Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection.
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.
Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, USA.
Aaron W
AW
Puri
Petr
P
Broz
Aimee
A
Shen
Denise M
DM
Monack
Matthew
M
Bogyo
D000818:Animals; D017209:Apoptosis; D020170:Caspase 1 / Q000378:metabolism*; D004789:Enzyme Activation; D008264:Macrophages / Q000166:cytology*; D051379:Mice; D012480:Salmonella Infections / Q000201:enzymology* / Q000473:pathology*
D020170:Caspase 1