IndraLab

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"Specifically, PGE2 suppresses the activation of the inflammasome protein NLRP3 via induction of cyclic adenosine monophosphate (cAMP), which binds to protein kinase A (PKA), resulting in NLRP3 phospho[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"IL-1 plays a crucial role in stimulating the synthesis of PGE2, which subsequently inhibits the activity of NLRP3, a member of the NLR family involved in regulating innate immune inflammatory responses by activating IL-1 and IL-28 cytokines [94]."

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"However, PGE2 can also inhibit NLRP3 activation and reduce IL-1 production under specific homeostatic conditions, and signalling mediated by PGE2 receptors can exert anti-inflammatory effects in certain situations [95, 96]."

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"Having found that exogenous PGE 2 inhibits NLRP3 inflammasome activation in human primary MDM, we wondered whether endogenous PGE 2 production might serve as a regulatory autocrine or paracrine mechanism against excessive NLRP3 activation."

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"These researchers demonstrated that NLR Family Pyrin Domain Containing 3 (NLRP3)-mediated inflammasome activation in human primary monocyte-derived macrophages was inhibited by PGE2."

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"Importantly, metabolic by-products and particularly those generated during quiescent states or during contracting and tolerogenic response phases, such as AMP, beta-hydroxybutyrate, and prostaglandin E2 (PGE2) can also function as resolution associated molecular patterns (RAMPs), inhibit NLRP3 inflammasome activation and contribute to the cessation of cell effector functions."

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"They also observed that adenylate cyclase inhibitors reversed PGE2-mediated NLRP3 inhibition."

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"Using multiple pharmacological and molecular approaches, we have determined that PGE 2 acted specifically through EP4 to decrease NLRP3 inflammasome activation in human primary MDM."

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"PGE2-dependent suppression of NLRP3 inflammasome in liver macrophages resulted in down-regulated secretion of inflammatory cytokines (IL-1β, IL-6 and IL-18) which led to the alleviation of acute liver inflammation[17]."

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"Similar findings were reported by Miao and colleagues who provided evidence that PGE2-dependent repression of NLRP3 inflammasome in Kupffer cells was mainly responsible for beneficial effects of BM-MSCs in the attenuation of acute liver injury during lipopolysaccharide (LPS)-induced sepsis in mice[18]."

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"MSC derived PGE 2 inhibited TAK1 signaling and NLRP3 inflammasome activation in liver macrophages; meanwhile, MSC derived PGE 2 could also induce M2 macrophages to secret anti-inflammatory cytokines, like IL-10 to promote inflammation resolution and limit liver injury through activating STAT6 and mTOR signaling in macrophages, finally to inhibit the liver inflammatory response and hepatocyte apoptosis induced by LPS and D-Gal."

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"Thus, PGE 2 specifically inhibited the activity of NLRP3 inflammasome."

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"It has also been shown that prostaglandin E2 can inhibit NLRP3 inflammasome activation by inducing PKA signaling."

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"In addition, since the number of M1 macrophages and total number of macrophages increased in the ASC + celecoxib group, PGE2 produced by ASCs in macrophages might suppress the inflammatory response by[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"PGE 2 inhibits NLRP3 inflammasome through EP4 receptor."

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"Here we found that PGE 2 decreased NLRP3 inflammasome activation, triggered by aluminum crystals, ATP or nigericin."

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"Prostaglandin E 2 inhibits NLRP3 inflammasome activation through EP4 receptor and intracellular cAMP in human macrophages."

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"Prostaglandin E 2 (PGE2), which is produced by the body as a reaction to inflammation, has been reported to efficiently inhibit the activation of the NLRP3 inflammasome in human primary monocyte-deriv[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The relationship between cell migration and pyroptosis were then evaluated in hEM15A cells co-cultured in PGE2 and CY09 (the inhibitor of NLRP3)."

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"Here we have found that PGE 2 inhibited NLRP3 inflammasome activation in human primary MDM."

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"PGE2 suppressed activation of the NLR family pyrin domain containing 3 (NLRP3) inflammasome in human monocyte-derived macrophages via EP4 signaling ( Sokolowska et al., 2015 )."

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"Here, we showed that NLRP3 inflammasome activation is inhibited by PGE 2 in human primary monocyte derived macrophages."

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"For instance, PGE2 and IL-10 secreted by MSCs can reduce the function of NLRP3 inflammasome and attenuate pyroptosis [49, 99]."

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"Moreover, inhibition of endogenous PGE2 production increased NLRP3 activation, suggesting an autocrine or paracrine regulating mechanism ( Sokolowska et al., 2015 )."

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"Prostaglandin E2 inhibits NLRP3 inflammasome activation through EP4 receptor and intracellular cyclic AMP in human macrophages."

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"MSC derived PGE 2 inhibited TGF-beta-activated kinase 1 (TAK1) signaling and NLRP3 inflammasome activation in liver macrophages to decrease the production of inflammatory cytokines."

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"This suggests that the proposed PGE 2 -mediated inhibition of NLRP3 by increase in cAMP might be an additional mechanism of ω-3 derived effects."