Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


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?

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}

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

Read the Full Text

Migrate, Differentiate, Proliferate, or Die: Pleiotropic Functions of an Apical "Apoptotic Caspase".
S. Kumar (2004)
Sci. STKE 2004, pe49
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882