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ERICE, a novel FLICE-activatable caspase

E W Humke1, J Ni, V M Dixit

  • 1Department of Cellular and Molecular Biology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.

The Journal of Biological Chemistry
|June 23, 1998
PubMed
Summary
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Researchers identified a new caspase, ERICE (caspase-13), which triggers apoptosis in human cells. It is activated by caspase-8, suggesting a role in death receptor-mediated cell death pathways.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Programmed cell death (apoptosis) is vital for cellular homeostasis in metazoans.
  • The caspase protease family is crucial for apoptosis and inflammation.
  • Mammalian caspases are related to the nematode death protein CED-3.

Purpose of the Study:

  • To isolate and characterize a novel mammalian caspase.
  • To determine the phylogenetic relationship and subfamily of the new caspase.
  • To investigate the role of the new caspase in apoptosis and cell death pathways.

Main Methods:

  • Phylogenetic analysis to classify the new caspase.
  • Overexpression studies in 293 human embryonic kidney and MCF7 breast carcinoma cells.
  • Investigating activation by granzyme B and caspase-8.

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Main Results:

  • Isolation and characterization of ERICE (caspase-13).
  • ERICE belongs to the ICE subfamily of caspases.
  • ERICE overexpression induces apoptosis in human cell lines.
  • ERICE is not activated by granzyme B but is activated by caspase-8.

Conclusions:

  • ERICE (caspase-13) is a novel caspase involved in apoptosis.
  • ERICE likely participates in tumor necrosis factor receptor-initiated cell death pathways.
  • ERICE does not appear to be involved in granzyme B-mediated cell death.