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

PERSPECTIVES

Cell Stress-Associated Caspase Activation: Intrinsically Complex?

Emma M. Creagh and Seamus J. Martin*

Molecular Cell Biology Laboratory, Department of Genetics, The Smurfit Institute, Trinity College, Dublin 2, Ireland.

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.

*Corresponding author: E-mail: martinsj{at}tcd.ie

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

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Migrate, Differentiate, Proliferate, or Die: Pleiotropic Functions of an Apical "Apoptotic Caspase".
S. Kumar (2004)
Sci. STKE 2004, pe49
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