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Blood, Vol. 93 No. 7 (April 1), 1999:
pp. 2342-2352
Nitric Oxide-Induced Apoptosis in Human Leukemic Lines Requires
Mitochondrial Lipid Degradation and Cytochrome C Release
Alexey Ushmorov,
Frank Ratter,
Volker Lehmann,
Wulf Dröge,
Volker Schirrmacher, and
Victor Umansky
From the Divisions of Immunochemistry and Cellular Immunology, Tumor
Immunology Program, German Cancer Research Center, Heidelberg, Germany.
We have previously shown that nitric oxide (NO) stimulates apoptosis
in different human neoplastic lymphoid cell lines through activation of
caspases not only via CD95/CD95L interaction, but also independently of
such death receptors. Here we investigated mitochondria-dependent
mechanisms of NO-induced apoptosis in Jurkat leukemic cells. NO donor
glycerol trinitrate (at the concentration, which induces apoptotic cell
death) caused (1) a significant decrease in the concentration of
cardiolipin, a major mitochondrial lipid; (2) a downregulation in
respiratory chain complex activities; (3) a release of the
mitochondrial protein cytochrome c into the cytosol; and (4) an
activation of caspase-9 and caspase-3. These changes were accompanied
by an increase in the number of cells with low mitochondrial
transmembrane potential and with a high level of reactive oxygen
species production. Higher resistance of the CD95-resistant Jurkat
subclone (APO-R) cells to NO-mediated apoptosis correlated with the
absence of cytochrome c release and with less alterations in
other mitochondrial parameters. An inhibitor of lipid peroxidation,
trolox, significantly suppressed NO-mediated apoptosis in APO-S Jurkat
cells, whereas bongkrekic acid (BA), which blocks mitochondrial
permeability transition, provided only a moderate antiapoptotic effect.
Transfection of Jurkat cells with bcl-2 led to a complete block of
apoptosis due to the prevention of changes in mitochondrial functions.
We suggest that the mitochondrial damage (in particular, cardiolipin
degradation and cytochrome c release) induced by NO in human
leukemia cells plays a crucial role in the subsequent activation of
caspase and apoptosis.
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