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

Nat Chem Biol. 2012 Sep;8(9):745-7. doi: 10.1038/nchembio.1023. Epub 2012 Jul 15.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Apoptosis*
  • Caspase 1 / metabolism*
  • Enzyme Activation
  • Macrophages / cytology*
  • Mice
  • Salmonella Infections / enzymology*
  • Salmonella Infections / pathology*

Substances

  • Caspase 1