Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice

Maya Saleh, John C. Mathison, Melissa K. Wolinski, Steve J. Bensinger, Patrick Fitzgerald, Nathalie Droin, Richard J. Ulevitch, Douglas R. Green () and Donald W. Nicholson ()
Additional contact information
Maya Saleh: La Jolla Institute for Allergy and Immunology
John C. Mathison: The Scripps Research Institute
Melissa K. Wolinski: La Jolla Institute for Allergy and Immunology
Steve J. Bensinger: La Jolla Institute for Allergy and Immunology
Patrick Fitzgerald: La Jolla Institute for Allergy and Immunology
Nathalie Droin: La Jolla Institute for Allergy and Immunology
Richard J. Ulevitch: The Scripps Research Institute
Douglas R. Green: La Jolla Institute for Allergy and Immunology
Donald W. Nicholson: Merck Research Laboratories

Nature, 2006, vol. 440, issue 7087, 1064-1068

Abstract: Sepsis target Proteases of the caspase family not only help cells to die (by apoptosis) but also process inflammatory cytokines. Caspase-12 has now been found to inhibit caspase-1, diminishing the production of pro-inflammatory cytokines. Mice lacking caspase-12 are therefore better able to combat bacteria than normal mice and become resistant to peritonitis and septic shock. This makes caspase-12 a potential drug target in the treatment of sepsis.

Date: 2006
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DOI: 10.1038/nature04656

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