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J Biol Chem, Vol. 273, Issue 16, 9357-9360, April 17, 1998
From the Institute of Molecular and Cell Biology, The National
University of Singapore, 30 Medical Drive, Singapore 117609, Republic of Singapore
Interleukin 1
COMMUNICATION
Caspase-3 Is Required for DNA Fragmentation and Morphological
Changes Associated with Apoptosis
-converting enzyme-like proteases
(caspases) are crucial components of cell death pathways. Among the
caspases identified, caspase-3 stands out because it is commonly
activated by numerous death signals and cleaves a variety of important
cellular proteins. Studies in caspase-3 knock-out mice have shown that this protease is essential for brain development. To investigate the
requirement for caspase-3 in apoptosis, we took advantage of the MCF-7
breast carcinoma cell line, which we show here has lost caspase-3 owing
to a 47-base pair deletion within exon 3 of the CASP-3
gene. This deletion results in the skipping of exon 3 during
pre-mRNA splicing, thereby abrogating translation of the
CASP-3 mRNA. Although MCF-7 cells were still sensitive
to tumor necrosis factor (TNF)- or staurosporine-induced apoptosis, no
DNA fragmentation was observed. In addition, MCF-7 cells undergoing cell death did not display some of the distinct morphological features
typical of apoptotic cells such as shrinkage and blebbing. Introduction
of the CASP-3 gene into MCF-7 cells resulted in DNA fragmentation and cellular blebbing following TNF treatment. These results indicate that although caspase-3 is not essential for TNF- or
staurosporine-induced apoptosis, it is required for DNA fragmentation
and some of the typical morphological changes of cells undergoing
apoptosis.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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