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J Biol Chem, Vol. 273, Issue 18, 10815-10818, May 1, 1998
From the Medical Research Council Toxicology Unit, Hodgkin
Building, University of Leicester, P. O. Box 138, Lancaster Road,
Leicester LE1 9HN, United Kingdom
Caspases plays a key role in the execution phase
of apoptosis. "Initiator" caspases, such as caspase-8, activate
"effector" caspases, such as caspase-3 and -7, which subsequently
cleave cellular substrates thereby precipitating the dramatic
morphological changes of apoptosis. Following treatment of mice with an
agonistic anti-Fas antibody to induce massive hepatocyte apoptosis, we
now demonstrate a distinct subcellular localization of the effector caspases-3 and -7. Active caspase-3 is confined primarily to the cytosol, whereas active caspase-7 is associated almost exclusively with
the mitochondrial and microsomal fractions. These data suggest that
caspases-3 and -7 exert their primary functions in different cellular
compartments and offer a possible explanation of the presence of
caspase homologs with overlapping substrate specificities. Translocation and activation of caspase-7 to the endoplasmic reticulum correlates with the proteolytic cleavage of the endoplasmic
reticular-specific substrate, sterol regulatory element-binding protein
1. Liver damage, induction of apoptosis, activation and
translocation of caspase-7, and proteolysis of sterol regulatory
element-binding protein 1 are all blocked by the caspase inhibitor,
benzyloxycarbonyl-Val-Ala-Asp fluoromethyl ketone (Z-VAD.fmk). Our data
demonstrate for the first time the differential subcellular
compartmentalization of specific effector caspases following the
induction of apoptosis in vivo.
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K. Machida, K. Tsukiyama-Kohara, E. Seike, S. Tone, F. Shibasaki, M. Shimizu, H. Takahashi, Y. Hayashi, N. Funata, C. Taya, et al. Inhibition of Cytochrome c Release in Fas-mediated Signaling Pathway in Transgenic Mice Induced to Express Hepatitis C Viral Proteins J. Biol. Chem., April 6, 2001; 276(15): 12140 - 12146. [Abstract] [Full Text] [PDF]
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R. V. Rao, E. Hermel, S. Castro-Obregon, G. del Rio, L. M. Ellerby, H. M. Ellerby, and D. E. Bredesen Coupling Endoplasmic Reticulum Stress to the Cell Death Program. MECHANISM OF CASPASE ACTIVATION J. Biol. Chem., August 31, 2001; 276(36): 33869 - 33874. [Abstract] [Full Text] [PDF]
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