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Caspase‐1 inflammasomes in infection and inflammation
Author(s) -
Lamkanfi Mohamed,
Kanneganti ThirumalaDevi,
Franchi Luigi,
Núñez Gabriel
Publication year - 2007
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.1206756
Subject(s) - inflammasome , nalp3 , biology , pyrin domain , aim2 , receptor , nlrc4 , innate immune system , pattern recognition receptor , signal transduction , caspase 1 , microbiology and biotechnology , genetics
Nucleotide‐binding and oligomerization domain‐like receptors (NLRs) constitute a family of germline‐encoded pattern‐recognition receptors, which allow the host to respond rapidly to a wide variety of pathogenic microorganisms. Here, we discuss recent advances in the study of a subset of NLRs, which control the activation of caspase‐1 through the assembly of large protein complexes, inflammasomes. The NALP1b inflammasome recognizes anthrax lethal toxin, and flagellin from Salmonella and Legionella induces assembly of the Ipaf inflammasome. Cryopyrin/NALP3 mediates caspase‐1 activation in response to a wide variety of bacterial ligands, imidazoquinolines, dsRNA, and the endogenous danger signal uric acid. The importance of these cytosolic receptors in immune regulation is underscored by the identification of mutations in cryopyrin/NALP3, which are genetically linked to human autoinflammatory disorders.