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J Biol Chem, Vol. 273, Issue 28, 17559-17564, July 10, 1998
From the Unité INSERM 419, Institut de Biologie, 9 Quai
Moncousu 44035, Nantes Cedex 01, France
Calcium is involved in several steps of the
apoptotic process. In nuclei, endonucleases are presumed to be the main
targets of calcium; however, little is known about its role during the cytosolic phase of apoptosis. We used a cell-free system to address this question. Our results show that CaCl2 triggered
nuclear apoptosis (i.e. typical morphological change and
DNA fragmentation) at concentrations of 5 mM. This
concentration was lowered 10-fold by the co-incubation with cytosolic
extracts from nonapoptotic cells. Apoptotic changes induced by the
incubation of nuclei with CaCl2 in the presence of these
cytosols were strongly reduced in the presence of an inhibitor of
caspase-3 and to a lesser extent by an inhibitor of caspase-1. We also
show that calcium-induced apoptosis is affected by protease inhibitors
such as N-tosyl-L-phenylalanine chloromethyl ketone, but not by calpain or several lysosomal protease inhibitors. The addition of CaCl2 to the cell-free system increased a
caspase-3 activity in nonapoptotic cytosols as shown by specific
antibodies and an enzymatic assay. No activation of a caspase-3-like
activity by the addition of cytochrome c was observed in
these extracts under similar conditions. The enhanced caspase-3
activity induced by calcium was inhibited by protease inhibitors
affecting morphological nuclear apoptosis except for those responsible
for the degradation of lamin A. These results suggest that
CaCl2 could trigger, in normal cells, an apoptotic cascade
through the activation of cytosolic caspase-3 activity.
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