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(Received for publication, July 2, 1996)
From the Department of Pathology, University of Michigan, Ann
Arbor, Michigan 48109 and the 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 vivo, 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.
Volume 271, Number 35,
Issue of August 30, 1996
pp. 20977-20980
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
and
Burnham Institute,
La Jolla, California 92037
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