The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response

@article{BarojaMazo2014TheNI,
  title={The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response},
  author={Alberto Baroja-Mazo and F{\'a}tima Mart{\'i}n-S{\'a}nchez and Ana Isabel Platero G{\'o}mez and Carlos Manuel Mart{\'i}nez and Joaqu{\'i}n Amores-Iniesta and Vincent Compan and Mar{\'i}a Barber{\`a}-Cremades and Jordi Yag{\"u}e and Est{\'i}baliz Ru{\'i}z-Ortiz and Jordi Ant{\'o}n and Segundo Buj{\'a}n and Isabelle Couillin and David Brough and Juan Ignacio Ar{\'o}stegui and Pablo Pelegr{\'i}n},
  journal={Nature Immunology},
  year={2014},
  volume={15},
  pages={738-748}
}
Assembly of the NLRP3 inflammasome activates caspase-1 and mediates the processing and release of the leaderless cytokine IL-1β and thereby serves a central role in the inflammatory response and in diverse human diseases. Here we found that upon activation of caspase-1, oligomeric NLRP3 inflammasome particles were released from macrophages. Recombinant oligomeric protein particles composed of the adaptor ASC or the p.D303N mutant form of NLRP3 associated with cryopyrin-associated periodic… 

Isolation of Particles of Recombinant ASC and NLRP3.

Studying the extracellular function of oligomeric ASC andNLRP3 inflammasome particles was possible by purification of recombinant particles of ASC or the constitutively activated NLRP3 mutant associated with cryopyrin-associated periodic syndromes, both tagged with the yellow fluorescent protein and expressed in HEK293 cells.

Regulation of the NLRP3 Inflammasome by Posttranslational Modifications

The posttranslational modifications that regulate NLRP3 inflammasome components, including ubiquitination, phosphorylation, and other forms of posttranslated modifications are described.

Priming is dispensable for NLRP3 inflammasome activation in human monocytes

It is shown that in primary human monocytes, the initial priming step is dispensable to form an active NLRP3 inflammasome and this work highlights the readiness of the NLRP2 inflammaome to assemble in the absence of priming and hence contribute to sterile inflammatory processes in health and disease.

Chloride regulates dynamic NLRP3-dependent ASC oligomerization and inflammasome priming

In insights into the dynamic nature of inflammasome oligomerization and its dependence on chloride ions are reported, revealing an additional layer of regulation and priming that can further enhance and drive inflammatory responses.

The NLRP3 Inflammasome: Relevance in Solid Organ Transplantation

The NOD, LRR, and pyrin domain-containing 3 (NLRP3) protein has been established as a central component of the inflammasome and regulates the inflammatory response to a myriad of environmental, microbial, and endogenous danger stimuli, which can be aberrantly activated by the likes of cell-free DNA, and cause significant autoimmune pathology.

The NLRP3 and Pyrin Inflammasomes: Implications in the Pathophysiology of Autoinflammatory Diseases

This review focuses on germline mutations that have been described in cryopyrin-associated periodic syndrome (CAPS) for NLRP3 or in familial Mediterranean fever (FMF) and pyrIn-associated autoinflammation with neutrophilic dermatosis (PAAND) for MEFV.

Peripheral NLCR4 inflammasome participates in the genesis of acute inflammatory pain

The results identified the inflammasome components NLRC4 and ASC as the molecular platform involved in the peripheral activation of caspase-1 and IL-1&bgr; maturation, which are responsible for the induction of acute inflammatory pain.

POP1 inhibits MSU-induced inflammasome activation and ameliorates gout

It is demonstrated that POP1 expression in macrophages is sufficient to dampen MSU crystal-mediatedinflammatory responses in animal models of gout and may play a crucial role in regulating inflammatory responses in gout.

Emerging Role of NLRP3 Inflammasome and Pyroptosis in Liver Transplantation

The recent literature addressing the role of the NLRP3 inflammasome and pyroptosis in all stages involved in LT is summarized and the potential targeting of this pathway as a future therapeutic strategy to improve LT outcomes is argued.
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