AI Article Synopsis
- - Measuring general caspase activity and purifying recombinant caspases in the lab is straightforward, but identifying active caspases in living cells is more difficult due to the lack of specific tools.
- - Current small molecule substrates and inhibitors used in research often fail to precisely target caspase activity, making it hard to analyze the complex relationships in caspase pathways.
- - The text outlines procedures to identify active caspases in cell cultures, determine which cleave specific substrates, and offers recommendations for evaluating the activity of recombinant initiator caspases and their natural substrates.
Article Abstract
The measurement of general caspase activity and the quantification of purified recombinant caspases in vitro can be accomplished with relative ease. But the determination of which caspases are active in a cellular context is much more challenging. This is because commercially available small molecule substrates and inhibitors do not display sufficient specificity to dissect the complex interplay of caspase pathways. Here we describe procedures that can be used to validate which caspases are active in cell culture models and determine which caspases are responsible for specific cleavage events. We also recommend methods for working with recombinant initiator caspases in vitro and suggest ways to accurately assess the cleavage efficiency of natural caspase substrates.
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| http://dx.doi.org/10.1016/S0076-6879(08)01621-2 | DOI Listing |
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