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Related Experiment Videos

Caspase activity is not sufficient to execute cell death.

Dunja Lukovic1, Akira Komoriya, Beverly Z Packard

  • 1Department of Microbiology and Immunology, University of Illinois College of Medicine, Chicago, IL 60612, USA.

Experimental Cell Research
|September 23, 2003
PubMed
Summary

Caspase activation is necessary but not sufficient for physiological cell death. Blocking caspase-dependent cyclin-dependent kinase 2 (Cdk2) activity spares cells from death, indicating commitment occurs after caspase activation.

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Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Effector caspases are critical in physiological cell death pathways.
  • Diverse death signals converge to activate caspases post-translationally.
  • Caspase substrates include proteins vital for cellular homeostasis.

Purpose of the Study:

  • To investigate whether caspase activation is the irreversible commitment point in cell death.
  • To determine if caspase activity alone is sufficient to cause cell death.
  • To explore the role of caspase-dependent cyclin-dependent kinase 2 (Cdk2) activity in cell death.

Main Methods:

  • Direct cytofluorimetric analysis of intracellular caspase activity.
  • Colony forming assays.
  • Transient blockade of caspase-dependent Cdk2 activity.

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Main Results:

  • Transient blockade of caspase-dependent Cdk2 activity conferred long-lived sparing from death.
  • Cells triggered to die were fully replete with caspase activity.
  • Caspase activation was necessary but not sufficient for cell lethality.

Conclusions:

  • Caspase activation does not represent the irreversible commitment point to physiological cell death.
  • Further downstream events, such as Cdk2 activity, are required for cell death execution.
  • Cell death involves more than simple proteolytic destruction; it has regulatory aspects.