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Information on EC 3.4.22.36 - caspase-1 and Organism(s) Mus musculus and UniProt Accession P29452
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EC Tree
3.4.22.36 caspase-1Specify your search results
Word Map
- 3.4.22.36
- inflammasome
-
pyroptosis
- pyrin
-
caspases
-
nod-like
- lps
- necrosis
- tnf
-
apoptosis-associated
-
speck-like
- lipopolysaccharide
- adaptor
-
pro-il-1
-
toll-like
-
card
-
domain-containing
-
nucleotide-binding
-
neuroinflammation
-
autoinflammatory
-
lps-induced
- bcl-2
-
domain-like
- thp-1
-
multiprotein
-
tunel
- microglia
-
gasdermin
-
danger
-
marrow-derived
- interleukin-18
-
leucine-rich
- cpp32
- urate
- nod2
-
damage-associated
- nigericin
- medicine
-
txnip
-
il-1ra
-
bmdms
-
pan-caspase
- hmgb1
-
gouty
- lymphopoietin
-
monosodium
-
fas-mediated
- z-vad-fmk
-
fas-associated
-
caspase-3-like
-
pathogen-associated
- z-devd-fmk
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/-
Synonyms
caspase-1, caspase 1, casp1, effector caspase, procaspase-1, interleukin-1beta-converting enzyme, interleukin-1 beta converting enzyme, interleukin-1beta converting enzyme, csp-1, il-1beta-converting enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C14.001
-
-
-
-
CASP-1
ICE
IL-1 beta converting enzyme
-
-
-
-
IL-1BC
-
-
-
-
interleukin-1 beta converting enzyme
-
-
-
-
interleukin-1beta-converting enzyme
-
-
-
-
p45
-
-
-
-
CASP-1
-
-
-
-
ICE
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
122191-40-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
interleukin-18 + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
interleukin-1beta + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-caspase-7 + H2O
caspase-7 + amino-terminal procaspase-7 peptide
-
consensus caspase-7 recognition sequence DEVD, caspase-1 cleaves caspase-7 at the canonical activation sites Asp23 and Asp198, D23A/D198A double caspase-7 mutant is no substrate
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
caspase-1 processing at position D20 activates interleukin-37
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37°C conditions
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
-
-
?
additional information
?
-
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
-
-
?
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
?
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
?
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
?
additional information
?
-
-
IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
-
-
?
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
?
additional information
?
-
-
caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
-
caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
-
-
?
additional information
?
-
-
caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
?
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
-
-
?
additional information
?
-
-
the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
additional information
?
-
-
peptide substrate screening, the enzyme preferably cleaves after Asp, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
interleukin-18 + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
interleukin-1beta + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
caspase-1 processing at position D20 activates interleukin-37
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
-
-
?
additional information
?
-
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
-
-
?
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
?
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
?
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
?
additional information
?
-
-
IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
-
-
?
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
?
additional information
?
-
-
caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
-
caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
-
-
?
additional information
?
-
-
caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
?
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
-
-
?
additional information
?
-
-
the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
high extracellular K+ levels inhibit Asc-dependent caspase-1 activation, whereas Ipaf-dependent activation was unaffected by potassium treatment
Zn2+
-
pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CA-074Me
-
the caspase-1 activation is inhibited by CA-074Me, marked inhibition at 0.05 mM
Cbz-Val-Asp-fluoromethylketone
-
increase in IL-1beta protein levels in a liver injury mouse model is completely prevented with the pan-caspase inhibitor demonstrating the efficacy of Cbz-Val-Asp-fluoromethylketone to block caspase-1 activity
E-64d
-
the caspase-1 activation is inhibited by E-64d, marked inhibition at 0.05 mM
flightless-I
-
inhibits caspase-1 as a pseudosubstrate. Flightless-I might function as an inhibitor of caspase-1 in living cells through a mechanism similar to that of CrmA
-
Z-L-Tyr-L-Val-L-Ala-L-Asp-fluoromethylketone
-
specific inhibitor for caspase-1, complete inhibition at 0.05 mM
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
additional information
-
heat shock inhibits caspase-1 activity while also preventing its Nalp1b or NLRP1b inflammasome-mediated or nigericin-induced activation by anthrax lethal toxin, but once caspase-1 activation is initiated, heat shock is ineffective, time dependence, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adapter protein Asc
-
is important for caspase-1 activation during Legionella pneumophila infection, mechanism, overview. Activation of caspase-1 through Asc does not require the flagellin-sensing pathway involving the host nucleotide-binding domain and leucine-rich repeat-containing protein Ipaf, NLRC4. Asc-dependent caspase-1 activation is inhibited by high extracellular potassium levels
-
alendronate
-
a nitrogen-containing bisphosphonate, activates caspase-1, activation is inhibited by clodronate. Pretreatment of cells with alendronate augments interleukin-1beta production stimulated by Toll-like receptor ligands, augmentation is inhibited by clodronate
anthrax lethal toxin
-
rapidly activates caspase-1/interleukin-1beta-converting enzyme and induces extracellular release of interleukin-1beta and interleukin-18
-
cathepsin B
-
cathepsin B can effectively cleave and activate pro-caspase-1 in a cell-free system only at an acidic pH and in THP-1 monocytic cells after stimulation with the microbial toxin nigericin
-
Ipaf
-
i.e. host nucleotide-binding domain and leucine-rich repeatcontaining protein Ipaf or NLRC4, Ipaf-dependent activation is unaffected by potassium treatment
-
Nalp1b
-
an inflammasome component is required for caspase-1 activation, Nalp1b is a member of the NOD-like receptor family, NLR, a family of cytoplasmic proteins involved in the recognition of microbial products or danger signals. Nalp1b has a caspase recruitment domain, CARD, that allows it to interact with caspase-1
-
NOD2
-
NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in muramyl dipeptide-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
protease activating factor
-
i.e. Ipaf. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
-
additional information
-
activation of caspase-1 in macrophages occurs independently of Nalp3 and proteasome activity
-
additional information
-
activation of caspase-1 is induced in macrophages by Listeria monocytogenes infection depending on cytolysin and listeriolysin O, after evasion from phagosome into the cytoplasm, overview
-
additional information
-
ATP induces caspase-1 expression, P2X7R-deficient macrophages exhibit no caspase-1 activation response to extracellular ATP. ATP-induced caspase-1 inflammasome activation and interleukin-1beta maturation are strictly dependent on lipopolysaccharides priming of dendritic cells before ATP stimulation
-
additional information
-
caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ. Yersinia pestis KIM5 strain displays an unusual ability to activate caspase-1 and kill infected macrophages compared to other Yersinia pestis and Yersinia pseudotuberculosis strains
-
additional information
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2 and NF-kappaB and MAPK signaling
-
additional information
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
additional information
-
caspase-1 activation pathways and regulation, detailed overview. Many Gram-negative bacteria, such as Salmonella typhimurium, Pseudomonas aeruginosa, Shigella flexneri, and Legionella pneumophila, can induce caspase-1 activation and rapid macrophage cell death, the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1
-
additional information
-
caspase-1 is activated in macrophages stimulated with recombinant of pneumolysin but not in those stimulated with lipopolysaccharide, and the level of activation is higher in macrophages infected with wild-type Streptococcus pneumoniae serotype 2 strain D39 than in those infected with the DELTAply mutant
-
additional information
-
infection with periodontal pathogenic bacteria, e.g. Porphyromonas gingivalis and Tannerella forsythia, leads to activation of caspase-1 in macrophages, augmented by alendronate
-
additional information
-
nigericin-induces caspase-1 activation. Nalp1b or NLRP1b inflammasome-mediated activation of caspase-1 by anthrax lethal toxin, prevented by heat shock, overview
-
additional information
-
pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
-
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 by caspase-1. Caspase-1 activation involves pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
-
additional information
-
some members of the nucleotide-binding domain and leucine-rich-repeat-containing, NLR, gene family, including ipaf and cryopyrin, induce caspase-1 activation and the release of the interleukin-1beta and interleukin-18 through the assembly of large protein complexes called inflammasomes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
Salmonella enterica serovar typhimurium invades host macrophages and induces a unique caspase-1-dependent pathway of cell death termed pyroptosis, which is activated during bacterial infection in vivo. DNA cleavage during pyroptosis results from caspase-1-stimulated nuclease activity. Membrane pores between 1.1 and 2.4 nm in diameter form during pyroptosis of host cells and cause swelling and osmotic lysis. Pore formation requires host cell actin cytoskeleton rearrangements and caspase-1 activity, as well as the bacterial type III secretion system
-
-
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
IFN regulatory factor IRF-2(-/-) macrophages exhibit increased basal and gliotoxin-induced caspase-1 mRNA expression and enhanced caspase-1 activity
-
the Gram-negative bacterium Shigella flexneri triggers pro-inflammatory apoptotic cell death in macrophages, which is crucial for the onset of an acute inflammatory diarrhoea termed bacillary dysentery. The Mxi-Spa type III secretion system promotes bacterial uptake and escape into the cytoplasm, where, dependent on the translocator/effector protein IpaB, caspase-1 and its substrate IL-1b are activated
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
caspase-1 is required for nuclear translocation of intracellular interleukin-37 and for secretion of mature interleukin-37
physiological function
malfunction
-
caspase 1 deficiency does not affect neutrophil-dominated joint inflammation, whereas in chronic arthritis, the lack of caspase 1 results in reduced joint inflammation and cartilage destruction
malfunction
-
infection with Mycobacterium leprae induces high levels of TNF-alpha production and NF-kappaB activation in macrophages of A/J mice (mutant mouse bearing amino acid differences in Naip5, one of the NOD-like receptors (NLRs), one of the adaptor proteins for caspase-1 activation) and C57BL/6 macrophages. Caspase-1 activation and IL-1beta secretion are also induced in both macrophages. Macrophages from A/J mice exhibit reduced caspase-1 activation and IL-1beta secretion compared to C57BL/6 macrophages
malfunction
-
apoptosis is triggered upon bacterial infection in primary murine bone marrow macrophages lacking caspase-1
physiological function
-
caspase-1 is dispensable for interleukin-33 release by macrophages
physiological function
-
the production of interleukin-1beta by neutrophils and mast cells is not exclusively dependent on caspase 1, and other proteases can compensate for the loss of caspase 1 in vivo
physiological function
-
the role of caspase-1 in inducing the CD4+ T cell activity increases with interleukin-18 rather than CD8+ suppressor cell activity. There is a selective deletion of T lymphocytes mediated by caspase-1 via interleukin-18
physiological function
-
lysosome exocytosis is a conserved caspase-1-dependent feature of pyroptosis. Caspase-1 activation leads to increased membrane permeability and an influx of calcium, which results in fusion of lysosomes with the cell surface and release of lysosomal contents. Secretion of processed IL-1beta and IL-18 in macrophages undergoing pyroptosis occurs independently of lysosome exocytosis. Multiple stimuli, acting through a diverse set of NLR proteins, lead to two conserved caspase-1-dependent secretion events: the release of processed inflammatory cytokines and lysosome-mediated release of antimicrobial host factors and degraded microbial products
physiological function
-
caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop during Francisella infection
physiological function
-
lysosomal swelling and mitochondrial impairment contribute to caspase-1 activation and to the consequent interleukin-1beta release
physiological function
-
the processing and release of the regulatory caspase-1 substrate interleukin-18 counteracts the proinflammatory activities of another caspase-1 substrate, interleukin-1beta, thereby balancing control of the Helicobacter infection with the prevention of excessive gastric immunopathology
physiological function
-
upon Salmonella infection, inflammasome-mediated caspase-1 activity is required to bypass apoptosis in favor of pro-inflammatory pyroptotic cell death
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CASP1_MOUSE
402
0
45640
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
caspase-1 is synthesized as an inactive zymogen that becomes activated by cleavage at aspartic residues to generate an enzymatically active 10-20 kDa heterodimer
proteolytic modification
-
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1, it is also activated by caspase-11
proteolytic modification
-
the inflammasome, a multiprotein complex, regulates caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
caspase-1-/- bone marrow-derived macrophages exhibit strong caspase-3 expression and reduced cell damage compared to wild-type cells during early Burkholderia pseudomallei infection, indicating classical apoptosis, whereas wild-type bone marrow-derived macrophages show signs of rapid caspase-1-dependent cell death. Caspase-1-/- bone marrow-derived macrophages exhibit impaired bactericidal activity compared to wild-type bone marrow-derived macrophages
additional information
-
caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
additional information
-
caspase-1-deficient mice have unimpaired inflammatory responses to necrotic cells
additional information
-
defective Anthrax-induced interleukin-1beta secretion in Nod2-/- or caspase-1-/- macrophages, not due to decreased pro-interleukin-1beta expression, caspase-1 or NOD2 deficiencies do not exert a major effect on TNF-alpha secretion
additional information
-
genetic disruption of cryopyrin or the adaptor apoptosis associated speck-like protein, ASC, abrogates caspase-1 activation in poly(I:C), dsRNA, or viral RNA-stimulated macrophages
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
additional information
-
secretion of interleukin-1beta following KIM5 infection is reduced in caspase-1-deficient macrophages compared to wild-type macrophages
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transient co-expression of of FALG-tagged NOD2, Myc-tagged caspase-1, and pro-interleukin-1beta in HEK293T cells allows muramyl dipeptide-induced pro-interleukin-1beta processing
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
caspase-1 is upregulated in CD8+ cells with decreased expression of interleukin-4 and interleukin-10
-
macrophages from A/J mice exhibit reduced caspase-1 activation and IL-1beta secretion compared to C57BL/6 macrophages
-
the activation of caspase-1 is markedly inhibited with increasing concentrations of extracellular KCl
-
the region of difference 1 locus in the Mycobacterium tuberculosis genome contributes to activation of caspase-1 via induction of potassium ion efflux in infected macrophages
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the caspase-1/IL-1beta signaling pathway plays an important role in diabetes-induced retinal pathology, and its inhibition might represent a new strategy to inhibit capillary degeneration in diabetic retinopathy
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
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64
821-846
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Homo sapiens, Mus musculus
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Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus (P29452), Mus musculus, Mus musculus C3H/An (P29452)
Nett-Fiordalisi, M.A.; Cerretti, D.P.; Berson, D.R.; Gilbert, D.J.; Jenkins, N.A.; Copeland, N.G.; Black, R.A.; Chaplin, D.D.
Molecular cloning of the murine IL-1 beta converting enzyme cDNA
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149
3254-3259
1992
Mus musculus (P29452), Mus musculus
Molineaux, S.M.; Casano, F.J.; Rolando, A.M.; et al.
Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a structurally conserved homologue of human IL-1 beta converting enzyme
Proc. Natl. Acad. Sci. USA
90
1809-1813
1993
Mus musculus (P29452), Mus musculus
Raupach, B.; Peuschel, S.K.; Monack, D.M.; Zychlinsky, A.
Caspase-1-mediated activation of interleukin-1beta (IL-1beta) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar typhimurium infection
Infect. Immun.
74
4922-4926
2006
Mus musculus
Cordoba-Rodriguez, R.; Fang, H.; Lankford, C.S.; Frucht, D.M.
Anthrax lethal toxin rapidly activates caspase-1/ICE and induces extracellular release of interleukin (IL)-1beta and IL-18
J. Biol. Chem.
279
20563-20566
2004
Mus musculus
Miao, E.A.; Alpuche-Aranda, C.M.; Dors, M.; Clark, A.E.; Bader, M.W.; Miller, S.I.; Aderem, A.
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
Nat. Immunol.
7
569-575
2006
Mus musculus
Sarkar, A.; Hall, M.W.; Exline, M.; Hart, J.; Knatz, N.; Gatson, N.T.; Wewers, M.D.
Caspase-1 regulates Escherichia coli sepsis and splenic B cell apoptosis independently of interleukin-1beta and interleukin-18
Am. J. Respir. Crit. Care Med.
174
1003-1010
2006
Mus musculus
Keller, M.; Rueegg, A.; Werner, S.; Beer, H.D.
Active caspase-1 is a regulator of unconventional protein secretion
Cell
132
818-831
2008
Homo sapiens, Mus musculus
Muehlbauer, S.M.; Evering, T.H.; Bonuccelli, G.; Squires, R.C.; Ashton, A.W.; Porcelli, S.A.; Lisanti, M.P.; Brojatsch, J.
Anthrax lethal toxin kills macrophages in a strain-specific manner by apoptosis or caspase-1-mediated necrosis
Cell Cycle
6
758-766
2007
Mus musculus
Fink, S.L.; Cookson, B.T.
Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages
Cell. Microbiol.
8
1812-1825
2006
Mus musculus
Merkle, S.; Frantz, S.; Schoen, M.P.; Bauersachs, J.; Buitrago, M.; Frost, R.J.; Schmitteckert, E.M.; Lohse, M.J.; Engelhardt, S.
A role for caspase-1 in heart failure
Circ. Res.
100
645-653
2007
Mus musculus
Vincent, J.A.; Mohr, S.
Inhibition of caspase-1/interleukin-1beta signaling prevents degeneration of retinal capillaries in diabetes and galactosemia
Diabetes
56
224-230
2007
Mus musculus
Li, J.; Yin, H.L.; Yuan, J.
Flightless-I regulates proinflammatory caspases by selectively modulating intracellular localization and caspase activity
J. Cell Biol.
181
321-333
2008
Mus musculus
Brough, D.; Rothwell, N.J.
Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death
J. Cell Sci.
120
772-781
2007
Mus musculus
Galle, M.; Schotte, P.; Haegman, M.; Wullaert, A.; Yang, H.J.; Jin, S.; Beyaert, R.
The Pseudomonas aeruginosa Type III secretion system plays a dual role in the regulation of caspase-1 mediated IL-1beta maturation
J. Cell. Mol. Med.
12
1767-1776
2008
Mus musculus
Cuesta, N.; Nhu, Q.M.; Zudaire, E.; Polumuri, S.; Cuttitta, F.; Vogel, S.N.
IFN regulatory factor-2 regulates macrophage apoptosis through a STAT1/3- and caspase-1-dependent mechanism
J. Immunol.
178
3602-3611
2007
Mus musculus
Pedra, J.H.; Sutterwala, F.S.; Sukumaran, B.; Ogura, Y.; Qian, F.; Montgomery, R.R.; Flavell, R.A.; Fikrig, E.
ASC/PYCARD and caspase-1 regulate the IL-18/IFN-gamma axis during Anaplasma phagocytophilum infection
J. Immunol.
179
4783-4791
2007
Mus musculus
Schroeder, G.N.; Jann, N.J.; Hilbi, H.
Intracellular type III secretion by cytoplasmic Shigella flexneri promotes caspase-1-dependent macrophage cell death
Microbiology
153
2862-2876
2007
Mus musculus
Fink, S.L.; Bergsbaken, T.; Cookson, B.T.
Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
Proc. Natl. Acad. Sci. USA
105
4312-4317
2008
Mus musculus
Yu, H.B.; Finlay, B.B.
The caspase-1 inflammasome: a pilot of innate immune responses
Cell Host Microbe
4
198-208
2008
Homo sapiens, Mus musculus
Reig, N.; Jiang, A.; Couture, R.; Sutterwala, F.S.; Ogura, Y.; Flavell, R.A.; Mellman, I.; van der Goot, F.G.
Maturation modulates caspase-1-independent responses of dendritic cells to Anthrax lethal toxin
Cell. Microbiol.
10
1190-1207
2008
Mus musculus
Levin, T.C.; Wickliffe, K.E.; Leppla, S.H.; Moayeri, M.
Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin
Cell. Microbiol.
10
2434-2446
2008
Mus musculus, Mus musculus BALB/cJ
Brough, D.; Pelegrin, P.; Rothwell, N.J.
Pannexin-1-dependent caspase-1 activation and secretion of IL-1beta is regulated by zinc
Eur. J. Immunol.
39
352-358
2009
Mus musculus
Thomas, P.G.; Dash, P.; Aldridge, J.R.; Ellebedy, A.H.; Reynolds, C.; Funk, A.J.; Martin, W.J.; Lamkanfi, M.; Webby, R.J.; Boyd, K.L.; Doherty, P.C.; Kanneganti, T.D.
The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1
Immunity
30
566-575
2009
Mus musculus
Case, C.L.; Shin, S.; Roy, C.R.
Asc and Ipaf inflammasomes direct distinct pathways for caspase-1 activation in response to Legionella pneumophila
Infect. Immun.
17
1981-1991
2009
Mus musculus, Mus musculus C57BL/6
Shoma, S.; Tsuchiya, K.; Kawamura, I.; Nomura, T.; Hara, H.; Uchiyama, R.; Daim, S.; Mitsuyama, M.
Critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro: a novel function of pneumolysin in caspase-1 activation
Infect. Immun.
76
1547-1557
2008
Mus musculus
Lilo, S.; Zheng, Y.; Bliska, J.B.
Caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ
Infect. Immun.
76
3911-3923
2008
Mus musculus
Breitbach, K.; Sun, G.W.; Koehler, J.; Eske, K.; Wongprompitak, P.; Tan, G.; Liu, Y.; Gan, Y.H.; Steinmetz, I.
Caspase-1 mediates resistance in murine melioidosis
Infect. Immun.
77
1589-1595
2009
Mus musculus
Marina-Garcia, N.; Franchi, L.; Kim, Y.G.; Miller, D.; McDonald, C.; Boons, G.J.; Nunez, G.
Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2
J. Immunol.
180
4050-4057
2008
Mus musculus, Mus musculus C57BL/6
Hara, H.; Tsuchiya, K.; Nomura, T.; Kawamura, I.; Shoma, S.; Mitsuyama, M.
Dependency of caspase-1 activation induced in macrophages by Listeria monocytogenes on cytolysin, listeriolysin O, after evasion from phagosome into the cytoplasm
J. Immunol.
180
7859-7868
2008
Mus musculus
Qu, Y.; Ramachandra, L.; Mohr, S.; Franchi, L.; Harding, C.V.; Nunez, G.; Dubyak, G.R.
P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome but is independent of caspase-1
J. Immunol.
182
5052-5062
2009
Mus musculus, Mus musculus C57BL/6
Rosenzweig, H.L.; Martin, T.M.; Planck, S.R.; Galster, K.; Jann, M.M.; Davey, M.P.; Kobayashi, K.; Flavell, R.A.; Rosenbaum, J.T.
Activation of NOD2 in vivo induces IL-1beta production in the eye via caspase-1 but results in ocular inflammation independently of IL-1 signaling
J. Leukoc. Biol.
84
529-536
2008
Mus musculus, Mus musculus BALB/c
Foley, K.; Kast, R.E.; Altschuler, E.L.
Ritonavir and disulfiram have potential to inhibit caspase-1 mediated inflammation and reduce neurological sequelae after minor blast exposure
Med. Hypotheses
72
150-152
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Lamkanfi, M.; Kanneganti, T.D.; Van Damme, P.; Vanden Berghe, T.; Vanoverberghe, I.; Vandekerckhove, J.; Vandenabeele, P.; Gevaert, K.; Nunez, G.
Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes
Mol. Cell. Proteomics
7
2350-2363
2008
Mus musculus, Mus musculus C57BL/6
Franchi, L.; Eigenbrod, T.; Munoz-Planillo, R.; Nunez, G.
The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis
Nat. Immunol.
10
241-247
2009
Homo sapiens, Mus musculus
Hornung, V.; Ablasser, A.; Charrel-Dennis, M.; Bauernfeind, F.; Horvath, G.; Caffrey, D.R.; Latz, E.; Fitzgerald, K.A.
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Nature
458
514-518
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Hsu, L.C.; Ali, S.R.; McGillivray, S.; Tseng, P.H.; Mariathasan, S.; Humke, E.W.; Eckmann, L.; Powell, J.J.; Nizet, V.; Dixit, V.M.; Karin, M.
A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide
Proc. Natl. Acad. Sci. USA
105
7803-7808
2008
Mus musculus
Deng, X.; Tamai, R.; Endo, Y.; Kiyoura, Y.
Alendronate augments interleukin-1beta release from macrophages infected with periodontal pathogenic bacteria through activation of caspase-1
Toxicol. Appl. Pharmacol.
235
97-104
2009
Mus musculus
Guma, M.; Ronacher, L.; Liu-Bryan, R.; Takai, S.; Karin, M.; Corr, M.
Caspase 1-independent activation of interleukin-1beta in neutrophil-predominant inflammation
Arthritis Rheum.
60
3642-3650
2009
Mus musculus
Joosten, L.A.; Netea, M.G.; Fantuzzi, G.; Koenders, M.I.; Helsen, M.M.; Sparrer, H.; Pham, C.T.; van der Meer, J.W.; Dinarello, C.A.; van den Berg, W.B.
Inflammatory arthritis in caspase 1 gene-deficient mice: contribution of proteinase 3 to caspase 1-independent production of bioactive interleukin-1beta
Arthritis Rheum.
60
3651-3662
2009
Mus musculus
Terada, K.; Yamada, J.; Hayashi, Y.; Wu, Z.; Uchiyama, Y.; Peters, C.; Nakanishi, H.
Involvement of cathepsin B in the processing and secretion of interleukin-1beta in chromogranin A-stimulated microglia
Glia
58
114-124
2010
Mus musculus
Kurenuma, T.; Kawamura, I.; Hara, H.; Uchiyama, R.; Daim, S.; Dewamitta, S.R.; Sakai, S.; Tsuchiya, K.; Nomura, T.; Mitsuyama, M.
The RD1 locus in the Mycobacterium tuberculosis genome contributes to activation of caspase-1 via induction of potassium ion efflux in infected macrophages
Infect. Immun.
77
3992-4001
2009
Mus musculus
Prantner, D.; Darville, T.; Sikes, J.D.; Andrews, C.W.; Brade, H.; Rank, R.G.; Nagarajan, U.M.
Critical role for interleukin-1beta (IL-1beta) during Chlamydia muridarum genital infection and bacterial replication-independent secretion of IL-1beta in mouse macrophages
Infect. Immun.
77
5334-5346
2009
Mus musculus
Bagchi, A.K.; Sinha, A.K.; Adhikari, R.; Maiti, P.; Mukherjee, J.; Panda, A.; Saha, D.R.
Selective deletion of CD8+ cells upregulated by caspases-1 via IL-18 in mice immunized with major outer membrane protein of Shigella dysenteriae 1 following infection
J. Clin. Immunol.
30
408-418
2010
Mus musculus
Ohno, T.; Oboki, K.; Kajiwara, N.; Morii, E.; Aozasa, K.; Flavell, R.A.; Okumura, K.; Saito, H.; Nakae, S.
Caspase-1, caspase-8, and calpain are dispensable for IL-33 release by macrophages
J. Immunol.
183
7890-7897
2009
Mus musculus
Bergsbaken, T.; Fink, S.L.; den Hartigh, A.B.; Loomis, W.P.; Cookson, B.T.
Coordinated host responses during pyroptosis: caspase-1-dependent lysosome exocytosis and inflammatory cytokine maturation
J. Immunol.
187
2748-2754
2011
Mus musculus
Kang, T.J.; Lee, G.S.; Kim, S.K.; Jin, S.H.; Chae, G.T.
Comparison of two mice strains, A/J and C57BL/6, in caspase-1 activity and IL-1beta secretion of macrophage to Mycobacterium leprae infection
Mediators Inflamm.
2010
708713
2010
Mus musculus
Williams, C.D.; Farhood, A.; Jaeschke, H.
Role of caspase-1 and interleukin-1beta in acetaminophen-induced hepatic inflammation and liver injury
Toxicol. Appl. Pharmacol.
247
169-178
2010
Mus musculus
Moquin, A.; Hutter, E.; Choi, A.O.; Khatchadourian, A.; Castonguay, A.; Winnik, F.M.; Maysinger, D.
Caspase-1 activity in microglia stimulated by pro-inflammagen nanocrystals
ACS nano
7
9585-9598
2013
Mus musculus
Juruj, C.; Lelogeais, V.; Pierini, R.; Perret, M.; Py, B.F.; Jamilloux, Y.; Broz, P.; Ader, F.; Faure, M.; Henry, T.
Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop
Front. Cell. Infect. Microbiol.
3
14
2013
Mus musculus
Hitzler, I.; Sayi, A.; Kohler, E.; Engler, D.B.; Koch, K.N.; Hardt, W.D.; Mueller, A.
Caspase-1 has both proinflammatory and regulatory properties in Helicobacter infections, which are differentially mediated by its substrates IL-1beta and IL-18
J. Immunol.
188
3594-3602
2012
Mus musculus
Puri, A.W.; Broz, P.; Shen, A.; Monack, D.M.; Bogyo, M.
Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection
Nat. Chem. Biol.
8
745-747
2012
Mus musculus
Bulau, A.M.; Nold, M.F.; Li, S.; Nold-Petry, C.A.; Fink, M.; Mansell, A.; Schwerd, T.; Hong, J.; Rubartelli, A.; Dinarello, C.A.; Bufler, P.
Role of caspase-1 in nuclear translocation of IL-37, release of the cytokine, and IL-37 inhibition of innate immune responses
Proc. Natl. Acad. Sci. USA
111
2650-2655
2014
Mus musculus
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