Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases

Kim Orth, Karen O'Rourke, Guy S. Salvesen, Vishva M. Dixit

Research output: Contribution to journalArticlepeer-review

184 Scopus citations

Abstract

Apoptosis is executed by cysteine proteases belonging to the CED-3/ICE family, which, unlike other mammalian cysteine proteases, cleave their substrates following aspartate residues. Proteases belonging to this family exist in the cytosol as zymogens that require accurate processing at internal aspartate residues to generate the two-chain active enzymes. As such, CED- 3/ICE family members are capable of activating each other in a manner analogous to the protease zymogens of the coagulation or complement cascades. At present, it is unknown whether such mutual processing exists in vive, and if so whether it is sequential, implying an order to the death pathway. Using a cell-free apoptosis system, recombinant ICE proteases and both biochemical and morphological criteria, we demonstrate an ordering of the mammalian ICEs that are most related to the Caenorhabditis elegans death protease CED-3.

Original languageEnglish (US)
Pages (from-to)20977-20980
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number35
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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