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J. Exp. Med.,
Volume 188, Number 11, December 7, 1998 2193-2198
By
From the Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology and
University of Gent, B-9000 Gent, Belgium
It is well established that apoptosis is accompanied by activation of procaspases and by mitochondrial changes, such as decrease in mitochondrial transmembrane potential (
m) and release of cytochrome c. We analyzed the causal relationship between activated caspases and these
mitochondrial phenomena. Purified recombinant caspase-1, -11, -3, -6, -7, and -8 were incubated with mitochondria in the presence or absence of additional cellular components, after
which m was determined. At lower caspase concentrations, only caspase-8 was able to activate a cytosolic factor, termed caspase-activated factor (CAF), which resulted in decrease in m and release of cytochrome c. Both CAF-mediated activities could not be blocked by protease inhibitors, including oligopeptide caspase inhibitors. CAF-induced cytochrome c release,
but not decrease of m, was blocked in mitochondria from cells overexpressing Bcl-2. CAF is
apparently involved in decrease of m and release of cytochrome c, whereas Bcl-2 only prevents the latter. Hence, CAF may form the link between death domain receptor-dependent activation of procaspase-8 and the mitochondrial events studied.
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