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Mammalian caspases: structure, activation, substrates, and functions during apoptosis
W C Earnshaw1, L M Martins, S H Kaufmann
1Institute of Cell and Molecular Biology, University of Edinburgh, Scotland, United Kingdom. bill.earnshaw@ed.ac.uk
Annual Review of Biochemistry
|June 29, 2000
Summary
Apoptosis, a programmed cell death, is executed by caspases, a family of proteases. These proteases are tightly regulated at multiple levels to control cell death pathways.
Area of Science:
- Cell Biology
- Biochemistry
Background:
- Apoptosis is a crucial genetically programmed cell death process.
- Proteases, particularly caspases, are key mediators in apoptosis initiation and execution.
Purpose of the Study:
- To elucidate the critical roles of proteases, specifically caspases, in the process of apoptosis.
- To detail the mechanisms regulating caspase activation and activity.
Main Methods:
- Review of studies on protease involvement in apoptosis over the past decade.
- Analysis of caspase synthesis, activation cascades, and regulatory mechanisms.
Main Results:
- Caspases, cysteine-dependent aspartate-directed proteases, are central to apoptosis.
- Caspase activation is regulated by gene transcription, Bcl-2 family proteins, and inhibitor of apoptosis proteins (cIAPs).
- Activated caspases cleave vital intracellular proteins, disrupting cell survival and architecture.
Conclusions:
- Caspase regulation is multifaceted, involving transcriptional control and inhibitory proteins.
- Caspase-mediated proteolysis is essential for the morphological and biochemical hallmarks of apoptotic cell death.