Induction of the apoptosis, degranulation and IL‐13 production of human basophils by butyrate and propionate via suppression of histone deacetylation

Immunology ◽  
2021 ◽  
Author(s):  
Yanbiao Shi ◽  
Meizhen Xu ◽  
Shuai Pan ◽  
Sijia Gao ◽  
Jinfeng Ren ◽  
...  
Keyword(s):  
Histone Deacetylation ◽  
Human Basophils

Dri1 mediates heterochromatin assembly via RNAi and histone deacetylation

Genetics ◽  
2021 ◽  
Author(s):  
Hyoju Ban ◽  
Wenqi Sun ◽  
Yu-hang Chen ◽  
Yong Chen ◽  
Fei Li
Keyword(s):  
Histone Deacetylases ◽  
Genome Stability ◽  
Rna Binding ◽  
Histone Deacetylation ◽  
Rnai Pathway ◽  
Chromatin Domain ◽  
Heterochromatin Protein 1 ◽  
Intrinsically Disordered ◽  
C Terminus ◽  
Heterochromatin Assembly

Abstract Heterochromatin, a transcriptionally silenced chromatin domain, is important for genome stability and gene expression. Histone 3 lysine 9 methylation (H3K9me) and histone hypoacetylation are conserved epigenetic hallmarks of heterochromatin. In fission yeast, RNA interference (RNAi) plays a key role in H3K9 methylation and heterochromatin silencing. However, how RNAi machinery and histone deacetylases (HDACs) are coordinated to ensure proper heterochromatin assembly is still unclear. Previously, we showed that Dpb4, a conserved DNA polymerase epsilon subunit, plays a key role in the recruitment of HDACs to heterochromatin during S phase. Here, we identified a novel RNA-binding protein Dri1 that interacts with Dpb4. GFP-tagged Dri1 forms distinct foci mostly in the nucleus, showing a high degree of colocalization with Swi6/Heterochromatin Protein 1. Deletion of dri1+ leads to defects in silencing, H3K9me, and heterochromatic siRNA generation. We also showed that Dri1 physically associates with heterochromatic transcripts, and is required for the recruitment of the RNA-induced transcriptional silencing (RITS) complex via interacting with the complex. Furthermore, loss of Dri1 decreases the association of the Sir2 HDAC with heterochromatin. We further demonstrated that the C-terminus of Dri1 that includes an intrinsically disordered (IDR) region and three zinc fingers is crucial for its role in silencing. Together, our evidences suggest that Dri1 facilitates heterochromatin assembly via the RNAi pathway and HDAC.

Vorinostat exhibits anticancer effects in triple-negative breast cancer cells by preventing nitric oxide-driven histone deacetylation

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Marianne B. Palczewski ◽  
Hannah Petraitis Kuschman ◽  
Rhea Bovee ◽  
Jason R. Hickok ◽  
Douglas D. Thomas
Keyword(s):  
Nitric Oxide ◽  
Histone Acetylation ◽  
Triple Negative ◽  
Soluble Guanylyl Cyclase ◽  
Prognostic Indicator ◽  
Histone Deacetylation ◽  
Breast Cancers ◽  
Cellular Iron ◽  
Lysine Residues ◽  
Pathway Interaction

Abstract Triple-negative breast cancers (TNBC) that produce nitric oxide (NO) are more aggressive, and the expression of the inducible form of nitric oxide synthase (NOS2) is a negative prognostic indicator. In these studies, we set out to investigate potential therapeutic strategies to counter the tumor-permissive properties of NO. We found that exposure to NO increased proliferation of TNBC cells and that treatment with the histone deacetylase inhibitor Vorinostat (SAHA) prevented this proliferation. When histone acetylation was measured in response to NO and/or SAHA, NO significantly decreased acetylation on histone 3 lysine 9 (H3K9ac) and SAHA increased H3K9ac. If NO and SAHA were sequentially administered to cells (in either order), an increase in acetylation was observed in all cases. Mechanistic studies suggest that the “deacetylase” activity of NO does not involve S-nitrosothiols or soluble guanylyl cyclase activation. The observed decrease in histone acetylation by NO required the interaction of NO with cellular iron pools and may be an overriding effect of NO-mediated increases in histone methylation at the same lysine residues. Our data revealed a novel pathway interaction of Vorinostat and provides new insight in therapeutic strategy for aggressive TNBCs.

scholarly journals Effects of butyrate on histone deacetylation and aldosterone-dependent Na+ transport in the toad bladder.

1983 ◽  
Vol 258 (5) ◽  
pp. 3388-3395
Author(s):  
A Truscello ◽  
K Geering ◽  
H P Gäggeler ◽  
B C Rossier
Keyword(s):  
Histone Deacetylation ◽  
Toad Bladder ◽  
Na Transport
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