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Related Experiment Videos

Caspase-14 is a novel developmentally regulated protease

S Hu1, S J Snipas, C Vincenz

  • 1Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.

The Journal of Biological Chemistry
|October 29, 1998
PubMed
Summary

A novel caspase, MICE (mini-interleukin-1 converting enzyme) or caspase-14, is highly expressed in embryonic tissues. Overexpression of MICE induces apoptosis, suggesting a unique role in cell death pathways.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Caspases are key cysteine proteases in apoptosis.
  • They possess a prodomain, large, and small catalytic subunit.
  • Interleukin-1 converting enzyme (ICE) is a related protease.

Purpose of the Study:

  • To characterize a novel caspase, MICE (caspase-14).
  • To investigate its expression pattern and functional associations.
  • To determine its role in apoptosis.

Main Methods:

  • Characterization of MICE (caspase-14) protein.
  • Analysis of caspase expression in embryonic and adult tissues.
  • Assessing MICE association with other caspases.
  • Investigating MICE processing by death stimuli.

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  • Overexpression studies in MCF7 breast cancer cells.

    • Main Results:

    • MICE has a short prodomain and is highly expressed in embryonic tissues, absent in adult tissues.
    • MICE preferentially associates with large prodomain caspases (caspase-1, -2, -4, -8, -10).
    • MICE is not processed by common death stimuli.
    • MICE overexpression induces apoptosis in MCF7 cells, inhibited by caspase inhibitors.

    Conclusions:

    • MICE (caspase-14) represents a novel caspase with a unique expression profile.
    • Its association patterns and resistance to processing suggest a distinct function.
    • MICE overexpression demonstrates its pro-apoptotic role, highlighting its significance in cell death.