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J Biol Chem, Vol. 274, Issue 25, 17484-17490, June 18, 1999
From the Division of Cellular Immunology, La Jolla Institute for
Allergy and Immunology, San Diego, California 92121
We investigated the ability of caspases (cysteine
proteases with aspartic acid specificity) to induce cytochrome
c release from mitochondria. When Jurkat cells were induced
to undergo apoptosis by Fas receptor ligation, cytochrome c
was released from mitochondria, an event that was prevented by the
caspase inhibitor, zVAD-fmk (zVal-Ala-Asp-CH2F). Purified
caspase-8 triggered rapid cytochrome c release from
isolated mitochondria in vitro. The effect was indirect, as
the presence of cytosol was required, suggesting that caspase-8 cleaves
and activates a cytosolic substrate, which in turn is able to induce
cytochrome c release from mitochondria. The cytochrome
c releasing activity was not blocked by caspase inhibition,
but was antagonized by Bcl-2 or Bcl-xL. Caspase-8 and caspase-3 cleaved
Bid, a proapoptotic Bcl-2 family member, which gains cytochrome
c releasing activity in response to caspase cleavage.
However, caspase-6 and caspase-7 did not cleave Bid, although they
initiated cytochrome c release from mitochondria in the
presence of cytosol. Thus, effector caspases may cleave and activate
another cytosolic substrate (other than Bid), which then promotes
cytochrome c release from mitochondria. Mitochondria significantly amplified the caspase-8 initiated DEVD-specific cleavage
activity. Our data suggest that cytochrome c release, initiated by the action of caspases on a cytosolic substrates, may act
to amplify a caspase cascade during apoptosis.
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