Please use this identifier to cite or link to this item:
https://doi.org/10.1074/jbc.273.16.9357
DC Field | Value | |
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dc.title | Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis | |
dc.contributor.author | Jänicke, R.U. | |
dc.contributor.author | Sprengart, M.L. | |
dc.contributor.author | Wati, M.R. | |
dc.contributor.author | Porter, A.G. | |
dc.date.accessioned | 2014-11-28T02:49:53Z | |
dc.date.available | 2014-11-28T02:49:53Z | |
dc.date.issued | 1998-04-17 | |
dc.identifier.citation | Jänicke, R.U., Sprengart, M.L., Wati, M.R., Porter, A.G. (1998-04-17). Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. Journal of Biological Chemistry 273 (16) : 9357-9360. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.273.16.9357 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/111806 | |
dc.description.abstract | Interleukin 1β-converting enzyme-like proteases (caspases) are crucial components of cell death pathways. Among the caspases identified, caspase-3 stands out because it is commonly activated by numerous death signals and cleaves a variety of important cellular proteins. Studies in caspase-3 knock- out mice have shown that this protease is essential for brain development. To investigate the requirement for caspase-3 in apoptosis, we took advantage of the MCF-7 breast carcinoma cell line, which we show hero has lost caspase-3 owing to a 47-base pair deletion within exon 3 of the CASP-3 gene. This deletion results in the skipping of exon 3 during pre-mRNA splicing, thereby abrogating translation of the CASP-3 mRNA. Although MCF-7 cells were still sensitive to tumor necrosis factor (TNF)- or staurosporine-induced apoptosis, no DNA fragmentation was observed. In addition, MCF-7 cells undergoing cell death did not display some of the distinct morphological features typical of apoptotic cells such as shrinkage and blebbing. Introduction of the CASP-3 gene into MCF-7 cells resulted in DNA fragmentation and cellular blebbing following TNF treatment. These results indicate that although caspase-3 is not essential for TNF- or staurosporine-induced apoptosis, it is required for DNA fragmentation and some of the typical morphological changes of cells undergoing apoptosis. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.273.16.9357 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1074/jbc.273.16.9357 | |
dc.description.sourcetitle | Journal of Biological Chemistry | |
dc.description.volume | 273 | |
dc.description.issue | 16 | |
dc.description.page | 9357-9360 | |
dc.description.coden | JBCHA | |
dc.identifier.isiut | 000073128800002 | |
Appears in Collections: | Staff Publications |
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