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J. Biol. Chem., Vol. 278, Issue 20, 18265-18270, May 16, 2003
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From the Cytochrome c released from
mitochondria into the cytoplasm plays a critical role in many forms of
apoptosis by stimulating apoptosome formation and subsequent caspase
activation. However, the mechanisms regulating cytochrome c
apoptotic activity are not understood. Here we demonstrate that
cytochrome c is nitrosylated on its heme iron during
apoptosis. Nitrosylated cytochrome c is found
predominantly in the cytoplasm in control cells. In contrast, when
cytochrome c release from mitochondria is inhibited by
overexpression of the anti-apoptotic proteins B cell lymphoma/leukemia
(Bcl)-2 or Bcl-XL, nitrosylated cytochrome c is
found in the mitochondria. These data suggest that during apoptosis,
cytochrome c is nitrosylated in mitochondria and then
rapidly released into the cytoplasm in the absence of Bcl-2 or
Bcl-XL overexpression. In vitro nitrosylation of cytochrome c increases caspase-3 activation in cell
lysates. Moreover, the inhibition of intracellular cytochrome
c nitrosylation is associated with a decrease in apoptosis,
suggesting that cytochrome c nitrosylation is a
proapoptotic modification. We conclude that nitrosylation of the heme
iron of cytochrome c may be a novel mechanism of apoptosis regulation.
Nitrosylation of Cytochrome c during
Apoptosis*
,¶
Department of Medicine, University of
Massachusetts Medical School, Worcester, Massachusetts 01605 and
§ Department of Pediatrics, University of Virginia Medical
School, Charlottesville, Virginia 22908
*
The work was funded by an American Cancer Society Research
Project Grant.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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