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(Received for publication, April 4, 1996, and in revised form, June 11, 1996)
From the Department of Molecular and Experimental Medicine, The
Scripps Research Institute, La Jolla, California 92037
Mitochondrial function was examined in Jurkat
cells undergoing Fas-mediated apoptosis. With succinate or
ascorbate/tetramethylphenylenediamine as substrate, oxygen uptake by
digitonin-permeabilized apoptotic mitochondria was greatly decreased as
compared with control. Assessment of the function of the cytochrome
c-cytochrome oxidase segment of the electron transport
chain of apoptotic mitochondria showed that the activity of cytochrome
oxidase appeared to be normal, but that of cytochrome c was
greatly diminished. A death protease was found to participate in the
events leading to the loss of cytochrome c activity, but
the cytochrome did not seem to be extensively degraded during the
course of apoptosis. Our results suggest that a rapid loss in
mitochondrial function due at least in part to the inhibition or
inactivation of cytochrome c is a potentially fatal
component of the apoptosis program of Jurkat cells.
Volume 271, Number 35,
Issue of August 30, 1996
pp. 21629-21636
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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