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Activation of caspases triggered by cytochrome c in vitro.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Pan, Guangjin Humke, Eric W. Dixit, Vishva M. |
| Copyright Year | 1998 |
| Abstract | Previous studies have shown that Apaf-1 and caspase-9 in the presence of cytochrome c and dATP can form an initiating complex for an apoptotic protease cascade. We have developed a cytochrome c-dependent in vitro system in which caspases downstream of this initiation complex are activated. The activation of caspase-9 from zymogen form to active dimeric protease requires intrinsic enzymatic activity. In contrast, caspase-3 and caspase-7 zymogens are proteolytically processed by active caspase-9. Activation of the above caspases is blocked by a dominant negative form of caspase-9. The in vitro system displays surprising specificity in that other caspases, including 1, 2, 4, 8, 10, and 13, are not activated. |
| Starting Page | 1041 |
| Ending Page | 1047 |
| Page Count | 7 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://deepblue.lib.umich.edu/bitstream/handle/2027.42/116354/feb2s0014579398003305.pdf;sequence=1 |
| PubMed reference number | 9598997v1 |
| Volume Number | 426 |
| Issue Number | 1 |
| Journal | FEBS letters |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | APAF1 gene Cascade Device Component Dominant-Negative Mutation Endopeptidases Enzyme Precursors Transcription Initiation caspase caspase-3 caspase-7 caspase-9 |
| Content Type | Text |
| Resource Type | Article |
