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Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3.

Mammalian caspases are a family of cysteine proteases that plays a critical role in apoptosis. We have analyzed caspase-2 processing in human cell lines containing defined mutations in caspase-3 and caspase-9. Here we demonstrate that caspase-2 processing, during cell death induced by UV irradiation, depends both on caspase-9 and caspase-3 activity, while, during TNF-alpha-dependent apoptosis, capase-2 processing is independent of caspase-9 but still requires caspase-3. In vitro procaspase-2 is the preferred caspase cleaved by caspase-3, while caspase-7 cleaves procaspase-2 with reduced efficiency. We have also demonstrated that caspase-2-mediated apoptosis requires caspase-9 and that cells co-expressing caspase-2 and a dominant negative form of caspase-9 are impaired in activating a normal apoptotic response and release cytochrome c into the cytoplasm. Our findings suggest a role played by caspase-2 as a regulator of the mitochondrial integrity and open questions on the mechanisms responsible for its activation during cell death.

Pubmed ID: 11399776


  • Paroni G
  • Henderson C
  • Schneider C
  • Brancolini C


The Journal of biological chemistry

Publication Data

June 15, 2001

Associated Grants


Mesh Terms

  • Amino Acid Substitution
  • Animals
  • Apoptosis
  • Caspase 2
  • Caspase 3
  • Caspase 7
  • Caspase 9
  • Caspases
  • Cell Death
  • Cell Line
  • Female
  • Fibroblasts
  • Fluorescent Antibody Technique, Indirect
  • Gene Expression Regulation, Enzymologic
  • Gene Library
  • Humans
  • Mammals
  • Mutagenesis, Site-Directed
  • Recombinant Proteins
  • Transfection
  • Tumor Necrosis Factor-alpha
  • Ultraviolet Rays