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Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection.


ABSTRACT: Here we report AWP28, an activity-based probe that can be used to biochemically monitor caspase-1 activation in response to proinflammatory stimuli. Using AWP28, we show that apoptosis is triggered upon Salmonella enterica var. Typhimurium infection in primary mouse bone marrow macrophages lacking caspase-1. Furthermore, we report that upon Salmonella infection, inflammasome-mediated caspase-1 activity is required to bypass apoptosis in favor of proinflammatory pyroptotic cell death.

SUBMITTER: Puri AW 

PROVIDER: S-EPMC3461347 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection.

Puri Aaron W AW   Broz Petr P   Shen Aimee A   Monack Denise M DM   Bogyo Matthew M  

Nature chemical biology 20120715 9


Here we report AWP28, an activity-based probe that can be used to biochemically monitor caspase-1 activation in response to proinflammatory stimuli. Using AWP28, we show that apoptosis is triggered upon Salmonella enterica var. Typhimurium infection in primary mouse bone marrow macrophages lacking caspase-1. Furthermore, we report that upon Salmonella infection, inflammasome-mediated caspase-1 activity is required to bypass apoptosis in favor of proinflammatory pyroptotic cell death. ...[more]

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