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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.

Trends in Biochemical Sciences
|August 1, 1997
PubMed
Summary
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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.

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  • 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.