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J. Biol. Chem., Vol. 276, Issue 19, 16059-16063, May 11, 2001
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From the Robert H. Lurie Comprehensive Cancer Center and the
Department of Medicine, Northwestern University Medical School,
Chicago, Illinois 60611
Caspases are universal effectors of
apoptosis. The mitochondrial and death receptor pathways
activate distinct apical caspases (caspase-9 and -8, respectively) that
converge on the proteolytic activation of the downstream executioner
caspase-3. Caspase-9 and -8 cleave procaspase-3 to produce a p24
processing intermediate (composed of its prodomain and large subunit),
which then undergoes autoproteolytic cleavage to remove the prodomain
from the active protease. Recently, several heat shock proteins have
been shown to selectively inhibit the mitochondrial apoptotic
pathway by disrupting the activation of caspase-9 downstream of
cytochrome c release. We report here that the small heat
shock protein
The Small Heat Shock Protein
B-Crystallin Negatively Regulates
Cytochrome c- and Caspase-8-dependent Activation of
Caspase-3 by Inhibiting Its Autoproteolytic Maturation*
B-crystallin inhibits both the mitochondrial and death
receptor pathways. In S-100 cytosolic extracts treated with cytochrome
c/dATP or caspase-8, B-crystallin inhibits the
autoproteolytic maturation of the p24 partially processed caspase-3
intermediate. In contrast, neither the closely related small heat shock
protein family member Hsp27 nor Hsp70 inhibited the maturation of the
p24 intermediate. We also demonstrate that B-crystallin
co-immunoprecipitates with the p24 partially processed caspase-3
in vivo. Taken together, our results demonstrate
that B-crystallin is a novel negative regulator of apoptosis that
acts distally in the conserved cell death machinery by inhibiting the
autocatalytic maturation of caspase-3.
*
This work was supported in part by a grant from the Muscular
Dystrophy Association (to V. L. C.), by National Institutes of Health
Grants NS31957 (to V. L. C.) and 5T32-CA70085 (to M. C. K.), by
institutional research grants to Northwestern University from the
Howard Hughes Medical Institute (to V. L. C.), and by the Elizabeth
Boughton Trust (to V. L. C.).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: Division of
Endocrinology, Tarry 15-755, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: 312-503-0644; Fax: 312-908-9032; E-mail: v-cryns@northwestern.edu.
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