Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Histone Modification

Histone Modification

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...

Spreading of Chromatin Modifications

Spreading of Chromatin Modifications

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...

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Histone Variants at the Centromere

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A cyclic peptide toolkit reveals mechanistic principles of peptidylarginine deiminase IV regulation.

Nature communications·2024

Same author

Anti-inflammatory therapy with nebulized dornase alfa for severe COVID-19 pneumonia: a randomized unblinded trial.

eLife·2024

Same author

Microbe capture by splenic macrophages triggers sepsis via T cell-death-dependent neutrophil lifespan shortening.

Nature communications·2022

Same author

Actin powers the neutrophil traps.

Blood·2022

Search research articles

Related Experiment Video

Updated: Jul 19, 2025

Isolation, Processing and Analysis of Murine Gingival Cells

Isolation, Processing and Analysis of Murine Gingival Cells

Published on: July 2, 2013

NET histones inflame periodontitis.

Venizelos Papayannopoulos¹

¹Antimicrobial Defence Laboratory, The Francis Crick Institute , London, UK.

The Journal of Experimental Medicine

|August 8, 2023

Summary

This summary is machine-generated.

Microbial dysbiosis causes periodontitis. Neutrophil extracellular trap histones drive Th17 inflammation, leading to gum and bone loss in this inflammatory disease.

More Related Videos

Inducing Apical Periodontitis in Mice

Inducing Apical Periodontitis in Mice

Published on: August 6, 2019

Robust Ligature-Induced Model of Murine Periodontitis for the Evaluation of Oral Neutrophils

Robust Ligature-Induced Model of Murine Periodontitis for the Evaluation of Oral Neutrophils

Published on: January 21, 2020

Related Experiment Videos

Last Updated: Jul 19, 2025

Isolation, Processing and Analysis of Murine Gingival Cells

Isolation, Processing and Analysis of Murine Gingival Cells

Published on: July 2, 2013

Inducing Apical Periodontitis in Mice

Inducing Apical Periodontitis in Mice

Published on: August 6, 2019

Robust Ligature-Induced Model of Murine Periodontitis for the Evaluation of Oral Neutrophils

Robust Ligature-Induced Model of Murine Periodontitis for the Evaluation of Oral Neutrophils

Published on: January 21, 2020

Area of Science:

Immunology
Microbiology
Periodontology

Background:

Microbial dysbiosis is a known trigger for inflammatory periodontitis.
Periodontitis is characterized by gum and bone loss.
The specific mediators driving pathogenic inflammation require further elucidation.

Purpose of the Study:

To identify the key mediators responsible for Th17 inflammation in periodontitis.
To understand the role of neutrophil extracellular traps in periodontitis pathogenesis.

Main Methods:

The study investigated the role of neutrophil extracellular trap (NET) components in periodontitis.
Experimental models were used to assess the impact of NET histones on Th17 cell responses.

Main Results:

Neutrophil extracellular trap histones were identified as major mediators of pathogenic Th17 inflammation.
These histones directly fuel the inflammatory processes contributing to gum and bone loss.

Conclusions:

Neutrophil extracellular trap histones are critical drivers of Th17-mediated inflammation in periodontitis.
Targeting NET histones may offer a therapeutic strategy for managing periodontitis.