Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization - PubMed (original) (raw)

. 2002 Aug 23;297(5585):1352-4.

doi: 10.1126/science.1074721.

Affiliations

• PMID: 12193789
• DOI: 10.1126/science.1074721

Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization

Patrice Lassus et al. Science. 2002.

Abstract

A current view is that cytotoxic stress, such as DNA damage, induces apoptosis by regulating the permeability of mitochondria. Mitochondria sequester several proteins that, if released, kill by activating caspases, the proteases that disassemble the cell. Cytokines activate caspases in a different way, by assembling receptor complexes that activate caspases directly; in this case, the subsequent mitochondrial permeabilization accelerates cell disassembly by amplifying caspase activity. We found that cytotoxic stress causes activation of caspase-2, and that this caspase is required for the permeabilization of mitochondria. Therefore, we argue that cytokine-induced and stress-induced apoptosis act through conceptually similar pathways in which mitochondria are amplifiers of caspase activity rather than initiators of caspase activation.

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Comment in

• Apoptosis. A cinderella caspase takes center stage.
  Kumar S, Vaux DL. Kumar S, et al. Science. 2002 Aug 23;297(5585):1290-1. doi: 10.1126/science.1076118. Science. 2002. PMID: 12193776 No abstract available.

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