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2023-11-02 12:58:31 | onclick: | Rapid activation of NLRP3 inflammatory corpuscle regulates neutrophil release

E-selectin-mediated rapid activation of NLRP3 inflammatory bodies regulates neutrophil release of S100A8/S100A9 through transient gasdermin protein D pore formation, according to Markus Sperandio team of the German Institute of Cardiovascular Physiology and Pathophysiology.The findings were published in Nature-Immunology, October 30, 2023.
They found that rapid release of E-selectin-induced S100A8/S100A9 occurred in the manner of NLRP3 inflammatory corpuscle dependence during inflammation.Mechanically, the involvement of E-selectin triggers Bruton tyrosine kinase-dependent phosphorylation of NLRP3 tyrosine.ASC oligomerization was mediated by voltage-gated potassium channel KV1.3.Subsequently, caspase 1 cleavage and downstream activation of gasdermin protein D resulted in the release of S100A8/S100A9 in the cytoplasm.
Remarkably, E-selectin-mediated gasdermin D-hole formation does not lead to cell death, but is a brief process involving activation of ESCRT III membrane repair mechanisms.These data elucidate the molecular mechanism of controlled release of S100A8/S100A9 from neutrophils and determine that NLRP3/gasdermin D axis is a rapidly reversible activation system of neutrophils during inflammation.
It is understood that S100A8/S100A9 is a proinflammatory medium released by bone marrow cells in many acute and chronic inflammatory diseases.However, the exact mechanism of its release from the neutrophil cytoplasmic chamber is unclear.

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