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Caspases and apoptosis

Guy S Salvesen1

  • 1Program in Apoptosis and Cell Death Research, Burnham Institute, La Jolla, CA 92037, USA. gsalvesen@burnham.org

Essays in Biochemistry
|December 5, 2002
PubMed

Insights

Programmed cell death, or apoptosis, is essential for development and survival. Caspases, a family of proteases, mediate this process and also activate inflammatory cytokines in vertebrates.

Area of Science:

  • Cell biology
  • Biochemistry
  • Immunology

Background:

  • Programmed cell death (apoptosis) is crucial for metazoan development and adult survival.
  • Apoptosis involves the ordered dismantling of cells, with fragments removed by phagocytosis.
  • This process is regulated by caspases, a family of cysteine proteases.

Purpose of the Study:

  • To elucidate the role of caspases in programmed cell death.
  • To understand the dual function of caspases in apoptosis and inflammatory signaling.

Main Methods:

  • Analysis of caspase activation following apoptotic stimuli.
  • Identification of caspase substrates involved in apoptotic morphology.
  • Investigation of caspase involvement in pro-inflammatory cytokine activation in vertebrates.

Main Results:

  • Caspase activation leads to characteristic apoptotic morphology through limited protein cleavage.
  • A subset of caspases in vertebrates participates in pro-inflammatory cytokine activation.
  • Caspases mediate distinct intracellular signaling pathways.

Conclusions:

  • Caspases are key mediators of apoptosis, ensuring cellular integrity during programmed cell death.
  • Vertebrate caspases play a dual role, regulating both cell death and inflammatory responses.
  • Understanding caspase pathways is vital for comprehending cellular homeostasis and immune function.

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