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Inflammasomes are multiprotein complexes involved in the activation of caspase-1 and the processing of the pro-inflammatory cytokines, interleukin-1 beta (IL-1 beta) and IL-18. The basic components of inflammasomes are a protease, caspase-1, the adaptor protein apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), and a sensor molecule, e.g. a NOD-like receptor (NLR) such NLRP1, -2 or -3, AIM2 or pyrin. Inflammasomes are activated by Damage-Associated Molecular Patterns (DAMPs) such as ATP, fatty acids, DNA or Pathogen-Associated Molecular Patterns (PAMPs) as Bacillus anthracis or flagellin. However, some inflammasomes respond to more than one type of inflammasome inducer, e.g. the NLRP2 inflammasome is assembled in response to reactive oxygen species (ROS) or ATP. In addition, Pannexin 1 (Panx1) and the purinergic receptor P2X7 signaling pathways are involved in inflammasome regulation. Following activation, inflammasomes oligomerize to produce massive cytokine signaling platforms termed ASC specks. ASC specks induce maturation of IL-1 beta and IL-18 through proteolytic cleavage of pro-IL-1 beta and pro-IL-18 resulting in an inflammatory cell death process termed pyroptosis. ASC specks are released into the extracellular space or into tissue fluids and process pro-IL-1 beta into active IL-1 beta causing excessive inflammation leading to cellular and tissue damage.
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