ABSTRACT
Protocol 9.3: Detection of active caspases or cleaved caspase substrates in individual cells by immunostaining
9.5 Use of cell-free extracts as a source of cytochrome cinducible active caspases and caspase substrates
Protocol 9.4: Use of cell-free extracts as a source of cytochrome c-inducible active caspases and caspase substrates
9.6 Use of radiolabelled caspases or caspase substrates as a readout of caspase activity
Protocol 9.5: Use of radiolabelled caspases or caspase substrates to detect caspase activity
9.7 Measurement of caspase activity using fluorogenic/ colorimetric substrate peptides
Protocol 9.6: Measurement of caspase activity using fluorogenic/ colorimetric substrate peptides
9.8 References 257
9.1 Introduction
The caspases (cysteinyl aspartate-specific proteases) are a group of proteolytic enzymes that were first implicated in programmed cell death through analysis of cell death-defective mutants of the nematode worm Caenorhabditis elegans. The C. elegans caspase, CED-3, is essential for all developmental-related programmed cell deaths in the nematode [1]. A large family of mammalian CED-3-related proteases (the caspases) has now been identified and many of these play important roles in apoptosis.
