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Related Experiment Videos

Granzyme A is an interleukin 1 beta-converting enzyme

M Irmler1, S Hertig, H R MacDonald

  • 1Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.

The Journal of Experimental Medicine
|May 1, 1995
PubMed
Summary

Cytotoxic T lymphocyte-mediated apoptosis involves granzyme A, which processes precursor interleukin-1 beta (pIL-1 beta). This granzyme A activity, distinct from granzyme B, generates biologically active IL-1 beta, potentially initiating local inflammation.

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Area of Science:

  • Cellular Biology
  • Immunology
  • Molecular Biology

Background:

  • Apoptosis regulation involves ced-3 in C. elegans and ICE in mammals.
  • Cytotoxic T lymphocytes induce apoptosis via granzymes A and B.
  • ICE and granzyme B process precursor IL-1 beta (pIL-1 beta) at specific aspartic acid sites.

Purpose of the Study:

  • To investigate the role of granzyme A in pIL-1 beta processing.
  • To determine if granzyme A generates biologically active IL-1 beta.
  • To understand the relationship between granzyme A, ICE, and apoptosis.

Main Methods:

  • Assessing pIL-1 beta conversion by granzyme A and B in vitro.
  • Mapping cleavage sites on pIL-1 beta.
  • Monitoring pIL-1 beta processing in activated macrophages attacked by cytotoxic T lymphocytes.

Related Experiment Videos

  • Inhibiting granzyme activity to block processing.

    • Main Results:

    • Granzyme A, but not granzyme B, converts pIL-1 beta to mature IL-1 beta.
    • Major cleavage by granzyme A occurs at Arg120, downstream of the ICE site.
    • Granzyme A-generated IL-1 beta is biologically active.
    • Intracellular pIL-1 beta processing precedes target cell lysis and is blocked by granzyme inactivation.

    Conclusions:

    • Apoptosis-inducing granzyme A and ICE share pIL-1 beta as a substrate.
    • Lymphocyte-derived granzyme A can initiate local inflammation independently of ICE.