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Literature summary for 3.4.22.64 extracted from

  • Lu, Y.; Meng, R.; Wang, X.; Xu, Y.; Tang, Y.; Wu, J.; Xue, Q.; Yu, S.; Duan, M.; Shan, D.; Wang, Q.; Wang, H.; Billiar, T.R.; Xiao, X.; Chen, F.; Lu, B.
    Caspase-11 signaling enhances graft-versus-host disease (2019), Nat. Commun., 10, 4044.
    View publication on PubMed
Search for more literature for 3.4.22.64

Activating Compound

Activating Compound Comment Organism Structure
lipopolysaccharide activation by intracellular LPS leading to caspase-11 oligomerizes into protein complexes and enzymatic cleavage of gasdermin D (GSDMD) into pore-forming peptides. Recognition of LPS by caspase-11 requires guanylate-binding proteins (GBPs). LPS-caspase-11 interaction in the intestinal epithelium is not observed when GBPchr3 KO (knockout) mice, which lack GBP1, 2, 3, 5, and 7, are used as HSCT recipients Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information lipopolysaccharide (LPS)-caspase-11 interaction enhances graft-versus-host disease (GVHD) in allogeneic hematopoietic stem cell transplantation (allo-HSCT). Caspase-11 enhances donor T cell expansion in allo-HSCT Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mus musculus 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
gasdermin D + H2O Mus musculus cleavage of gasdermin D (GSDMD) into pore-forming peptides ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P70343 cf. caspase-4, EC 3.4.22.57; C57BL/6 and and BALB/c mice
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Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
 Mus musculus
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intestine
-
 Mus musculus
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lymphocyte intraepithelial lymphocytes, and intestinal lamia propria lymphocytes Mus musculus
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macrophage
-
 Mus musculus
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neutrophil
-
 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gasdermin D + H2O cleavage of gasdermin D (GSDMD) into pore-forming peptides Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
caspase-11
-
 Mus musculus

General Information

General Information Comment Organism
malfunction deletion of caspase-11 or Gsdmd, inhibition of LPS-caspase-11 interaction, or neutralizing IL-1alpha uniformly reduces intestinal inflammation, tissue damage, donor T cell expansion, and mortality in allo-HSCT. Importantly, Caspase-11 deficiency does not decrease the graft-versus-leukemia (GVL) activity, which is essential to prevent cancer relapse. Caspase-11 deficiency preserves GVL activity, overview. Loss of caspase-11 renders mice susceptible to Burkholderia pseudomallei, a Gram-negative bacterium. Neutralizing IL-1alpha attenuates GVHD. Overactivation of caspase-11 in endotoxemia or polymicrobial sepsis leads to organ injury and lethality. Dysregulated activation of caspase-11 also contributes to the pathogenesis of age-related macular degeneration Mus musculus
metabolism caspase-11 is a cytosolic LPS receptor that senses various Gram-negative bacteria infections. Caspase-11 enhances GVHD through gasdermin D (GSDMD). GSDMD is a caspase-11 substrate that directly triggers pyroptosis Mus musculus
physiological function caspase-11 is a cytosolic LPS receptor that senses various Gram-negative bacteria infections. Caspase-11 is the cytosolic receptor for bacterial endotoxin (lipopolysaccharide, LPS). Caspase-11 signaling enhances graft-versus-host disease (GVHD). Allogeneic hematopoietic stem cell transplantation (allo-HSCT) markedly increases the LPS-caspase-11 interaction, leading to the cleavage of gasdermin D (GSDMD). Caspase-11 and GSDMD mediate the release of interleukin-1alpha (IL-1alpha) in allo-HSCT. Upon activation by intracellular LPS, caspase-11 oligomerizes into protein complexes and enzymatically cleaves gasdermin D (GSDMD) into pore-forming peptides, leading to a lytic form of cell death, termed pyroptosis. This process destroys the intracellular niche for microbes and triggers inflammation by releasing alarmins, such as IL-1alpha Mus musculus