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Measuring Apoptosis: Caspase Inhibitors and Activity Assays

MCSTAY, Gavin and Green, D. R. (2014) Measuring Apoptosis: Caspase Inhibitors and Activity Assays. Cold Spring Harbor Protocols, 2014 (8). pdb.top070359-pdb.top070359. ISSN 1559-6095

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Abstract or description

Caspases are proteases that initiate and execute apoptotic cell death. These caspase-dependent events are caused by cleavage of specific substrates that propagate the proapoptotic signal. A number of techniques have been developed to follow caspase activity in vitro and from apoptotic cellular extracts. Many of these techniques use molecules that are based on optimal peptide motifs for each caspase and on our understanding of caspase cleavage events that occur during apoptosis. Although these approaches are useful, there are several drawbacks associated with them. The optimal peptide motifs are not unique recognition sites for each caspase, so techniques that use them may yield information about more than one caspase. Furthermore, caspase cleavage does not take into account the different caspase activation mechanisms. Recently, probes having greater specificity for individual caspases have been developed and are being used successfully. This introduction provides background on the various caspases and introduces a set of complementary techniques to examine the activity, substrate specificity, and activation status of caspases from in vitro or cell culture experiments.

Item Type: Article
Faculty: School of Life Sciences and Education > Biological Sciences
Depositing User: Gavin MCSTAY
Date Deposited: 11 May 2018 13:19
Last Modified: 11 May 2018 13:20
URI: http://eprints.staffs.ac.uk/id/eprint/4347

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