3.4.22.56: caspase-3
This is an abbreviated version!
For detailed information about caspase-3, go to the full flat file.
Word Map on EC 3.4.22.56
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3.4.22.56
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bcl-2
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caspase-9
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necrosis
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tunel
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parp
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anti-apoptotic
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neuroprotective
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pro-apoptotic
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tnf
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endothelial
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annexin
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leukemia
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apoptosis-related
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mapks
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fas
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ischemia
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dismutase
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deoxynucleotidyl
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erk
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neurotoxicity
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artery
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cyclin
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cerebral
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dutp
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malondialdehyde
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reperfusion
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infarct
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nick
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cardiac
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sirna
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apoptosis-inducing
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myocardial
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gsh
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cardiomyocytes
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sham
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c-jun
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cisplatin
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survivin
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transferase-mediated
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iodide
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hippocampal
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adp-ribose
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hoechst
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antiproliferative
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caspase-dependent
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polyadp-ribose
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bid
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ischemia-reperfusion
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propidium
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ladder
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analysis
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drug development
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molecular biology
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medicine
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diagnostics
- 3.4.22.56
- bcl-2
- caspase-9
- necrosis
-
tunel
- parp
-
anti-apoptotic
-
neuroprotective
-
pro-apoptotic
- tnf
- endothelial
-
annexin
- leukemia
-
apoptosis-related
- mapks
- fas
- ischemia
- dismutase
-
deoxynucleotidyl
- erk
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neurotoxicity
- artery
- cyclin
- cerebral
- dutp
- malondialdehyde
-
reperfusion
- infarct
- nick
- cardiac
- sirna
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apoptosis-inducing
- myocardial
- gsh
- cardiomyocytes
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sham
- c-jun
- cisplatin
- survivin
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transferase-mediated
- iodide
- hippocampal
- adp-ribose
-
hoechst
-
antiproliferative
-
caspase-dependent
-
polyadp-ribose
- bid
-
ischemia-reperfusion
- propidium
-
ladder
- analysis
- drug development
- molecular biology
- medicine
- diagnostics
Reaction
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position =
Synonyms
apopain, C14.003, Cas-3, CASP-3, CASP3, caspase 3, caspase-3, CgCaspase-3, CPP-32, CPP32, CPP32/apopain, cystein aspartic-specific protease-3, cysteine aspartic acid-specific protease, cysteine protease CPP32, DEVDase, IRP, Lyccasp3, Mncaspase-3c, More, SBTc-3, SCA-1, SREBP cleavage activity 1, Yama protein, Yama/CPP32, ZCASP3
ECTree
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analysis
diagnostics
drug development
medicine
molecular biology
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engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-3, overview
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cell-permeable substrate N-acetyl-L-Asp-L-Glu-L-Val-L-Asp-NĀ-morpholinecarbonyl-rhodamine 110, high turnover rate and sensitivity both in enzyme solution and in living cells
analysis
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the highly cell-permeable caspase-3 substrate is obtained by linking a fluorogenic DNA-binding dye to the caspase-3 recognition sequence that renders the dye nonfunctional. On substrate cleavage, the dye is released and becomes highly fluorescent on binding to DNA. DEVD-NucView488 detects caspase-3 activation within a live-cell population much earlier and with higher sensitivity compared with other apoptosis reagents. Cells incubated with DEVD-NucView488 exhibit no toxicity and normal apoptotic progression. DEVD-NucView488 is an ideal substrate for kinetic studies of caspase-3 activation because it detects caspase-3 activity in real-time and also efficiently labels DNA in nuclei of caspase-3-activated cells for real-time fluorescent visualization of apoptotic morphology
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a simple biochemical assay of caspase-3 activity in blood, may be useful for predicting the disposition of drugs that undergo extensive conjugation and biliary elimination like silymarin in patients with liver disease, caspase-3 activity correlates with the amount of silymarin conjugates, e.g. silychristin and silybin A and B, and is 5fold higher in the HCV cirrhosis cohort, overview
diagnostics
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active caspase-3 immunostaining is considered as a highly reliable and specific morphological marker of early apoptosis
diagnostics
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caspase-3 activity is a marker for apoptosis in gut epithelium, leading to impairment of the gastrointestinal mucosal barrier, that contributes to progression of HIV infection, immunohistochemical staining of cleaved caspase-3, overview
diagnostics
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caspase-3 activity is a marker for cell death, e.g. in microglia, overview
diagnostics
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caspase-3 is a helpful indicator of apoptosis induction, e.g. in mammary carcinomas
diagnostics
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caspase-3 is a marker for apoptosis, e.g. useful in patients with urothelial carcinoma of the upper urinary tract, overview
diagnostics
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caspase-3 is a marker of apoptotic cell death in embryonic fibroblasts, NIH-3T3 and WST-1 cells
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the VHH proteins, isolated from heavy chain antibody variable domain, i.e. VHH phage display library, are antagonist and agonist of apoptosis and could have potential for the development of therapeutics for neurodegenerative diseases and cancer, respectively
drug development
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caspase-3 ia a target for structure-based drug design approach
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during glutamte-induced apoptotic cell death, at least two mechanisms are involved: a caspase-3-dependent pathway and an enzyme-independent pathway using calpain and apoptosis inducing factor
medicine
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during glutamte-induced apoptotic cell death, glutamate induces activation of calpain, enzyme and translocation of mitochondrial apoptosis inducing factor AIF to cytosol and nuclei. These processes are inhibited/reversed by 17beta-estradiol and DELTA8,17beta-estradiol with the latter being more potent
medicine
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in macrophages from arteriosclerotic carotid artery, presence of proapoptotic markers such as enzyme, poly(ADP-ribose) polymerase, apoptosis-inducing factor, c-Jun/AP-1, and proinflammatory markers such as macrophage migration inhibitory factor and cyclooxygenase-2. Colocalization of proapoptic markers and proinflammatory markers and oxidized low-density lipoproteins
medicine
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induction of apoptosis with mitomycin-c in presence or absence of general caspase inhibitor benzoyl-Val-Ala-Asp-fluoromethylketone. Benzoyl-Val-Ala-Asp-fluoromethylketone prevents mitomycin-c-induced cell death. In contrast, specific inhibition of enzyme or caspase-7 in presence of mitomycin-c induces necrotic-like or paraptotic-like morphological changes but does not prevent cell death
medicine
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PANDER-induced downregulation of cyclin-dependent kinase inhibitor 1A expression coupled with induced CASP3-activation may serve a central role in islet cell death and offers further insight into the mechanisms of cytokine-induced beta-cell apoptosis
medicine
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caspase 3-dependent apoptosis contributes to the pathogenesis of lethal West Nile virus encephalitis and suggests possible novel therapeutic targets to restrict injury of central nervous system
medicine
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geldanamycin limits caspase-3 expression and protects from organ injury by suppressing inducible nitric oxide synthase expression and apoptosome formation. Geldanamycin, therefore may prove useful as an adjuvant in fluids used to treat patients suffering blood loss
medicine
light-activated caspase-3 can be used for precise ablation of neurons in vivo
medicine
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PANDER-induced downregulation of cyclin-dependent kinase inhibitor 1A expression coupled with induced CASP3-activation may serve a central role in islet cell death and offers further insight into the mechanisms of cytokine-induced beta-cell apoptosis
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