Dec 3, 2014

Activation of NLRP3 inflammasome by crystalline structures via cell surface contact

Scientific Reports
Aswin HariYan Shi


Crystalline structures activate the NLRP3 inflammasome, leading to the production of IL-1β, however, the molecular interactions responsible for NLRP3 activation are not fully understood. Cathepsin B release from the ruptured phagolysosome and potassium ion efflux have been suggested to be critical for this activation. Here, we report that Cathepsin B redistribution was not a crucial event in crystal-induced IL-1β production. Silica and monosodium urate crystal-treated macrophages with undisturbed lysosomes demonstrated strong co-localization of ASC and Caspase-1, indicative of NLRP3 inflammasome activation. Importantly, we provided evidence to suggest that macrophage cell membrane binding to immobilized crystals was sufficient to induce IL-1β release, and this activation of the NLRP3 inflammasome was inhibited by blocking potassium efflux. Therefore, this work reveals additional complexity in crystalline structure-mediated NLRP3 inflammasome regulations.

  • References49
  • Citations40

Mentioned in this Paper

Establishment and Maintenance of Localization
Crystal - Body Material
Interleukin-1 Production
CASP1 gene
CTSB gene
Cathepsins B
NLRP3 gene
Cell Surface

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