Anti-NLRP1 antibody

Target data

Acts as the sensor component of the NLRP1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed : 12191486, PubMed : 17349957, PubMed : 22665479, PubMed : 27662089, PubMed : 31484767, PubMed : 33093214, PubMed : 33410748, PubMed : 33731929, PubMed : 33731932, PubMed : 35857590). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed : 12191486, PubMed : 17349957, PubMed : 22665479). Acts as a recognition receptor (PRR) : recognizes specific pathogens and other damage-associated signals, such as cleavage by some human enteroviruses and rhinoviruses, double-stranded RNA, UV-B irradiation, or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex composed of NLRP1, CASP1 and PYCARD/ASC (PubMed : 12191486, PubMed : 17349957, PubMed : 22665479, PubMed : 25562666, PubMed : 30096351, PubMed : 30291141, PubMed : 33093214, PubMed : 33243852, PubMed : 33410748, PubMed : 35857590). In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and associates with PYCARD/ASC to initiate the formation of the inflammasome complex : the NLRP1 inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (PubMed : 12191486, PubMed : 17349957, PubMed : 22665479, PubMed : 32051255, PubMed : 33093214). In the absence of GSDMD expression, the NLRP1 inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (PubMed : 33852854, PubMed : 35594856). Activation of NLRP1 inflammasome is also required for HMGB1 secretion; the active cytokines and HMGB1 stimulate inflammatory responses (PubMed : 22801494). Binds ATP and shows ATPase activity (PubMed : 11113115, PubMed : 15212762, PubMed : 33243852). Plays an important role in antiviral immunity and inflammation in the human airway epithelium (PubMed : 33093214). Specifically recognizes a number of pathogen-associated signals : upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion (PubMed : 33093214). Positive-strand RNA viruses, such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion (PubMed : 33243852). Acts as a direct sensor for long dsRNA and thus RNA virus infection (PubMed : 33243852). May also be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed : 18511561). The NLRP1 inflammasome is also activated in response to UV-B irradiation causing ribosome collisions : ribosome collisions cause phosphorylation and activation of NLRP1 in a MAP3K20-dependent manner, leading to pyroptosis (PubMed : 35857590).. NACHT, LRR and PYD domains-containing protein 1. Constitutes the precursor of the NLRP1 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals.. NACHT, LRR and PYD domains-containing protein 1, N-terminus. Regulatory part that prevents formation of the NLRP1 inflammasome : in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the NLRP1 inflammasome (PubMed : 33093214). In response to pathogen-associated signals, this part is ubiquitinated and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the NLRP1 inflammasome (PubMed : 33093214).. NACHT, LRR and PYD domains-containing protein 1, C-terminus. Constitutes the active part of the NLRP1 inflammasome (PubMed : 33093214, PubMed : 33731929, PubMed : 33731932). In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the NLRP1 inflammasome (PubMed : 33093214). In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing this form, which polymerizes and associates with PYCARD/ASC to form of the NLRP1 inflammasome complex : the NLRP1 inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis (PubMed : 33093214).. Isoform 2. It is unclear whether is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release (PubMed : 22665479). However, in an vitro cell-free system, it has been shown to be activated by MDP (PubMed : 17349957).

Alternative Names

CARD7, DEFCAP, KIAA0926, NAC, NALP1, NLRP1, Caspase recruitment domain-containing protein 7, Death effector filament-forming ced-4-like apoptosis protein, Nucleotide-binding domain and caspase recruitment domain