EC Number   |
Activating Compound |
Reference |
|---|
   3.4.22.61 | 6'-benzyloxy-4-bromo-2'-hydroxychalcone |
compound displays potent cytotoxic properties against human leukaemia cells U-937, HL-60, K-562, NALM-6 and MOLT-3. Application results in significant activation of caspase-8 after 24 h of treatment |
753244 |
| 3.4.22.61 | actinomycin D |
significantly activates caspase-8 |
695622 |
| 3.4.22.61 | CD95 |
FLICE is the first in a cascade of ICE-like proteases activated by CD95. This activation requires a functional CD95 disc |
647446 |
| 3.4.22.61 | cellular FLIP long form |
- |
665918 |
| 3.4.22.61 | complement factor 5a |
increases caspase-8 activity and expression level of procaspase-8, and increases caspase 8 homologue FLICE-inhibitory protein, cFLIP, activation, C5a stimulation initiated cFLIP cleavage, which increased the 43 kDa active fragment, overview |
698264 |
| 3.4.22.61 | edelfosine |
i.e. 1-O-octadecyl-2-O-methyl-racglycero-3-phosphocholine, an anti-tumor drug, induces activation of procaspase-8 in T-cell leukemia, specific inhibition of caspase-8 prevents the apoptotic response triggered by edelfosine, overview. The compound induces the generation of the so-called death-inducing signaling complex, DISC, made up of Fas/CD95, FADD, and procaspase-8, in lipid rafts |
700899 |
| 3.4.22.61 | Fas death domain |
FADD, activating caspase-8 via its death-effector domain, DED. FADD dimerizes on binding to Fas, a crucial event that greatly enhances both the FADD-Fas interaction and caspase-8 activation |
699692 |
| 3.4.22.61 | Fas-associated death domain protein-like interleukin-1-beta-converting enzyme-like inhibitory protein, long form |
FLIP L, results in a heterodimeric enzyme |
663939 |
| 3.4.22.61 | FLIPL protein |
a catalytically defective caspase-8 paralogue, can interact with caspase-8 to activate its catalytic function |
717282 |
| 3.4.22.61 | harmol |
i.e. 1-methyl-9H-beta-carbolin-7-ol, a natural beta-carboline plant alkaloid, induces caspase-8 activation |
695617 |
