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
-
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
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
results (
results (Source Tissue
Source Tissue on EC 3.4.22.36 - caspase-1
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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increased enzyme content during pregnancy, women with spontaneous labor at term have a higher median caspase-1 amniotic fluid concentration than women at term without labor
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functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
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high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
of feeding and wandering larvae. Expression of Hearm caspase-1 in the haemocytes appears to be correlated with the pulse of ecdysone, and it is up-regulated by ecdysone agonist RH-2485, implying that Hearm caspase-1 activation is regulated by ecdysone
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caspase-1 gene is expressed in 1 day post-hatching larvae and its mRNA levels increases throughout development
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high activity in from peripheral blood of mevalonate kinase deficiency patients
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caspase-1 activity is required for neuronal differentiation of PC12 cells
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bacterial infection leads to a decrease in the mRNA levels of caspase-1
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caspase-1 is increased in lesional psoriatic skin capared with non-lesional psoriatic skin
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high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
additional information
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acute coronary syndromes is related to increased concentration of systemic soluble ICE. Patients with myocardial infarction demonstrate heightened systemic levels of ICE as compared to patients with stable angina and patients with unstable angina
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bacterial infection leads to a decrease in the mRNA levels of caspase-1
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inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
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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
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bacterial infection leads to a decrease in the mRNA levels of caspase-1
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low activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
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inactive 45000 Da proform of caspase-1 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 20000 Da form
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bone marrow-derived macrophages, wild-type and superoxide dismutase-deficient
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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
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caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
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IFN regulatory factor IRF-2(-/-) macrophages exhibit increased basal and gliotoxin-induced caspase-1 mRNA expression and enhanced caspase-1 activity
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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
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both the active and the precursor domains of caspase-1are localized in the cytoplasmatic matrix and on the cell surface
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primary neuron, caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
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bacterial infection leads to a decrease in the mRNA levels of caspase-1
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quantification of caspase-1 p20 subunit levels in culture supernatants of THP-1 cells
