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Papers In Press, published online ahead of print February 8, 2002
Molecular Biology and Biochemistry, Howard Hughes Medical Institute, Piscataway, New Jersey 08854
Corresponding Author: ewhite{at}cabm.rutgers.edu
Summary Pro-apoptotic Bax and Bak have been implicated in regulation of p53-dependent apoptosis. We assessed the ability of primary baby mouse kidney (BMK) epithelial cells from bax-/-, 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 TNF-a -mediated apoptosis. The loss of both Bax and Bak severely impaired TNF-a-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-a, but not in cells deficient in both. Thus, either Bax or Bak is required for death signaling through mitochondria in response to TNF-a but both are dispensable for p53-dependent transformation inhibition.
J. Biol. Chem, 10.1074/jbc.M109939200
Submitted on October 15, 2001
Revised on February 8, 2002
Accepted on February 8, 2002
Bax and Bak independently promote cytochrome c release from mitochondria
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