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Inhibition of caspase activity induces a switch from apoptosis to necrosis

C Lemaire1, K Andréau, V Souvannavong

  • 1Institut de Biochimie, CNRS ERS 0571, Université Paris-Sud, Orsay, France. christophe.lemaire@bbmpc.u-psud.fr

FEBS Letters
|April 29, 1998
PubMed

Insights

Caspase inhibitors blocked B cell apoptosis but led to necrosis, suggesting shared pathways. Active caspases determine cell death type, impacting lymphocyte survival.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Caspases are key mediators of programmed cell death (apoptosis).
  • B lymphocytes undergo apoptosis as a critical process in immune regulation.
  • The precise role of caspases in determining cell death pathways (apoptosis vs. necrosis) in B cells requires further elucidation.

Purpose of the Study:

  • To investigate the role of caspases in B lymphocyte cell death.
  • To determine if caspase inhibition alters the mode of cell death from apoptosis to necrosis.
  • To explore the relationship between caspase activity and cell death pathways.

Main Methods:

  • Utilized broad-spectrum caspase inhibitors (Z-Asp-cmk and Z-VAD-fmk) in B lymphocyte cultures.
  • Assessed spontaneous and drug-induced apoptosis.
  • Measured CPP32/caspase-3-like activity in apoptotic cells.
  • Observed cell survival and death morphology (apoptosis vs. necrosis).

Main Results:

  • Caspase inhibitors completely prevented spontaneous and drug-induced apoptosis in B lymphocytes.
  • Inhibitors suppressed CPP32/caspase-3-like activity.
  • Suppression of apoptosis resulted in a switch to necrotic cell death, not increased survival.
  • Necrotic cell death was observed instead of apoptosis upon caspase inhibition.

Conclusions:

  • Caspase activity is essential for executing apoptosis in B lymphocytes.
  • Apoptosis and necrosis share common initiation pathways in B cells.
  • The presence of active caspases dictates whether a cell undergoes apoptosis or necrosis.

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