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Protease signalling in cell death: caspases versus cysteine cathepsins
1Department of Biochemistry, Molecular and Structural Biology, J. Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia. boris.turk@ijs.si
FEBS Letters
|June 5, 2007
Summary
Proteases are now recognized as signaling molecules, particularly in apoptosis. This review compares the roles of caspases and cysteine cathepsins in programmed cell death signaling pathways.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Proteases were historically viewed as solely protein-degrading enzymes.
- Recent research highlights proteases' crucial roles as signaling molecules.
- Apoptosis, or programmed cell death, is a key eukaryotic process for cell removal.
Purpose of the Study:
- To compare and discuss the roles of caspases and cysteine cathepsins in apoptosis signaling.
- To provide an updated perspective on protease functions in cell death.
Main Methods:
- Literature review comparing existing studies on caspases and cathepsins in apoptosis.
- Analysis of signaling pathways involving these protease families.
Main Results:
- Caspases have long been considered the primary proteases in apoptosis.
- Cysteine cathepsins are increasingly recognized for their significant involvement in apoptosis signaling.
- Both protease families play distinct yet interconnected roles in regulating programmed cell death.
Conclusions:
- The understanding of protease function has evolved beyond simple degradation.
- Caspases and cysteine cathepsins are both critical regulators of apoptosis.
- Further research is warranted to fully elucidate the complex interplay between these proteases in cell death.
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