IndraLab
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Nitric oxide inhibits NLRP3. 86 / 86
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86
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"For example, infection of macrophages with B. abortus that are deficient in NO production, which is known to inhibit NLRP3, resulted in higher secretion of IL-1β, but no differences in bacterial load were observed, indicating that B. abortus employs additional mechanisms to ensure survival in macrophages (165)."
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"Altogether, mitophagy is accomplished by SESN2- and ULK1 mediated selective autophagy of perinuclearly clustered mitochondria primed by SESN2-SQSTM1, leading to the suppression of prolonged inflammasome activation.suggesting that perinuclear clustering of damaged mitochondria may not always be required for mitophagy induction in BMDMs in response to LPS and ATP.It has been reported that NOS2 generated NO can suppress the activation of the NLRP3 inflammasome by maintaining mitochondrial homeostasis in macrophages,35 though the mechanism by which NO regulates mitochondrial homeostasis has not been reported."
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"Since the deleterious effects of LPS are associated with the secretion of TNF-α, and NO predominantly by tissue macrophages, significantly lower level of both TNF-α and NO induced by L-LPS in our study further confirms its lower endotoxicity than E-LPS.Leptospira can activate NLRP3 inflammasome in mouse macrophages via signalling through its LPS, lipoproteins and glycoproteins [47]."
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"Interestingly, another small molecule, nitric oxide (NO), attenuates NLRP3 inflammasome activity at the post-translational level by direct S-nitrosylation158.In addition to post-translational and post-transcriptional regulation, a number of molecules can directly or indirectly interact with different components of the NLRP3 inflammasome, through which they impede the assembly of NLRP3 with ASC and caspase-1."
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"Interestingly, another small molecule, nitric oxide (NO), attenuates NLRP3 inflammasome activity at the post-translational level by direct S-nitrosylation158.In addition to post-translational and post-transcriptional regulation, a number of molecules can directly or indirectly interact with different components of the NLRP3 inflammasome, through which they impede the assembly of NLRP3 with ASC and caspase-1."
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"In this study, we found that NO not only inhibits NLRP3 inflammasome mediated IL-1beta secretion and caspase-1 activation, but also inhibits NLRC4- and AIM-2-mediated IL-1beta secretion and caspase-1 activation (XREF_SUPPLEMENTARY), but to a much less extent (3-fold decrease for NLRC4 and AIM-2, 40-fold decrease for NLRP3)."