---
res:
  bibo_abstract:
  - 'Some inflammatory stimuli trigger activation of the NLRP3 inflammasome by inducing
    efflux of cellular potassium. Loss of cellular potassium is known to potently
    suppress protein synthesis, leading us to test whether the inhibition of protein
    synthesis itself serves as an activating signal for the NLRP3 inflammasome. Murine
    bone marrow-derived macrophages, either primed by LPS or unprimed, were exposed
    to a panel of inhibitors of ribosomal function: ricin, cycloheximide, puromycin,
    pactamycin, and anisomycin. Macrophages were also exposed to nigericin, ATP, monosodium
    urate (MSU), and poly I:C. Synthesis of pro-IL-ß and release of IL-1ß from cells
    in response to these agents was detected by immunoblotting and ELISA. Release
    of intracellular potassium was measured by mass spectrometry. Inhibition of translation
    by each of the tested translation inhibitors led to processing of IL-1ß, which
    was released from cells. Processing and release of IL-1ß was reduced or absent
    from cells deficient in NLRP3, ASC, or caspase-1, demonstrating the role of the
    NLRP3 inflammasome. Despite the inability of these inhibitors to trigger efflux
    of intracellular potassium, the addition of high extracellular potassium suppressed
    activation of the NLRP3 inflammasome. MSU and double-stranded RNA, which are known
    to activate the NLRP3 inflammasome, also substantially inhibited protein translation,
    supporting a close association between inhibition of translation and inflammasome
    activation. These data demonstrate that translational inhibition itself constitutes
    a heretofore-unrecognized mechanism underlying IL-1ß dependent inflammatory signaling
    and that other physical, chemical, or pathogen-associated agents that impair translation
    may lead to IL-1ß-dependent inflammation through activation of the NLRP3 inflammasome.
    For agents that inhibit translation through decreased cellular potassium, the
    application of high extracellular potassium restores protein translation and suppresses
    activation of the NLRP inflammasome. For agents that inhibit translation through
    mechanisms that do not involve loss of potassium, high extracellular potassium
    suppresses IL-1ß processing through a mechanism that remains undefined.@eng'
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Meghan
      foaf_name: Vyleta, Meghan
      foaf_surname: Vyleta
      foaf_workInfoHomepage: http://www.librecat.org/personId=418901AA-F248-11E8-B48F-1D18A9856A87
  - foaf_Person:
      foaf_givenName: John
      foaf_name: Wong, John
      foaf_surname: Wong
  - foaf_Person:
      foaf_givenName: Bruce
      foaf_name: Magun, Bruce
      foaf_surname: Magun
  bibo_doi: 10.1371/journal.pone.0036044
  bibo_issue: '5'
  bibo_volume: 7
  dct_date: 2012^xs_gYear
  dct_identifier:
  - UT:000305339400011
  dct_language: eng
  dct_publisher: Public Library of Science@
  dct_title: Suppression of ribosomal function triggers innate immune signaling through
    activation of the NLRP3 inflammasome@
...