rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2003-10-10
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pubmed:abstractText |
Crosslinking 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.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Oct
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
9
|
pubmed:volume |
553
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
51-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14550545-Antibodies,
pubmed-meshheading:14550545-Apoptosis,
pubmed-meshheading:14550545-B-Lymphocytes,
pubmed-meshheading:14550545-Caspases,
pubmed-meshheading:14550545-Cathepsins,
pubmed-meshheading:14550545-Cell Division,
pubmed-meshheading:14550545-Cysteine Endopeptidases,
pubmed-meshheading:14550545-DNA Fragmentation,
pubmed-meshheading:14550545-Enzyme Activation,
pubmed-meshheading:14550545-Humans,
pubmed-meshheading:14550545-Immunoglobulin M,
pubmed-meshheading:14550545-Leucine,
pubmed-meshheading:14550545-Peptide Hydrolases,
pubmed-meshheading:14550545-Protease Inhibitors,
pubmed-meshheading:14550545-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
B cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity.
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pubmed:affiliation |
Faculty of Pharmacy, University of Ljubljana, Slovenia. irena.mlinaric@ffa.uni-lj.si
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pubmed:publicationType |
Journal Article
|