| Autor: |
Racke, M.M., Mosior, M., Kovacevic, S., Chang, C.H.S., Glasebrook, A.L., Roehm, N.W., Na, S. |
| Předmět: |
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| Zdroj: |
Journal of Neurochemistry; 3/15/2002, Vol. 80 Issue 6, p1039-1048, 10p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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