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PMID:11836241
| Citation |
Degenhardt, K, Sundararajan, R, Lindsten, T, Thompson, C and White, E (2002) Bax and Bak independently promote cytochrome C release from mitochondria. J. Biol. Chem. 277:14127-34 |
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| Abstract |
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(-/-), 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-alpha (TNF-alpha)-mediated apoptosis. The loss of both Bax and Bak severely impaired TNF-alpha-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-alpha but not in cells deficient in both. Thus, either Bax or Bak is required for death signaling through mitochondria in response to TNF-alpha, but both are dispensable for p53-dependent transformation inhibition. |
| Links |
PubMed Online version:10.1074/jbc.M109939200 |
| Keywords |
Animals; Apoptosis; Blotting, Western; Caspase 9; Caspases/metabolism; Cell Death; Cells, Cultured; Cytochrome c Group/metabolism; Dimerization; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Immunoblotting; Membrane Proteins/metabolism; Mice; Microscopy, Phase-Contrast; Mitochondria/metabolism; Plasmids/metabolism; Precipitin Tests; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-bcl-2; Signal Transduction; Subcellular Fractions; Tumor Necrosis Factor-alpha/metabolism; Tumor Suppressor Protein p53/metabolism; bcl-2 Homologous Antagonist-Killer Protein; bcl-2-Associated X Protein |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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