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PMID:10205158
| Citation |
Samali, A, Cai, J, Zhivotovsky, B, Jones, DP and Orrenius, S (1999) Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 18:2040-8 |
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| Abstract |
Activation of pro-caspase-3 is a central event in the execution phase of apoptosis and appears to serve as the convergence point of different apoptotic signaling pathways. Recently, mitochondria were found to play a central role in apoptosis through release of cytochrome c and activation of caspases. Moreover, a sub-population of pro-caspase-3 has been found to be localized to this organelle. In the present study, we demonstrate that pro-caspase-3 is present in the mitochondrial fraction of Jurkat T cells in a complex with the chaperone proteins Hsp60 and Hsp10. Induction of apoptosis with staurosporine led to the activation of mitochondrial pro-caspase-3 and its dissociation from the Hsps which were released from mitochondria. The release of Hsps occurred simultaneously with the release of other mitochondrial intermembrane space proteins including cytochrome c and adenylate kinase, prior to a loss of mitochondrial transmembrane potential. In in vitro systems, recombinant Hsp60 and Hsp10 accelerated the activation of pro-caspase-3 by cytochrome c and dATP in an ATP-dependent manner, consistent with their function as chaperones. This finding suggests that the release of mitochondrial Hsps may also accelerate caspase activation in the cytoplasm of intact cells. |
| Links |
PubMed PMC1171288 Online version:10.1093/emboj/18.8.2040 |
| Keywords |
Apoptosis; Caspase 3; Caspase 9; Caspases/metabolism; Chaperonin 10/metabolism; Chaperonin 60/metabolism; Cytosol/enzymology; Enzyme Precursors/metabolism; Humans; Jurkat Cells; Mitochondria/enzymology; Mitochondria/metabolism; Protein Binding; Recombinant Proteins/metabolism; Subcellular Fractions/enzymology; Subcellular Fractions/metabolism |
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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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See also
References
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