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Caspases

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...

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Related Experiment Video

Updated: May 2, 2026

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

Caspase protocols in Caenorhabditis elegans.

Eui Seung Lee¹, Ding Xue

¹Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO, USA.

Methods in Molecular Biology (Clifton, N.J.)

|February 26, 2014

Summary

This summary is machine-generated.

Researchers purified active CED-3 caspase from Caenorhabditis elegans and developed in vitro assays. These methods identify CED-3 substrates and cleavage sites, crucial for understanding programmed cell death.

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Area of Science:

Molecular Biology
Genetics
Cell Biology

Background:

The Caenorhabditis elegans genome contains four caspase-like genes, including CED-3, a key cell-killing caspase.
CED-3 plays a central role in the conserved apoptotic pathway, providing insights into mammalian and metazoan apoptosis.
Understanding CED-3 substrates is vital for connecting its activation to downstream cell death events.

Purpose of the Study:

To describe a method for purifying active CED-3 caspase.
To outline in vitro assays for assessing CED-3 proteolytic activity.
To identify potential CED-3 substrates and their cleavage sites.

Main Methods:

Purification of active CED-3 caspase from C. elegans.
In vitro enzymatic assays to determine proteolytic activity.
Analysis of protein cleavage by CED-3 to identify substrates and cleavage sites.

Main Results:

Successful purification of active CED-3 caspase.
Established in vitro assays for CED-3 activity and substrate identification.
Demonstrated the utility of in vitro cleavage assays for predicting in vivo substrates.

Conclusions:

The described methods enable the purification and characterization of active CED-3 caspase.
These techniques are essential for identifying CED-3 substrates and understanding programmed cell death execution.
This work facilitates further research into the conserved apoptotic pathways.