Published online before print April 18, 2007
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Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, Michigan, USA
1 Correspondence: Department of Pathology, University of Michigan Medical School, 4215 CCGC, 1500 E. Medical Center Drive, Ann Arbor, MI 48109, USA. E-mail: bclx{at}umich.edu
ABSTRACT
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.
Key Words: NLR • TLR • ASC • Ipaf • cryopyrin
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