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IL-1[beta]: interleukin-1[beta]; IL-18: interleukin-18; IL- 17: interleukin-17; NLRP3: NOD-like receptor pyrin domain-containing 3; ASC, apoptosis-associated speck-like protein containing a caspase recruitment domain; BBB: blood-brain barrier; GM-CSF: granulocyte-macrophage colony-stimulating factor.
ASC recruits procaspase-1 through its C-terminal caspase recruitment domain (CARD) and interacts with NLRP3 via its pyrin domain (PYD), serving as a bridge between these two molecules.
CML = [N.sup.[epsilon]] (carboxymethyl)lysine; DAMPs = damage-associated molecular patterns; eATP = extracellular ATP; ER = endoplasmic reticulum; FFAs = free fatty acids; IL-1[beta] = interleukin-1 [beta]; LDLs = low density lipoprotein; MVs = microvesicles; NADPH ox = NADPH oxidase; NF-[kappa]B = nuclear factor-[kappa]B; NLRP3 = nucleotide-binding and oligomerization domain (NOD), leucine-rich repeat and pyrin domain containing 3; PR[2X.sub.7] = purinergic receptor [2X.sub.7]; PYCARD = the PYD- CARD adaptor protein apoptosis-associated speck-like protein containing a caspase recruitment domain; RAGE = receptor for advanced glycation end products; ROS = reactive oxygen species; TLR = toll-like receptor; TNF-[alpha] = tumor necrosis factor-[alpha].
ASC (apoptosis-associated speck-like protein containing a CARD), characterized as the central structure of inflammasome, contains a pyrin domain (PYD) and a caspase recruitment domain to link pattern recognition receptors (PRRs) with procaspase 1.
After interaction with apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), the activated NLRP3 can recruit caspase-1 precursors and form a protein complex "inflammasome." Activated NLRP3 inflammasome, in the form of caspase-1 shear body (p20), cleaves the precursor of IL-1[beta] to form mature IL-1[beta].
After formation and activation, the NLRP3 inflammasome associates with the adaptor protein apoptosis speck-like protein containing a caspase recruitment domain (ASC) via its pyrin domain.
AMs were treated with LPS and adenosine triphosphate (ATP); caspase-1-dependent cell death was evaluated using flow cytometry; the apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) pyroptosomes were examined by immunofluorescence.
Danger-associated molecular patterns (DAMPs), for example, ATP, cholesterol crystals, urate crystals, and ceramide, promote formation of the inflammasome, which is a multimeric protein complex consisting of Nod-like receptor family pyrin domain containing 3 (NLRP3), apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), and procaspase1 [7-10].
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