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- W3206088604 abstract "Neutrophil extracellular traps (NETs) have been implicated in the pathogenesis of acute respiratory distress syndrome (ARDS) driven by viruses or bacteria, as well as in numerous immune-mediated disorders. Histone citrullination by the enzyme peptidylarginine deiminase 4 (PAD4) and the consequent decondensation of chromatin are hallmarks in the induction of NETs. Nevertheless, additional histone modifications that may govern NETosis are largely overlooked. Herein, we show that histone deacetylases (HDACs) play critical roles in driving NET formation in human and mouse neutrophils. HDACs belonging to the zinc-dependent lysine deacetylases family are necessary to deacetylate histone H3, thus allowing the activity of PAD4 and NETosis. Of note, HDAC inhibition in mice protects against microbial-induced pneumonia and septic shock, decreasing NETosis and inflammation. Collectively, our findings illustrate a new fundamental step that governs the release of NETs and points to HDAC inhibitors as therapeutic agents that may be used to protect against ARDS and sepsis." @default.
- W3206088604 created "2021-10-25" @default.
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- W3206088604 date "2021-11-01" @default.
- W3206088604 modified "2023-10-16" @default.
- W3206088604 title "Zinc-dependent histone deacetylases drive neutrophil extracellular trap formation and potentiate local and systemic inflammation" @default.
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- W3206088604 doi "https://doi.org/10.1016/j.isci.2021.103256" @default.
- W3206088604 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8567386" @default.
- W3206088604 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34761180" @default.
- W3206088604 hasPublicationYear "2021" @default.
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