Severe Sepsis Clinical Trial
Official title:
Characterization of Non-canonical Way in Inflammasome Monocytes of Patients With Severe Sepsis
Activation of caspase-4 and human caspase-5 (orthologs of caspase-11 in mice) in innate immune cells.
Lipopolysaccharide (LPS) of the wall of Gram-negative bacteria is one of pathogen associated
molecular patterns (PAMPs), which are recognized by cells of the innate immune system via
Toll-like receptor 4 (TLR4) . The LPS / TLR4 interaction induces the secretion of a variety
of proinflammatory cytokines. Among them, interleukin-1β (IL-1β) is a major cytokine, and
alterations to its secretion has been associated with various diseases, such as periodic
syndrome associated cryopyrin (CAPS), gout, rheumatoid arthritis or multiple sclerosis.
The release of IL-1β is controlled by a molecular platform protein, known as the
inflammasome name. The canonical protein (that is to say conserved in evolution) of the
inflammasome NLRP3 are NLRC4 and that engages the ASC adapter protein to activate caspase-1,
which promotes the cleavage of interleukin IL-1β. Gram-negative bacteria such as Escherichia
coli cause non-canonical activation of caspase-1, caspase-11In involving more NLRP3 and AUC.
In mouse, caspase-11 is essential to the immune response to gram-negative bacteria, but
bacterial PAMPs that are responsible for triggering of the non-canonical inflammasome remain
to be identified. It has recently been shown that caspase-11 is involved in the death of the
mice subjected to septic shock. The mouse model requires caspase-11-dependent mechanism,
caspase-independent -1 since the CASP1 - / - mouses are also susceptible to LPS as wild type
mice. A key question to be answered is whether LPS triggers similar events in human cells.
If this is the case, this knowledge may be useful in drug development for treatment of
sepsis.
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