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The Journal of Immunology, 2001, 166: 6473-6476.
Copyright © 2001 by The American Association of Immunologists

CUTTING EDGE

Cutting Edge: Cellular Fas-Associated Death Domain-Like IL-1-Converting Enzyme-Inhibitory Protein Protects Germinal Center B Cells from Apoptosis During Germinal Center Reactions

Marco van Eijk1,*, Jan Paul Medema{dagger} and Cornelis de Groot2,*

* Department of Cell Biology and Histology, Cellular Immunology Group, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands; and {dagger} Department of Immunohematology and Bloodbank, Leiden University Medical Center, Leiden, The Netherlands

During germinal center (GC) reactions, follicular dendritic cells are believed to select memory B lymphocytes by switching off apoptosis in the successfully binding B cells. The cellular signals involved in this process are largely unknown. Here, we show that GC B lymphocytes have a long isoform of the cellular homologue of the viral Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein (cFLIPL), which is capable of inhibiting death receptor-induced caspase activation. In isolated GC B cells, cFLIPL decays rapidly even without Fas ligation, and this results in activation of caspase activity and apoptosis. Contact with follicular dendritic cells prevents cFLIPL degradation and blocks all signs of apoptosis, even in the presence of anti-Fas Abs. cFLIPL expression is sustained by CD40 ligation as well, suggesting that at least at some stage of the GC reaction activated T cells may help selected B cells to leave the follicular dendritic cell network without becoming apoptotic.




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