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J Biol Chem, Vol. 274, Issue 11, 6823-6826, March 12, 1999
From the In cultured human endothelial cells,
physiological levels of NO prevent apoptosis and interfere with the
activation of the caspase cascade. In vitro data have
demonstrated that NO inhibits the activity of caspase-3 by
S-nitrosation of the enzyme. Here we present evidence for
the in vivo occurrence and functional relevance of this
novel antiapoptotic mechanism. To demonstrate that the cysteine residue
Cys-163 of caspase-3 is S-nitrosated, cells were
transfected with the Myc-tagged p17 subunit of caspase-3. After
incubation of the transfected cells with different NO donors, Myc-tagged p17 was immunoprecipitated with anti-Myc antibody. S-Nitrosothiol was detected in the immunoprecipitate by
electron spin resonance spectroscopy after liberation and spin trapping of NO by
N-methyl-D-glucamine-dithiocarbamate-iron
complex. Transfection of cells with a p17 mutant, where the essential
Cys-163 was mutated into alanine, completely prevented
S-nitrosation of the enzyme. As a functional correlate, in
human umbilical vein endothelial cells the NO donors sodium
nitroprusside or PAPA NONOate (50 µM) significantly
reduced the increase in caspase-3-like activity induced by
overexpressing caspase-3 by 75 and 70%, respectively. When human
umbilical vein endothelial cells were cotransfected with
COMMUNICATION
Nitric Oxide Inhibits Caspase-3 by S-Nitrosation
in Vivo
,,,,
Molecular Cardiology,
-galactosidase, morphological analysis of stained cells revealed
that cell death induction by overexpression of caspase-3 was completely
suppressed in the presence of sodium nitroprusside, PAPA NONOate, or
S-nitroso-L-cysteine (50 µM). Thus, NO
supplied by exogenous NO donors serves in vivo as an
antiapoptotic regulator of caspase activity via
S-nitrosation of the Cys-163 residue of caspase-3.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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