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

Abstract

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.

Citation:

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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