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Literature summary for 3.4.22.36 extracted from

  • Fink, S.L.; Bergsbaken, T.; Cookson, B.T.
    Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms (2008), Proc. Natl. Acad. Sci. USA, 105, 4312-4317.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine ?
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine Mus musculus ?
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