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Papers In Press, published online ahead of print August 4, 2000
Adult Oncology, Dana-Farber Cancer Institute, Boston, M.A. 02115
Corresponding Author: Rakesh_Datta{at}dfci.harvard.edu
The inhibitor of apoptosis (IAP) family of anti-apoptotic proteins regulate programmed cell death. Of the six known human IAP related proteins, XIAP is the most potent inhibitor. To study the mechanistic effects of XIAP on DNA damage-induced apoptosis, we prepared U-937 cells that stably overexpress XIAP. The results demonstrate that XIAP inhibits apoptosis induced by 1-
J. Biol. Chem, 10.1074/jbc.M910231199
Submitted on December 23, 1999
Revised on June 22, 2000
Accepted on August 4, 2000
XIAP regulates DNA damage-induced apoptosis downstream of caspase-9 clevage
-D-arabinofuranosylcytosine (ara-C) and other genotoxic agents. XIAP had no detectable effect on ara-C-induced release of mitochondrial cytochrome c and attenuated cleavage of pro-caspase-9. In addition, we show that ara-C induces the association of XIAP with the cleaved fragments of caspase-9 and thereby inhibition of caspase-9 activity. The results also demonstrate that ara-C induces cleavage of pro-caspase-3 by a caspase-8-dependent mechanism and that XIAP inhibits caspase-3 activity. These results demonstrate that XIAP functions downstream to pro-caspase-9 cleavage as an inhibitor of both proteolytically processed caspase-9 and caspase-3 in the cellular response to genotoxic stress.
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