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Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity

A Ito1, T Uehara, Y Nomura

  • 1Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

FEBS Letters
|April 4, 2000
PubMed

Insights

Caspase-2S, a form of caspase-2, promotes cell survival. Researchers identified ISBP as a binding protein that mediates caspase-2S

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Caspases are key regulators of apoptosis.
  • Caspase-2 exists as two isoforms, caspase-2L and caspase-2S, with opposing roles in cell death.
  • The anti-apoptotic mechanism of caspase-2S is not well understood.

Purpose of the Study:

  • To identify proteins interacting with caspase-2S.
  • To elucidate the mechanism underlying caspase-2S-mediated cell survival.

Main Methods:

  • Yeast two-hybrid screening using caspase-2S cDNA.
  • In vitro binding assays with purified proteins.
  • Co-immunoprecipitation in cultured cells.
  • Northern blot analysis for protein expression.

Main Results:

  • Identified ISBP (Ich-1S-binding protein) as a caspase-2S interacting protein.
  • ISBP is a calcium and integrin-binding protein.
  • ISBP interacts with caspase-2S in vitro and in vivo.
  • ISBP partially inhibits pro-caspase-2L processing.

Conclusions:

  • ISBP is a novel mediator of caspase-2S's anti-apoptotic function.
  • ISBP may play a significant role in neuronal cell survival regulated by caspase-2S.

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