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J. Biol. Chem., Vol. 275, Issue 21, 15657-15664, May 26, 2000
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From the Department of Biochemistry and the Institute for Molecular
Virology, College of Agricultural and Life Sciences and Graduate
School, University of Wisconsin, Madison, Wisconsin 53706
Signal-induced activation of caspases, the
critical protease effectors of apoptosis, requires proteolytic
processing of their inactive proenzymes. Consequently, regulation of
procaspase processing is critical to apoptotic execution. We report
here that baculovirus pancaspase inhibitor P35 and inhibitor of
apoptosis Op-IAP prevent caspase activation in vivo, but at
different steps. By monitoring proteolytic processing of endogenous
Sf-caspase-1, an insect group II effector caspase, we show
that Op-IAP blocked the first activation cleavage at TETD
Caspase Inhibitor P35 and Inhibitor of Apoptosis Op-IAP Block
in Vivo Proteolytic Activation of an Effector
Caspase at Different Steps*
G between
the large and small caspase subunits. In contrast, P35 failed to affect
this cleavage, but functioned downstream to block maturation cleavages
(DXXD(G/A)) of the large subunit. Substitution of P35's
reactive site residues with TETDG failed to increase its effectiveness
for blocking TETDG processing of pro-Sf-caspase-1,
despite wild-type function for suppressing apoptosis. These data are
consistent with the involvement of a novel initiator caspase that is
resistant to P35, but directly or indirectly inhibitable by Op-IAP. The
conservation of TETDG processing sites among insect effector
caspases, including Drosophila drICE and DCP-1, suggests
that in vivo activation of these group II caspases involves
a P35-insensitive caspase and supports a model wherein apical and
effector caspases function through a proteolytic cascade to execute
apoptosis in insects.
*
This work was supported by a National Science Foundation
graduate fellowship (to D. J. L.), Viral Oncology Training
Grant CA09075 from the National Institutes of Health (to S. F. H.), and Public Health Service Grant AI40482 from NIAID,
National Institutes of Health (to P. D. F.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Inst. for Molecular
Virology, Bock Laboratories, University of Wisconsin-Madison, 1525 Linden Dr., Madison, WI 53706-1596. Tel.: 608-262-7774; Fax: 608-262-7414; E-mail: pfriesen@facstaff.wisc.edu.
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