20 research outputs found

    Mechanism of immune escape by mycobacteria via TREM2 in mice.

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    TREM2 inhibits the Mincle-FcRγ-CARD9 pathway and reduces iNOS to kill bacteria. On the other hand, TREM2 promotes the synthesis and release of monocyte chemotactic protein (MCP)-1 to recruit permissive macrophages to enhance infectivity [42]. The illustration rendering portion of this work was supported by Figdraw (https://www.figdraw.com/). TREM2, triggering receptor expressed on myeloid cells 2; CARD9, caspase-recruitment domain family member 9; SYK, splenic tyrosine kinase; DAP12, DNAX activation protein 12; BCL10, B cell lymphoma 10; iNOS, inducible nitric oxide synthase; MALT1, mucosa-associated lymphoid tissue translocation protein 1.</p

    The role of TREM2 in bacterial infection.

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    (A) TREM2 binds to lipid components on bacteria via the hydrophobic and cationic regions of extracellular fragments and progressively activates SYK, PI3K, and GTPases via the ITAM motif of DAP12. GTPases rearrange of actin-rich formation near the bacteria, allowing the bacteria to be internalized by the surrounding membrane [41,53]. (B) TREM2 inhibits NLRP3 inflammasome transcription and assembly by stabilizing β-catenin and reducing mitochondrial ROS release, which in turn inhibits cell pyroptosis and IL-1β release. In addition, AKT and PKC downstream of TREM2 can stimulate NADPH oxidase complex on phagosomes to release ROS, promoting bacterial killing [46,48,50]. The illustration rendering portion of this work was supported by Figdraw (https://www.figdraw.com/). TREM2, triggering receptor expressed on myeloid cells 2; SYK, splenic tyrosine kinase; PI3K, phosphoinositide 3-kinase; ITAM, immunoreceptor tyrosine activator motif; DAP12, DNAX activation protein 12; NLRP3, NACHT, LRR, and PYD domains-containing protein 3; ROS, reactive oxygen species; IL, interleukin; NADPH, nicotinamide adenine dinucleotide phosphate; GSMDM, gesdermin D; PIP2, phosphatidylinositol-4,5-bisphosphate; PIP3, phosphatidylinositol-3,4,5-trisphosphate; DAG, diacylglycerol; AKT, protein kinase B; PKC, protein kinase C.</p

    The antimicrobial effects of TREM2 on barrier immune cells.

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    (A) TREM2 expression in acne lesions enhances the phagocytic capacity of macrophages against lipids and bacteria, but the macrophages do not facilitate microbial bacterial clearance due to the ability of squalene to clear ROS and to inhibit ROS production [25]. (B) TREM2 inhibits C1q transcription and basal C1q production by suppressing PPAR-δ activity in AMs, and C1q was up-regulated in Trem2-/- AMs to enhance macrophage phagocytosis [45]. The illustration rendering portion of this work was supported by Figdraw (https://www.figdraw.com/). TREM2, triggering receptor expressed on myeloid cells 2; ROS, reactive oxygen species; C1q, complement 1q; PPAR-δ, peroxisome proliferator-activated receptor-δ; AMs, alveolar macrophages; DAP12, DNAX activation protein 12.</p

    The role of TREM2 in regulating bacterial phagocytosis, clearance and the release of inflammatory factors<sup>α</sup>.

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    The role of TREM2 in regulating bacterial phagocytosis, clearance and the release of inflammatory factorsα.</p

    Proton-Induced Dysfunction Mechanism of Cathodes in an Aqueous Lithium Ion Battery

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    The proton-induced dysfunction mechanism of cathodes in aqueous lithium ion batteries is investigated by combining both experimental and theoretical research. We have found the electrochemical stability of the cathodes in a Li<sup>+</sup>-containing aqueous electrolyte solution is critically dependent on the pH value of the solution. The cyclic voltammograms of the cathodes show that the cathodes become dysfunctional when the pH of the solution decreases right below a certain value. We find that the competition reactions to the cathodes of the H<sup>+</sup> and Li<sup>+</sup> in the solution dominate whether Li<sup>+</sup> or H<sup>+</sup> would be intercalated. Thermodynamic analysis proves that the critical pH, which divide the normal and dysfunctional behaviors, is determined by both the difference of the binding energies of Li<sup>+</sup> and H<sup>+</sup> cations to the cathodes and the chemical potentials of the Li<sup>+</sup> and H<sup>+</sup> in the solution
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