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When the body is injured or unwell, many biochemical reactions are activated, including immune response, blood coagulation response and inflammatory response. Polyprotein oligomers (molecules composed of many protein units) called inflammasomes mediate this inflammatory response to injury/disease.

The inflammasome is composed of caspase-1 enzyme, caspase-5 enzyme, Pycard/Asc and NAPL1. NAPL1 is a protein carrying Pyrin domain and has a structure with NOD (nucleotide-binding oligomerization domain-like receptor) Homology. The main scaffold for inflammasome assembly is composed of filaments of the Pyrin domain (the way proteins chemically interact with each other) and the caspase recruitment domain.

Caspase is an enzyme that is a part of the inflammasome and is mediated by it. It is a family of endoproteases closely related to cell death and inflammation. The activation of these specific enzymes is strictly controlled by some biochemical mediators, including inflammasomes. Once these enzymes are released, they will obtain catalytic energy through signal events (including biochemical cascade reactions). This specificity ensures the controlled destruction of cellular components that are no longer needed, which can then be used in other parts of the cell.

A group of germline-encoded pattern recognition receptors together with other receptors are the main components of the inflammasome activation complex. Once there is a certain stimulus (such as a specific pathogen cell surface protein), the relevant receptor will be oligomerized to become a caspase-1 activated scaffold, which will eventually induce an inflammatory response.

The cascade of inflammasome activation depends on the type of inflammasome exposed to the irritant. Prominent inflammasomes include ASC, AIM2 and NAIP/NLRC4. For example, AIM2 binds directly to double-stranded DNA, which is its specific stimulus. Compared with all other known inflammasomes, NLRP3 inflammasomes can be activated under the widest range of stimuli, which leads to a common theory that different agonists can induce further downstream responses, which are controlled by NLRP3 Inflammatory body perception.

If some inflammasomes/related inflammation receptors are wrong, it will lead to disease. For example, functional mutations in the NACHT domain of the NLRP3 inflammasome can lead to a series of chronic, aseptic inflammatory diseases: Muckle-wells syndrome, familial influenza autoinflammatory disease (FCAS) and neonatal multi-system inflammatory disease/chronic Infant neurocutaneous joint disease. Syndrome (NOMID/CINCA). These conditions are all related to the family of periodic syndromes related to cold and hot proteins.

Gout is an inflammatory disease caused by the deposition of monosodium urate crystals in various tissues of the body. It can cause clinical symptoms such as acute monoarthritis. It causes the deposition of monosodium urate crystals in the joints, which triggers an acute inflammatory response in the NLRP3 inflammasome. Sodium urate crystals can activate NLRP3 inflammasomes in vitro (laboratory) and in vivo (in patients).

A common treatment method is to use Interleukin-1 for treatment. This ligand and receptor family is associated with acute and chronic inflammatory diseases, and interleukin (IL) 1β has been observed as a therapeutic target for local autoinflammatory diseases. The inactivation of IL-1β can lead to a rapid and continuous decrease in the severity of the disease and its symptoms.

Phoebe Hinton-Sheley holds a Bachelor of Science degree. Microbiology, University of Wolverhampton (First Class Honours). Due to her background and interests, Phoebe mainly writes for the life sciences of News-Medical, focusing on microbiology and related technologies and diseases. However, she also likes to write articles on topics such as genetics, molecular biology, and biochemistry.

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