|
Sci. STKE, 25 March 2003 PERSPECTIVESCell 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. Summary: 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). The editors suggest the following Related Resources on Science sites:In Science Signaling
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
|
Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
Magazine | News | Signaling | Careers | Multimedia | Collections | Help | Site Map | RSS
Subscribe | Feedback | Privacy / Legal | About Us | Advertise With Us | Contact Us
© 2003 American Association for the Advancement of Science. All Rights Reserved.
AAAS is a partner of HINARI, AGORA, PatientInform, CrossRef, and COUNTER.
You have reached the bottom of the page. Back to top