In:
Journal of Neurochemistry, Wiley, Vol. 80, No. 6 ( 2002-03-15), p. 1039-1048
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0022-3042
,
1471-4159
DOI:
10.1046/j.0022-3042.2002.00787.x
Language:
English
Publisher:
Wiley
Publication Date:
2002
detail.hit.zdb_id:
80158-6
detail.hit.zdb_id:
2020528-4
SSG:
12
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