Cell Stress-Associated Caspase Activation: Intrinsically Complex?

Sci. STKE, 25 March 2003
Vol. 2003, Issue 175, p. pe11
DOI: 10.1126/stke.2003.175.pe11

Cell Stress-Associated Caspase Activation: Intrinsically Complex?

  1. Emma M. Creagh and
  2. Seamus J. Martin*
  1. Molecular Cell Biology Laboratory, Department of Genetics, The Smurfit Institute, Trinity College, Dublin 2, Ireland.
  1. *Corresponding author: E-mail: martinsj{at}tcd.ie


Apoptosis, or programmed cell death, involves the activation of the caspases, a family of cysteine proteases that coordinate the process of cellular demolition. In the intrinsic--or mitochondrial--pathway to apoptosis, which is initiated in response to various types of cell stress, the prevailing view is that caspases become activated in a structure called the apoptosome after cytochrome c is released from the mitochondria. However, recent research challenges this view and suggests that one or more caspases are activated before mitochondrial release of cytochrome c and that the apoptosome acts as an amplifier, rather than as an initiator, of apoptosis-associated caspase activation. Here, we critically discuss the evidence in support of the latter view and suggest that revision of the established pathway may be premature.


E. M. Creagh and S. J. Martin, Cell Stress-Associated Caspase Activation: Intrinsically Complex?. Sci. STKE 2003, pe11 (2003).

Migrate, Differentiate, Proliferate, or Die: Pleiotropic Functions of an Apical "Apoptotic Caspase"
S. Kumar
Sci Signal 2004, pe49-pe49 (12 October 2004)

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