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Literature summary for 3.4.24.83 extracted from
- Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin (2008), Cell. Microbiol., 10, 2434-2446.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | the in vitro effects of thermal stress on the killing of murine macrophages by anthrax lethal toxin are investigated. Heat shock rapidly halts anthrax lethal toxin-induced cell death without any impact on toxin uptake or mitogen-activated protein kinases cleavage, by a mechanism independent of novel protein synthesis, p38 activation, HSP90 activity or proteasome inhibition. Rather, heat shock prevents the activation of procaspase-1 in anthrax lethal toxin -treated cells, apparently by the sequestration of pro-caspase-1 in a large, inhibitory complex. Heat-shocked cell lysates strongly inhibit the active caspase-1 heterotetramer in vitro, independent of a specific inflammasome platform. Results suggest the presence of a cellular, heat shock-inducible, caspase-1 inhibiting factor | Bacillus anthracis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| anthrax lethal toxin | - |
Bacillus anthracis |
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