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Caspases: killer proteases
D W Nicholson1, N A Thornberry
1Department of Biochemistry and Molecular Biology, Merck Frosst Centre for Therapeutic Research, Merck Frosst Canada Inc., Pointe Claire-Dorval, Quebec, Canada.
Abstract:
Caspases (cysteinyl aspartate-specific proteinases) mediate highly specific proteolytic cleavage events in dying cells, which collectively manifest the apoptotic phenotype. The key and central role that these enzymes play in a biochemical cell-suicide pathway has been conserved throughout the evolution of multicellular eukaryotes.
Insights
Caspases (cysteinyl aspartate-specific proteinases) are key enzymes in programmed cell death, or apoptosis. These proteases execute specific cleavage events, driving the cellular dismantling process conserved across multicellular life.
Area of Science:
- Biochemistry
- Cell Biology
- Evolutionary Biology
Background:
- Caspases are essential proteases that execute programmed cell death (apoptosis).
- These enzymes are critical for the characteristic biochemical and morphological changes observed in dying cells.
Purpose of the Study:
- To highlight the central role of caspases in apoptosis.
- To emphasize the evolutionary conservation of caspase function in multicellular eukaryotes.
Main Methods:
- Literature review of caspase function in apoptosis.
- Comparative analysis of caspase-mediated events across different species.
Main Results:
- Caspases mediate specific proteolytic cleavages during apoptosis.
- These proteolytic events are conserved throughout the evolution of multicellular organisms.
Conclusions:
- Caspases are indispensable executioners of the apoptotic pathway.
- The fundamental role of caspases in cell-suicide pathways is a conserved evolutionary trait.