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J Biol Chem, Vol. 273, Issue 44, 28549-28552, October 30, 1998
From the Department of Tumor Cell Biology, St. Jude Children's
Research Hospital, Memphis, Tennessee 38101
Apoptosis involves the proteolysis of specific
cellular proteins by a group of cysteine proteases known as caspases.
Many of these cellular targets are either functionally inactivated (e.g. poly(ADP-ribose) polymerase) or activated
(e.g. other caspases, gelsolin) by such processing, thereby
facilitating the cell death process. Caspase 3 is involved in the
processing of many of these proteins. Recently, however, it was
reported that caspase 3 is dispensable for the cleavage of a large
number of cellular caspase substrates during apoptosis. Among these
substrates is DFF-45/ICAD, a subunit of the heterodimeric DNA
fragmentation factor (DFF), otherwise known as caspase-activated DNase
(CAD), that mediates genomic DNA degradation during apoptosis.
Conversely, others have reported that caspase 3 is essential for the
cleavage and activation of DFF-45/ICAD. To resolve this controversy we
examined DFF-45/ICAD processing during apoptosis in MCF-7 breast
carcinoma cells that lack functional caspase 3 and in MCF-7 cells
expressing caspase 3. We found that DFF-45/ICAD is cleaved by two
distinct caspases, one of which is caspase 3. Furthermore, cleavage of
the carboxyl-terminal region of DFF-45/ICAD, which is necessary for
activation of the enzyme, requires functional caspase 3. In the absence
of caspase 3 cleavage of the amino-terminal region of DFF-45/ICAD by
another caspase occurs, but the DFF-45 enzyme remains inactive.
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