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Related Concept Videos

Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Chromatin Modification in iPS Cells01:32

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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Spreading of Chromatin Modifications02:25

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
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Histone deacetylase 3 regulates microglial function through histone deacetylation.

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Epigenetics
|July 28, 2023
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Summary

Inhibiting histone deacetylase 3 (Hdac3) in microglia boosts histone acetylation, enhancing their ability to clear debris and reduce neuroinflammation. This offers new therapeutic insights for brain injury and disease.

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Hdac3Microglia cellschromatingene expressionneuroinflammation

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Area of Science:

  • Neuroimmunology
  • Epigenetics
  • Molecular Biology

Background:

  • Microglia are key innate immune cells in the brain, releasing inflammatory molecules in response to damage.
  • Histone acetylation regulates inflammatory gene expression, and Hdac3 inhibition shows therapeutic potential in neurological conditions.
  • The precise mechanisms of Hdac3 in microglial inflammatory gene regulation remain unclear.

Purpose of the Study:

  • To investigate how Hdac3 inhibition affects histone acetylation and inflammatory gene expression in microglia.
  • To elucidate the molecular mechanisms of Hdac3 in regulating microglial inflammatory responses.
  • To assess the impact of Hdac3 inhibition on microglial neuroprotective functions.

Main Methods:

  • Pharmacological inhibition of Hdac3 in an immortalized microglial cell line (BV2).
  • Assessment of global and promoter-specific histone acetylation using flow cytometry and CUT & RUN.
  • Analysis of pro- and anti-inflammatory gene expression following lipopolysaccharide (LPS) challenge.

Main Results:

  • Hdac3 inhibition increased global and promoter-specific histone acetylation.
  • This led to derepression of genes at baseline and enhanced inflammatory responses to LPS.
  • Hdac3 inhibition improved microglial neuroprotective functions, reducing nitric oxide and increasing phagocytosis.

Conclusions:

  • Hdac3 acts as a crucial regulator of microglial inflammatory responses.
  • Inhibiting Hdac3 enhances microglial capacity to manage inflammation and clear cellular debris.
  • These findings provide mechanistic insights into Hdac3 inhibition as a therapeutic strategy for neuroinflammation.