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Caspase-8 Collaborates with Caspase-11 to Drive Tissue Damage and Execution of Endotoxic Shock

Author:
Manda, Pratyusha  Feng, Yanjun  Lyons, John D.  Berger, Scott B.  Otani, Shunsuke  DeLaney, Alexandra  Tharp, Gregory K.  Maner-Smith, Kristal  Burd, Eileen M.  Schaeffer, Michelle  Hoffman, Sandra  Capriotti, Carol  Roback, Linda  Young, Cedrick B.  Liang, Zhe  Ortlund, Eric A.  DiPaolo, Nelson C.  Bosinger, Steven  Bertin, John  Gough, Peter J.  Brodsky, Igor E.  Coopersmith, Craig M.  Shayakhmetov, Dmitry M.  Mocarski, Edward S.  


Journal:
IMMUNITY


Issue Date:
2018


Abstract(summary):

The execution of shock following high dose E. coli lipopolysaccharide (LPS) or bacterial sepsis in mice required pro-apoptotic caspase-8 in addition to pro-pyroptotic caspase-11 and gasdermin D. Hematopoietic cells produced MyD88- and TRIF-dependent inflammatory cytokines sufficient to initiate shock without any contribution from cas pase-8 or caspase-11. Both proteases had to be present to support tumor necrosis factor- and interferon-beta-dependent tissue injury first observed in the small intestine and later in spleen and thymus. Caspase-11 enhanced the activation of caspase-8 and extrinsic cell death machinery within the lower small intestine. Neither caspase-8 nor caspase-11 was individually sufficient for shock. Both caspases collaborated to amplify inflammatory signals associated with tissue damage. Therefore, combined pyroptotic and apoptotic signaling mediated endotoxemia independently of RIPK1 kinase activity and RIPK3 function. These observations bring to light the relevance of tissue compartmentalization to disease processes in vivo where cytokines act in parallel to execute diverse cell death pathways.


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42---+


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