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- W1963548438 abstract "The role of caspase-1 in inflammation has been studied intensely over recent years. However, the research of caspase-1 has remained difficult mainly due to the lack of sensitive and selective tools to monitor not only its abundance but also its activity. Here we present a bioluminescent activity-based probe (ABP) for caspase-1, developed by the Reverse Design concept, where chemically optimized protease inhibitors are turned into selective substrate ABPs. The probe exhibits excellent selectivity for caspase-1 and ∼1000-fold increase in sensitivity compared to available fluorogenic peptidic caspase-1 substrates. Moreover, we have been able to monitor and quantify specific caspase-1 activity directly in cell lysates. The activity correlated well with processing of prointerleukin-1β and prointerleukin-18 in phorbol 12-myristate 13-acetate (PMA)-stimulated cells. A detectable caspase-1 activity was present also in nonstimulated cells, consistent with processing of constitutively expressed prointerleukin-18." @default.
- W1963548438 created "2016-06-24" @default.
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- W1963548438 date "2010-09-01" @default.
- W1963548438 modified "2023-09-27" @default.
- W1963548438 title "Selective and Sensitive Monitoring of Caspase-1 Activity by a Novel Bioluminescent Activity-Based Probe" @default.
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- W1963548438 doi "https://doi.org/10.1016/j.chembiol.2010.07.011" @default.
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