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Papers In Press, published online ahead of print October 24, 2001
Oncology Research, Mayo Clinic, Rochester, MN 55905
Corresponding Author: Kaufmann.Scott{at}Mayo.edu
SUMMARY MCF-7 human breast cancer cells are widely utilized to study apoptotic processes. Recent studies demonstrated that these cells lack procaspase-3. In the present study, caspase activation and activity was examined in this cell line after treatment with the microtubule poison paclitaxel. When cells were harvested 72 h after the start of a 24 h treatment with 100 nM paclitaxel, 37 ± 5 % of the cells were nonadherent and displayed apoptotic morphological changes. Although mitochondrial cytochrome c release and caspase-9 cleavage were detectable by immunoblotting, assays of cytosol and nuclei prepared from the apoptotic cells failed to demonstrate the presence of activity that cleaved the synthetic caspase substrates LEHD-AFC, DEVD-AFC and VEID-AFC. Likewise, the paclitaxel-treated MCF-7 cells failed to cleave a variety of caspase substrates, including lamin A, b-catenin, gelsolin, protein kinase Cd, topoisomerase I and procaspases-6, 8 and 10. Transfection of MCF-7 cells with wildtype procaspase-3 partially restored cleavage of these polypeptides but did not result in detectable activities that could cleave the synthetic caspase substrates. Immunoblotting revealed that caspases-9, and -3, which were proteolytically cleaved in paclitaxel-treated MCF-7/caspase-3 cells, were sequestered in a sedimentable fraction rather than released to the cytosol. These observations suggest that sequestration and inhibition of caspases can occur in some model systems, causing tetrapeptide-based activity assays to underestimate the amount of caspase activation that has occurred in situ.
J. Biol. Chem, 10.1074/jbc.M108419200
Submitted on August 31, 2001
Revised on October 24, 2001
Accepted on October 24, 2001
Lack of correlation between caspase activation and caspase activity assays in paclitaxel-treated MCF-7 breast cancer cells
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