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Literature summary for 3.4.22.64 extracted from

  • Agnew, A.; Nulty, C.; Creagh, E.M.
    Regulation, activation and function of caspase-11 during health and disease (2021), Int. J. Mol. Sci., 22, 1506.
    View publication on PubMed
Search for more literature for 3.4.22.64

Activating Compound

Activating Compound Comment Organism Structure
LPS caspase-11 is an essential endogenous receptor for LPS, which binds to the CARD domain of caspase-11 through its lipid A tail moiety to regulate caspase-11 activation, overview Mus musculus
oxidized phospholipids interact with caspase-11 by binding to the CARD domain, high doses induce caspase-11 oligomerization and activation Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
gene Casp4, the murine inflammatory caspases genes are located on syntenic regions of mouse chromosome 9A1 Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
L-adrenaline inhibits of caspase-11 activation via activated PKA that facilitates caspase-11 phosphorylation Mus musculus
oxidized phospholipids interact with caspase-11 by binding to the CARD domain, low doses compete with LPS and inhibit caspase-11 activation Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus P70343 cf. caspase-4, EC 3.4.22.57
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein L-adrenaline binds ADRA2B, activating PKA. Activated PKA facilitates caspase-11 phosphorylation Mus musculus
proteolytic modification caspases are expressed in most cells as inactive monomeric zymogens (pro-caspases), requiring processing and heterodimerization to facilitate their activation. Caspase-11 auto-proteolysis is essential for its activation and the subsequent regulation of downstream events. Caspase-11 activation, induced experimentally via its overexpression or cytoplasmic LPS stimulation, induces two autoproteolysis events, resulting in the removal of the N-terminal CARD domain from the large subunit and separating the large and small catalytic domains Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
colon
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 Mus musculus
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epithelial cell
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 Mus musculus
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intestine
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 Mus musculus
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Subunits

Subunits Comment Organism
dimer caspases are expressed in most cells as inactive monomeric zymogens (pro-caspases), requiring processing and heterodimerization to facilitate their activation Mus musculus

Expression

Organism Comment Expression
Mus musculus caspase-11 expression is stimulated by TLR signaling, IL-1 signaling, mitochondrial DNA damage, the complement pathway, and IFN signaling involving receptors TLR2, TLR3, TLR4, TLR5, ILR9, IL-1R, mtDNA, C3aR, IFNAR, and IFNGR: The responsible stimulators of the receptors are Pam3CSK4, dsRNA, LPS, flagellin, CpG-rich DNA, interleukin-1beta, c-Gas-STING, C3a, and IFNalpha/beta. Involved pathways and regulation mechanisms, detailed overview up

General Information

General Information Comment Organism
evolution caspases-4 and -5 are the human orthologues of murine caspase-11, sharing with it 68% and 47% amino acid sequence identity, respectively Mus musculus
malfunction the increased susceptibility of caspase-11 deficient mice to colitis-associated carcinogenesis (CAC) is associated with decreased STAT1 activity, identifying an anti-tumor role for caspase-11 during CAC via its ability to provide positive enhance STAT1 activation. Casp-11-/- intestinal epithelial cells (IECs) are significantly more susceptible to CAC than wild-type IECs. Colons from CAC-treated Casp-11-/- mice have increased expression of proteins associated with early-stage angiogenesis, suggesting that caspase-11 may have a role in inflammation- and cancer-associated angiogenesis. Caspase-11 activation is significantly impaired in GBPchro3-deficient macrophages Mus musculus
metabolism IRGMs are involved in regulating vacuole/lysosome stability and regulate caspase-11 activity, as well as HMGB1, that binds LPS, entering macrophages/endothelial cells via RAGE-mediated endocytosis, promoting lysosomal rupture and LPS release. Another cytokine that acts as a major regulator of caspase-11 expression is IFN-gamma Mus musculus
additional information the enzymatic activity of caspases is ruled by a dominant specificity for aspartic acid containing proteins and a cysteine side chain that acts as a catalytic nucleophile to employ peptide cleavage. Caspase-11 structure analysis and comparison Mus musculus
physiological function caspase-11 is an essential endogenous receptor for LPS, which binds to the CARD domain of caspase-11 through its lipid A tail moiety to regulate caspase-11 activation. Caspase-11 upregulation occurs as a result of PAMP and/or cytokine signaling and can be amplified by complement signaling Mus musculus