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J. Biol. Chem., Vol. 277, Issue 16, 14127-14134, April 19, 2002
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§,,§
**
From the Pro-apoptotic Bax and Bak have been implicated in
the regulation of p53-dependent apoptosis. We assessed the
ability of primary baby mouse kidney (BMK) epithelial cells from
bax Howard Hughes Medical Institute,
Center for Advanced Biotechnology and Medicine,
§ Department of Molecular Biology and Biochemistry, the
** Cancer Institute of New Jersey, Rutgers University,
Piscataway, New Jersey 08854, and ¶ University of Pennsylvania,
Departments of Medicine, Cancer Biology, and Pathology and Laboratory
Medicine, Abramson Family Cancer Research Institute,
Philadelphia, Pennsylvania 19104-6160
/, bak/, and
bax/ bak/ mice
to be transformed by E1A alone or in conjunction with dominant-negative p53 (p53DD). Although E1A alone transformed BMK cells from
p53-deficient mice, E1A alone did not transform BMK cells from
bax/, bak/, or
bax/ bak/ mice.
Thus, the loss of both Bax and Bak was not sufficient to relieve
p53-dependent suppression of transformation in epithelial cells. To test the requirement for Bax and Bak in other death signaling
pathways, stable E1A plus p53DD-transformed BMK cell lines were derived
from the bax/,
bak/, and bax/
bak/ mice and characterized for their
response to tumor necrosis factor-
(TNF-)-mediated apoptosis. The
loss of both Bax and Bak severely impaired TNF--mediated apoptosis,
but the presence of either Bax or Bak alone was sufficient for cell
death. Cytochrome c was released from mitochondria, and
caspase-9 was activated in Bax- or Bak-deficient cells in response to
TNF- but not in cells deficient in both. Thus, either Bax or Bak is
required for death signaling through mitochondria in response to
TNF-, but both are dispensable for p53-dependent
transformation inhibition.
To whom correspondence should be addressed. Tel.: 732-235-5329;
Fax: 732-235-5795; E-mail: ewhite@cabm.rutgers.edu.
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