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J. Biol. Chem., Vol. 276, Issue 20, 16704-16710, May 18, 2001
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From the Institute for Molecular Virology, and Department of
Biochemistry, Graduate School and College of Agricultural and Life
Sciences, University of Wisconsin, Madison, Wisconsin 53706
Activation of caspases by proteolytic processing
is a critical step during apoptosis in metazoans. Here we use high
resolution time lapse microscopy to show a tight link between caspase
activation and the morphological events delineating apoptosis in
cultured SF21 cells from the moth Spodoptera frugiperda, a
model insect system. The principal effector caspase,
Sf-caspase-1, is proteolytically activated during SF21
apoptosis. To define the potential role of initiator caspases in
vivo, we tested the effect of cell-permeable peptide inhibitors
on pro-Sf-caspase-1 processing. Anti-caspase peptide
analogues prevented apoptosis induced by diverse signals, including UV
radiation and baculovirus infection. IETD-fmk potently inhibited the
initial processing of pro-Sf-caspase-1 at the junction (TETD-G) of the large and small subunit, a cleavage that is blocked by
inhibitor of apoptosis Op-IAP but not pancaspase inhibitor P35. Because
Sf-caspase-1 was inhibited poorly by IETD-CHO, our data
indicated that the protease responsible for the first step in
pro-Sf-caspase-1 activation is a distinct apical caspase.
Thus, Sf-caspase-1 activation is mediated by a novel,
P35-resistant caspase. These findings support the hypothesis that
apoptosis in insects, like that in mammals, involves a cascade of
caspase activations.
Apoptosis in Motion
AN APICAL, P35-INSENSITIVE CASPASE MEDIATES PROGRAMMED CELL
DEATH IN INSECT CELLS*,
and
*
This work was supported in part by Public Health Service
Grants AI25557 and AI40482 from the NIAID, National Institutes of Health (to P. D. F.) and a Steenbock/Wharton Predoctoral
Fellowship from the Department of Biochemistry (to G. A. M).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.
The on-line version of this article (available at
http://www.jbc.org) contains three QuickTime videos as
supplemental material.
Current address: Millennium Pharmaceuticals, Cambridge, MA 02139
§
To whom correspondence should be addressed: Inst. for Molecular
Virology, R. M. Bock Laboratories, University of Wisconsin, 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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