EC Number   |
Substrates |
Products  |
Reversibility |
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   3.4.22.64 | more |
caspase-11 plays a crucial role in both inflammation and apoptosis. Caspase-11 not only activates caspase-1, that is required for the maturation of proinflammatory cytokines such as interleukin (IL)-1 and IL-18, but also activates caspase-3, leading to cellular apoptosis under pathological conditions. The expression of caspase-11 is strongly induced at both mRNA and protein levels by inflammatory stimuli such as lipopolysaccharide, interferon-Q Q, and tumor necrosis factor-K K in C6 rat glial cells as well as primary astrocytes. Induction of caspase-11 by LPS in astrocytes is mediated through the p38 MAPK pathway. Inflammatory induction of caspase-11 in astrocytes may play an important role in both inflammatory responses involving these cells and auto-regulatory apoptosis of activated astrocytes in inflammatory sites |
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| 3.4.22.64 | more |
caspase-11 has a regulatory role in ethanol-induced apoptosis. Suppression of caspase-11 expression may be a mechanism by which Scutellariae radix (Chinese herbal medicine) exerts its cytoprotective effect |
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| 3.4.22.64 | more |
caspase-11 may be a central regulator of multiple events, including cell migration, cytokine maturation and apoptosis, during inflammation responses. Caspase-11 interacts physically and functionally with actin interacting protein 1, an activator of cofilin-mediated actin depolymerization. Caspase-11 and actin interacting protein 1 work cooperatively to promote cofilin-mediated actin depolymerization |
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| 3.4.22.64 | more |
a pathway modulating inflammatory-cell migration involve caspase-11 and actin interacting protein 1 |
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| 3.4.22.64 | more |
Flightless-I regulates the subcellular distribution of caspase-11 by promoting its localization at the cell leading edge |
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| 3.4.22.64 | more |
other caspases are substrates of caspase-11 |
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| 3.4.22.64 | more |
dimerised caspase-11 cannot cleave pro-interleukin-1beta of either species, mouse or human |
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| 3.4.22.64 | more |
mouse caspase-11 cannot cleave IL-1beta efficiently |
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| 3.4.22.64 | more |
mouse caspase-11 has an inadequate capacity to cleave pro-IL-1beta. It cleaves gasdermin D more efficiently than pro-IL-1beta |
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| 3.4.22.64 | mouse interleukin-18 + H2O |
low activity |
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