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pubmed-article:14550545pubmed:abstractTextCrosslinking of the WEHI 231 lymphoma B cell receptor (BCR) leads to growth arrest followed by apoptosis. In a study of the role of lysosomal cysteine proteinases in BCR-mediated apoptosis we provide evidence that commitment to apoptosis correlates with a time-dependent increase in caspase and cathepsin activities. We also show that activation of cathepsins is a caspase-independent process, and caspase cascade activation is independent of lysosomal endopeptidases. BCR-induced nuclear fragmentation was not prevented, but rather delayed in the absence of detectable caspase and cathepsin activities, suggesting that BCR-driven apoptosis of these cells may use an alternative proteolytic mechanism independent of caspases and cathepsins.lld:pubmed
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pubmed-article:14550545pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:14550545pubmed:articleTitleB cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity.lld:pubmed
pubmed-article:14550545pubmed:affiliationFaculty of Pharmacy, University of Ljubljana, Slovenia. irena.mlinaric@ffa.uni-lj.silld:pubmed
pubmed-article:14550545pubmed:publicationTypeJournal Articlelld:pubmed