3.4.22.36: caspase-1
This is an abbreviated version!
For detailed information about caspase-1, go to the full flat file.
Word Map on EC 3.4.22.36
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3.4.22.36
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inflammasome
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pyroptosis
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pyrin
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caspases
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nod-like
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lps
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necrosis
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tnf
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apoptosis-associated
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speck-like
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lipopolysaccharide
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adaptor
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pro-il-1
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toll-like
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card
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domain-containing
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nucleotide-binding
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neuroinflammation
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autoinflammatory
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lps-induced
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bcl-2
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domain-like
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thp-1
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multiprotein
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tunel
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microglia
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gasdermin
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danger
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marrow-derived
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interleukin-18
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leucine-rich
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cpp32
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urate
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nod2
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damage-associated
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nigericin
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medicine
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txnip
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il-1ra
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bmdms
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pan-caspase
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hmgb1
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gouty
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lymphopoietin
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monosodium
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fas-mediated
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z-vad-fmk
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fas-associated
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caspase-3-like
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pathogen-associated
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z-devd-fmk
- 3.4.22.36
- inflammasome
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pyroptosis
- pyrin
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caspases
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nod-like
- lps
- necrosis
- tnf
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apoptosis-associated
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speck-like
- lipopolysaccharide
- adaptor
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pro-il-1
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toll-like
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card
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domain-containing
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nucleotide-binding
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neuroinflammation
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autoinflammatory
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lps-induced
- bcl-2
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domain-like
- thp-1
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multiprotein
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tunel
- microglia
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gasdermin
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danger
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marrow-derived
- interleukin-18
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leucine-rich
- cpp32
- urate
- nod2
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damage-associated
- nigericin
- medicine
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txnip
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il-1ra
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bmdms
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pan-caspase
- hmgb1
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gouty
- lymphopoietin
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monosodium
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fas-mediated
- z-vad-fmk
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fas-associated
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caspase-3-like
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pathogen-associated
- z-devd-fmk
Reaction
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/- =
Synonyms
apoptosis-related cysteine protease, C14.001, CASP-1, Casp1, caspase 1, caspase-1, Csp-1, cysteine aspartyl protease-1, effector caspase, H.a.CASP1, hearm caspase-1, ICE, IL-1 beta converting enzyme, IL-1 converting enzyme, IL-1-converting enzyme, IL-1B converting enzyme, IL-1BC, IL-1beta-converting enzyme, IL-1beta–-converting enzyme, IL1beta-converting enzyme, interleukin 1, beta, convertase, interleukin converting enzyme, interleukin-1 beta converting enzyme, interleukin-1 converting enzyme, interleukin-1-converting enzyme, interleukin-1B converting enzyme, interleukin-1beta converting enzyme, interleukin-1beta-converting enzyme, interleukin-converting enzyme, p45, procaspase-1
ECTree
3.4.22.36 caspase-1Advanced search results
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results (Activating Compound
Activating Compound on EC 3.4.22.36 - caspase-1
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
adapter protein Asc
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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
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alendronate
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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
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rapidly activates caspase-1/interleukin-1beta-converting enzyme and induces extracellular release of interleukin-1beta and interleukin-18
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cathepsin B
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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
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Ipaf
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i.e. host nucleotide-binding domain and leucine-rich repeatcontaining protein Ipaf or NLRC4, Ipaf-dependent activation is unaffected by potassium treatment
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Nalp1b
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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
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NOD2
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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
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protease activating factor
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i.e. Ipaf. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
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simvastatin
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blocks inhibition of caspase-1 activation, simvastatin acts synergistically with lipopolysaccharides and causes an impairment of non-sterol isoprenoid biosynthesis, the isoprenyl intermediate GGPP could block activation of caspase-1 and interleukin-1beta release, overview
thalidomide
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thalidomide inhibits activation and activity of caspase-1 in cultured cells but not in vitro
additional information
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activation of the Rac1/PI3K/protein kinase B pathway is required for caspase-1 activation mediating increased interleukin-1beta release
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additional information
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association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
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additional information
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caspase-1 activation is induced by ATP and lipopolysaccharides
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additional information
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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
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additional information
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caspase-1 activation is stimulated by ATP and 120fold lipopolysaccharides
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additional information
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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, e.g. besides T3SS and flagellin, the host factor NLRC4 is also required for activation of caspase-1 by Salmonella typhimurium or Pseudomonas aeruginosa. Lipopolysaccharide-stimulated caspase-1 activation. Caspase-1 activation by NLRP1 does not require but is enhanced by adaptor protein ASC
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additional information
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caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
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additional information
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infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC, Listeria monocytogenes induces caspase-1 activation through both the NLRC4 and NLRP3 inflammasomes
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additional information
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TLR7 and TLR8 ligands and antiphospholipid antibodies show synergistic effects on the induction of IL-1beta and caspase-1 in monocytes and dendritic cells
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additional information
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transcription of caspase-1 gene is increased upon lipopolysaccharide and interferon-gamma stimulation
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additional information
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Bacillus anthracis poly-gamma-D-glutamic acid capsule activates caspase-1
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additional information
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caspase-1 is activated in innate immune complexes called inflammasomes
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additional information
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infection of cervical epithelial cells by Chlamydia trachomatis leads to activation of caspase-1, through a process requiring the NOD-like receptor family member NLRP3 and the inflammasome adaptor protein ASC. Elevated levels of reactive oxygen species as a result of K+ efflux are responsible for NLRP3-dependent caspase-1 activation in the infected cells
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additional information
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the inflammasome activator ATP can induce the production of reactive oxygen species, which are important for caspase-1 activation
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additional information
substrate binding increases the dimerization affinity and activity of caspase-1
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additional information
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association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
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additional information
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activation of caspase-1 in macrophages occurs independently of Nalp3 and proteasome activity
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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infection with periodontal pathogenic bacteria, e.g. Porphyromonas gingivalis and Tannerella forsythia, leads to activation of caspase-1 in macrophages, augmented by alendronate
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additional information
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nigericin-induces caspase-1 activation. Nalp1b or NLRP1b inflammasome-mediated activation of caspase-1 by anthrax lethal toxin, prevented by heat shock, overview
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additional information
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pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
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additional information
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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
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additional information
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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
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additional information
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association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
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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
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additional information
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the enzyme and apoptosis in SF-21 cell line are induced by the conditioned medium of the entomopathogenic fungus, Nomuraea rileyi, cell phenotype, overview
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