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Expression, proteolysis and activation of caspases 6 and 7 during rat C6 glioma cell apoptosis

Activation of cysteinyl aspartate-specific proteases (caspases) may underlie apoptotic cell death in brain. Terminal, executioner caspases 3, 6 and 7 likely contribute to such cell death in a stimulus- and cell type-specific manner. Here we investigate the processing and activation of caspases 3, 6...

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Bibliographic Details
Published in:Neuroscience letters 2002-05, Vol.324 (1), p.33-36
Main Authors: Meller, Robert, Skradski, Shana L., Simon, Roger P., Henshall, David C.
Format: Article
Language:English
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Summary:Activation of cysteinyl aspartate-specific proteases (caspases) may underlie apoptotic cell death in brain. Terminal, executioner caspases 3, 6 and 7 likely contribute to such cell death in a stimulus- and cell type-specific manner. Here we investigate the processing and activation of caspases 3, 6 and 7 in rat C6 glioma cells induced to undergo apoptosis by staurosporine (STS) treatment as a model of apoptosis in glia. Proteolysis and activation of caspases 3 and 7 as determined by immunoblotting and substrate-specific cleavage assay (DEVDase) preceded caspase-6 proteolysis and increased VEIDase activity following STS treatment. Activation of caspase-6 was paralleled by cleavage of the nuclear envelope protein lamin-A. These results highlight temporal differences in the activation of the triad of executioner caspases 3, 6 and 7 during glial cell apoptosis.
ISSN:0304-3940
1872-7972
DOI:10.1016/S0304-3940(02)00166-0