title: Negative regulators and their mechanisms in NLRP3 inflammasome activation and signaling.
abstract: Inflammasomes are cytosolic multiprotein complexes that cause the release of biologically active interleukin-1β. The best-characterized inflammasome is the NLRP3 (nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3 or Nod-like receptor protein 3) inflammasome. The NLRP3 inflammasome forms an assembly consisting of the ASC (apoptosis-associated speck-like protein containing a C-terminal caspase recruitment domain) adaptor protein and the effector, caspase-1 (cysteine-dependent aspartate-directed protease-1). Numerous agents and ligands derived from pathogens, modified self-cells and the environment induce NLRP3 inflammasome complex formation. NLRP3 inflammasome activation is tightly controlled at the transcriptional and post-translational levels to prevent unwanted excessive inflammation. Recent studies have highlighted the roles and mechanisms of several negative regulators that inhibit the assembly of NLRP3 inflammasome complexes and suppress inflammatory responses. The identification and characterization of new players in the regulation of NLRP3 inflammasome may lead to the development of inflammasome-targeting therapeutics against various inflammatory diseases related to NLRP3 inflammasome-associated pathogenesis.
authors.affiliation: Department of Microbiology, Chungnam National University School of Medicine, Daejeon, Korea.|Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea.
authors.forename: Jin Kyung
authors.initials: JK
authors.lastname: Kim
authors.affiliation: Department of Microbiology, Chungnam National University School of Medicine, Daejeon, Korea.|Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea.|Biomedical Research Institute, Chungnam National University Hospital, Daejeon, Korea.
authors.forename: Hyo Sun
authors.initials: HS
authors.lastname: Jin
authors.affiliation: Department of Microbiology, Chungnam National University School of Medicine, Daejeon, Korea.|Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea.
authors.forename: Hyun-Woo
authors.initials: HW
authors.lastname: Suh
authors.affiliation: Department of Microbiology, Chungnam National University School of Medicine, Daejeon, Korea.|Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea.
authors.forename: Eun-Kyeong
authors.initials: EK
authors.lastname: Jo
mesh_terms: D000818:Animals; D006801:Humans; D058847:Inflammasomes / Q000378:metabolism*; D008954:Models, Biological; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D058847:Inflammasomes; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein