Autor: |
Songqing Na, Andrew L. Glasebrook, Neal W. Roehm, Chan Hsin S. Chang, Margaret M. Racke, Marian Mosior, Steve Kovacevic |
Rok vydání: |
2002 |
Předmět: |
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Zdroj: |
Journal of Neurochemistry. 80:1039-1048 |
ISSN: |
0022-3042 |
DOI: |
10.1046/j.0022-3042.2002.00787.x |
Popis: |
Activated caspase-3 is considered an important enzyme in the cell death pathway. To study the specific role of caspase-3 activation in neuronal cells, we generated a stable tetracycline-regulated SK-N-MC neuroblastoma cell line, which expressed a highly efficient self-activating chimeric caspase-3, consisting of the caspase-1 prodomain fused to the caspase-3 catalytic domain. Under expression-inducing conditions, we observed a time-dependent increase of processed caspase-3 by immunostaining for the active form of the enzyme, intracellular caspase-3 enzyme activity, as well as poly(ADP-ribose) polymerase (PARP) cleavage. Induced expression of the caspase fusion protein showed predominantly caspase-3 activity without any apoptotic morphological changes. In contrast, staurosporine treatment of the same cells resulted in activation of multiple caspases and profound apoptotic morphology. Our work provides evidence that auto-activation of caspase-3 can be efficiently achieved with a longer prodomain and that neuronal cell apoptosis may require another caspase or activation of multiple caspase enzymes. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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