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(Received for publication, November 11, 1996)
,
From the Engagement of CD95 or tumor necrosis factor 1 receptor (TNFR-1) by ligand or agonist antibodies is capable of
activating the cell death program, the effector arm of which is
composed of mammalian interleukin-1
Department of Pathology, University of
Michigan Medical School, Ann Arbor, Michigan 48109 and the
¶ Burnham Institute, San Diego, California 92037
converting enzyme (ICE)-like
cysteine proteases (designated caspases) that are related to the
Caenorhabditis elegans death gene, CED-3.
Caspases, unlike other mammalian cysteine proteases, cleave their
substrates following aspartate residues. Furthermore, proteases
belonging to this family exist as zymogens that in turn require
cleavage at internal aspartate residues to generate the two-subunit
active enzyme. As such, family members are capable of activating each
other. Remarkably, both CD95 and TNFR-1 death receptors initiate
apoptosis by recruiting a novel ICE/CED-3 family member, designated
FLICE/MACH, to the receptor signaling complex. Therefore, FLICE/MACH
represents the apical triggering protease in the cascade. Consistent
with this, recombinant FLICE was found capable of proteolytically
activating downstream caspases. Furthermore, CrmA, a pox virus-encoded
serpin that inhibits Fas and tumor necrosis factor-induced cell death
attenuates the ability of FLICE to activate downstream caspases.
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E. W. Humke, J. Ni, and V. M. Dixit ERICE, a Novel FLI |
