Abstract
ALDOA: aldolase A; AMPK: AMP-activated protein kinase; ATG: autophagy related; ATG5: autophagy related 5; ATP: adenosine triphosphate; BMDMs: bone marrow-derived macrophages; CALCOCO2: calcium binding and coiled-coil domain 2; CASP1: caspase 1; CQ: chloroquine; FOXO3: forkhead box O3; IL1B: interleukin 1 beta; LPS: lipopolysaccharide; MAP1LC3B/LC3B: microtubule-associated protein 1 light chain 3 beta; MT: mutant; mtDNA: mitochondrial DNA; MTORC1: mechanistic target of rapamycin kinase complex 1; mtROS: mitochondrial reactive oxygen species; NLRP3: NLR family, pyrin domain containing 3; OPTN: optineurin; PBS: phosphate-buffered saline; PRKN/Parkin: parkin RBR E3 ubiquitin protein ligase; SN: supernatant; SQSTM1/p62: sequestosome 1; STK11/LKB1: serine/threonine kinase 11; TOMM20: translocase of outer mitochondrial membrane 20; ULK1: unc-51 like autophagy activating kinase 1; v-ATPase: vacuolar type H+-ATPase; WT: wild-type.
Keywords:
ALDOA; AMPK; LYG-202; NLRP3 inflammasome; mitophagy.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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AMP-Activated Protein Kinases
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Adenosine Triphosphatases
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Autophagy* / physiology
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Caspase 1
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DNA, Mitochondrial / metabolism
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Inflammasomes* / metabolism
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Lipopolysaccharides
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NLR Family, Pyrin Domain-Containing 3 Protein
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Ubiquitin-Protein Ligases / metabolism
Substances
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DNA, Mitochondrial
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Inflammasomes
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Lipopolysaccharides
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NLR Family, Pyrin Domain-Containing 3 Protein
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Ubiquitin-Protein Ligases
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AMP-Activated Protein Kinases
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Caspase 1
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Adenosine Triphosphatases
Grants and funding
This work was supported by the National Natural Science Foundation of China [81903626]; National Natural Science Foundation of China [81872899]; Natural Science Foundation of Jiangsu Province [BK20180576]; Research Innovation Program for College Graduates of Jiangsu Province [1152100016]; Social Development Project of Jiangsu Provincial Science and Technology Department [BE2018711]; Fundamental Research Funds for the Central Universities [No.2632021ZD03].