代謝副產物誘導的 NLRP3 發炎體活化的失調涉及代謝疾病例如肥胖和第 2 型糖尿病的發病機制，然而尚未有充分的研究探討代謝相關因子是否調控發炎體活化。許多代謝相關調控因子已被提出具有抗發炎的功能，例如哺乳動物雷帕黴素靶蛋白(mTOR)、缺氧誘導因子 1α(HIF-1a)、過氧化物酶體增殖物活化受體γ(PPARγ)以及 NAD-依賴性去乙醯化酶 1(sirtuin 1, SIRT1)，顯示代謝及免疫系統條件間可能具有一定的相關性。然而這些調控因子是否能夠直接影響 NLPR3 發炎體的機制尚未充分探討，因此，本研究針對其中兩種代謝相關因子: PPARγ 以及 SIRT1 進一步分析兩種蛋白對於 NLRP3 發炎體直接的影響，我們在先前的研究中發現透過在 priming 訊號前後不同時間點給予此 PPARγ 以及 SIRT1 的活化劑皆能夠降低 NLRP3 發炎體活化產生的 caspase-1以及IL-1β，並利用免疫沈澱及影像分析的方式發現NLRP3發炎體與PPARγ 以及 SIRT1 的相互作用，NLRP3 透過不同結構與兩者進行相互作用後減少發炎體組裝進而降低 IL-1β的產生，透過分析進行減重手術的肥胖患者所分離出的外周血單核細胞，我們也發現 PPARγ 與 caspase-1 之間呈現負向相關性。此外，我們也發現到 PPARγ 活化劑在 PPARγ 表現低下時依然能夠抑制 NLRP3 發炎體活化。另一方面，作為去乙醯化酶，SIRT1 活化劑降低 NLRP3 發炎體活化過程中的乙醯化程度，透過質譜儀及蛋白質體分析篩選出可能的去乙醯化蛋白後仍需進一步分析。本研究發現 PPARγ以及 SIRT1 蛋白透過非依賴配體活化的方式對於 NLRP3 發炎體直接的影響之外，也提出活化劑可能透過不同的方式對於 NLRP3 發炎體進行調控，進一步將 PPARγ和 SIRT1 及兩者的活化劑調控 NLRP3 發炎體的概念得以應用到臨床上 NLRP3 發炎體相關疾病的治療。

Recent studies showed that aberrant metabolic byproducts facilitated NLRP3 inflammasome dysregulation which is involved in the pathogenesis of metabolic diseases such as obesity and type 2 diabetes. However, the detailed mechanism of how metabolic- related factors modulate NLRP3 inflammasome activation remains unclear. Since some metabolic regulators, including mechanistic target of rapamycin (mTOR), hypoxia-inducible factor 1a (HIF-1a), peroxisome proliferator-activated receptor gamma (PPARγ), and NAD- dependent deacetylase sirtuin-1 (SIRT1), were implicated to perform anti-inflammatory function, indicating the strong relationship between metabolism and inflammatory regulation. However, whether these metabolic-related factors directly target NLRP3 inflammasome is still vague. Here, our research focused on two metabolic factors, PPARγ and SIRT1, and investigated the role of these two proteins on NLRP3 inflammasome regulation. Our team previously found that both PPARγ and SIRT1 agonist, rosiglitazone and resveratrol, attenuated caspase-1 activation and IL-1β maturation triggered by NLRP3 inflammasome activator nigericin in LPS-primed mouse peritoneal macrophages. These effects were through both priming and activation signals of NLRP3 inflammasome. Moreover, co-immunoprecipitation and image analysis in mouse peritoneal macrophages and NLRP3 inflammasome-reconstituted HEK293T cells showed that NLRP3 interacted with PPARγ and SIRT1 through indicated domains. We also observed that overexpression of PPARγ and SIRT1 downregulated NLRP3 inflammasome formation. Furthermore, the negative correlation between PPARγ and caspase-1 was found in circulating mononuclear cells of obese patients after weight-loss surgery. In addition, we also determined that rosiglitazone attenuated NLRP3 inflammasome activation under a PPARγ hypomorphic condition. Since SIRT1 functions as a deacetylase, we found that resveratrol decreased acetylation level during NLRP3 inflammasome activation. The deacetylated targets of resveratrol and SIRT1 were examined by LC-MS/MS based proteomic analysis and need further investigation with other experiments. Our study demonstrated that PPARγ and SIRT1 physically interacted with NLRP3 inflammasome to interfere NLRP3 inflammasome assembly through a ligand-independent mechanism. PPARγ and SIRT1 agonism hence may be therapeutic options for targeting NLRP3-related metabolic diseases.

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