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Fig. 2 | Inflammation and Regeneration

Fig. 2

From: Amyloid β directly interacts with NLRP3 to initiate inflammasome activation: identification of an intrinsic NLRP3 ligand in a cell-free system

Fig. 2

Direct interaction between Aβ and NLRP3 induced the initial event of NLRP3 inflammasome activation. a Schematic representations of NLRP3 and ASC. Synthetic C-terminal biotinylated full-length NLRP3 (NLRP3-FL-Btn), N-terminal FLAG-tagged ASC (FLAG-ASC-FL), and N-terminal FLAG-tagged ASC-CARD (FLAG-ASC-CARD) are indicated. The pyrin domain (PYD) is indicated by black boxes. The caspase recruitment domain (CARD) is indicated by a dark gray box. The nucleotide-binding oligomerization domain (NOD) is indicated by a light gray box. Leucine-rich repeats are indicated by a striped box. Amino acid sequence numbers are indicated under each schematic. b Interaction between NLRP3-FL-Btn and each form of Aβ with indicated concentrations is presented. c Interaction between NLRP3-FL-Btn and Aβ fibrils with indicated concentrations is presented. d Interaction between NLRP3-FL-Btn and FLAG-ASC-FL upon incubation with each form of Aβ with indicated concentrations. Interactions between NLRP3-FL-Btn and FLAG-ASC-FL upon incubation with poly(I:C) were positive controls. Interaction between NLRP3-FL-Btn and FLAG-ASC-CARD was the negative control. Interaction was detected by an amplified luminescent proximity homogeneous assay (ALPHA). Results are given as means ± standard deviation of triplicate data acquisition. *p value < 0.05 was considered significant

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Inflammation and Regeneration

ISSN: 1880-8190

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