FEBS Letters | |
B cell receptor‐mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity | |
Turk, Boris1  Mlinaric-Rascan, Irena2  | |
[1] Department of Biochemistry and Molecular Biology, Josef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia;Faculty of Pharmacy, University of Ljubljana, Askerceva 7, 1000 Ljubljana, Slovenia | |
关键词: Caspase; Cathepsin; B cell receptor; Apoptosis; Inhibitor; Ac-DEVD.AMC; acetyl-Asp-Glu-Val-Asp-AMC; AFC; 7-amino-4-trifluoromethyl coumarin; AMC; 7-amino-4-methyl coumarin; DMSO; dimethylsulfoxide; fmk; fluoromethyl ketone; z-VAD.fmk; benzyloxycarbonyl-Val-Ala-Asp.fmk; z-FR.AFC; benzyloxycarbonyl-Phe-Arg-AFC; E-64d; (2S; 3S)-trans-epoxysuccinyl-leucylamido-3-methyl-butane ethyl ester; | |
DOI : 10.1016/S0014-5793(03)00966-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
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