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Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.

Cell | Nov 14, 1997

We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.

Pubmed ID: 9390557 RIS Download

Mesh terms: Amino Acid Sequence | Apoptosis | Apoptotic Protease-Activating Factor 1 | Binding Sites | Breast Neoplasms | Caspase 3 | Caspase 9 | Caspases | Cell Line | Cysteine Endopeptidases | Cytochrome c Group | Deoxyadenine Nucleotides | Enzyme Activation | Epithelial Cells | HeLa Cells | Humans | Kidney | Models, Chemical | Molecular Sequence Data | Multienzyme Complexes | Mutation | Protein Binding | Proteins | Tumor Cells, Cultured

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