decreased histone H3 acetylation in primary neurons. The SIK1 siRNA also exacerbated OGD-induced neuronal death in the presence of trichostatin A (TSA), an HDAC inhibitor, and decreased histone H3 acetylation at 4 hours reoxygenation in TSA-treated neurons. Finally, we showed that DHT at protective doses prevented ischemia-induced histone deacetylation after MCAO. Our finding suggests that SIK1 contributes to neuroprotection by androgens within physiological ranges by inhibiting histone deacetylation.

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.

Inhibition of Histone Deacetylation by MS-275 Alleviates Colitis by Activating the Vitamin D Receptor

2020 ◽  
Vol 14 (8) ◽  
pp. 1103-1118
Author(s):  
Chunxiao Li ◽  
Yi Chen ◽  
Huatuo Zhu ◽  
Xiuming Zhang ◽  
Lu Han ◽  
...  
Keyword(s):  
Vitamin D ◽  
Disease Severity ◽  
Vitamin D Receptor ◽  
Histone H3 ◽  
Histone Deacetylation ◽  
Epithelial Barrier ◽  
Deficient Diet ◽  
Negatively Associated ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Abstract Background Ulcerative colitis [UC] is a common chronic inflammatory bowel disease without curative treatment. Methods We conducted gene set enrichment analysis to explore potential therapeutic agents for UC. Human colon tissue samples were collected to test H3 acetylation in UC. Both in vivo and in vitro colitis models were constructed to verify the role and mechanism of H3 acetylation modification in UC. Intestine-specific vitamin D receptor [VDR]-/- mice and VD [vitamin D]-deficient diet-fed mice were used to explore downstream molecular mechanisms accordingly. Results According to the Connectivity Map database, MS-275 [class I histone deacetylase inhibitor] was the top-ranked agent, indicating the potential importance of histone acetylation in the pathogenesis of UC. We then found that histone H3 acetylation was significantly lower in the colon epithelium of UC patients and negatively associated with disease severity. MS-275 treatment inhibited histone H3 deacetylation, subsequently attenuating nuclear factor kappa B [NF-κB]-induced inflammation, reducing cellular apoptosis, maintaining epithelial barrier function, and thereby reducing colitis activity in a mouse model of colitis. We also identified VDR as be a downstream effector of MS-275. The curative effect of MS-275 on colitis was abolished in VDR-/- mice and in VD-deficient diet-fed mice and VDR directly targeted p65. In UC patients, histone H3 acetylation, VDR and zonulin-1 expression showed similar downregulation patterns and were negatively associated with disease severity. Conclusions We demonstrate that MS-275 inhibits histone deacetylation and alleviates colitis by ameliorating inflammation, reducing apoptosis, and maintaining intestinal epithelial barrier via VDR, providing new strategies for UC treatment.

scholarly journals Histone Acetyltransferases (HATs) in Chinese Cabbage: Insights from Histone H3 Acetylation and Expression Profiling of HATs in Response to Abiotic Stresses

2018 ◽  
Vol 143 (4) ◽  
pp. 296-303
Author(s):  
Seung Hee Eom ◽  
Tae Kyung Hyun
Keyword(s):  
Chinese Cabbage ◽  
Abiotic Stresses ◽  
Higher Plants ◽  
Expression Patterns ◽  
Histone H3 ◽  
Genomic Analysis ◽  
Environmental Stresses ◽  
Comparative Genomic ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

Histone acetyltransferase (HAT) is known as an epigenetic enzyme that acetylates specific lysine residues on the histone tail to promote chromatin dynamics and gene expression. In higher plants, HATs have been recognized as playing a fundamental role in plant development, growth, and the response to diverse environmental stresses. In this study, using comprehensive bioinformatic analyses, we identified 15 HATs in genome of chinese cabbage [Brassica rapa (BraHATs)], which are divided into four families. In addition, evolution analysis suggested that the BraHAT genes were duplicated mainly via a segmental duplication event originating 3.05–18.39 million years ago. To determine the effects of abiotic stresses, such as salt, wounding, and drought, on histone H3 acetylation in chinese cabbage, histone H3 acetylation was analyzed via immunoblot analysis, suggesting that the acetylation level of histone H3 increased in response to wounding and salt stresses. Furthermore, the analysis of BraHAT expression patterns using quantitative real-time polymerase chain reaction (qRT-PCR) suggested that the increased acetylation of histone H3 was related to BraHAT transcripts and/or the functional interplay between HAT and histone deacetylase (HDAC) activities. Taken together, our comparative genomic analysis of HAT genes in this important vegetable crop will provide a solid foundation to further our understanding of epigenetically regulated processes in response to environmental stresses.

α2-Adrenoceptor agonist dexmedetomidine protects septic acute kidney injury through increasing BMP-7 and inhibiting HDAC2 and HDAC5

2012 ◽  
Vol 303 (10) ◽  
pp. F1443-F1453 ◽  
Author(s):  
Chung-Hsi Hsing ◽  
Chiou-Feng Lin ◽  
Edmund So ◽  
Ding-Ping Sun ◽  
Tai-Chi Chen ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Histone Deacetylases ◽  
Trichostatin A ◽  
Histone H3 ◽  
Cecal Ligation ◽  
Kidney Injury ◽  
Protective Effects ◽  
Tnf Α

Bone morphogenetic protein (BMP)-7 protects sepsis-induced acute kidney injury (AKI). Dexmedetomidine (DEX), an α2-adrenoceptor (α2-AR) agonist, has anti-inflammatory effects. We investigated the protective effects of DEX on sepsis-induced AKI and the expression of BMP-7 and histone deacetylases (HDACs). In vitro , the effects of DEX or trichostatin A (TSA, an HDAC inhibitor) on TNF-α, monocyte chemotactic protein (MCP-1), BMP-7, and HDAC mRNA expression in LPS-stimulated rat renal tubular epithelial NRK52E cells, was determined using real-time PCR. In vivo, mice were intraperitoneally injected with DEX (25 μg/kg) or saline immediately and 12 h after cecal ligation and puncture (CLP) surgery. Twenty-four hours after CLP, we examined kidney injury and renal TNF-α, MCP-1, BMP-7, and HDAC expression. Survival was monitored for 120 h. LPS increased HDAC2, HDAC5, TNF-α, and MCP-1 expression, but decreased BMP-7 expression in NRK52E cells. DEX treatment decreased the HDAC2, HDAC5, TNF-α, and MCP-1 expression, but increased BMP-7 and acetyl histone H3 expression, whose effects were blocked by yohimbine, an α2-AR antagonist. With DEX treatment, the LPS-induced TNF-α expression and cell death were attenuated in scRNAi-NRK52E but not BMP-7 RNAi-NRK52E cells. In CLP mice, DEX treatment increased survival and attenuated AKI. The expression of HDAC2, HDAC5, TNF-α, and MCP-1 mRNA in the kidneys of CLP mice was increased, but BMP-7 was decreased. However, DEX treatment reduced those changes. DEX reduces sepsis-induced AKI by decreasing TNF-α and MCP-1 and increasing BMP-7, which is associated with decreasing HDAC2 and HDAC5, as well as increasing acetyl histone H3.

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