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CUTTING EDGE |
B Activation1
* Center for Immunology and Department of Molecular Biology & Biochemistry, University of California, Irvine. CA 92697; and
Amnis Corporation, Seattle, WA 98121
Recently, it has been demonstrated that stimulated T cells bearing defects in caspase-8 fail to promote nuclear shuttling of NF-
B complexes. Such cells display strikingly similar proliferative and survival defects as T cells lacking Fas-associated death domain protein (FADD) function. We characterized NF-B signaling in T cells bearing a dominant-negative FADD transgene (FADDdd). Whereas FADDdd T cells displayed proliferative defects following activation, these were not a consequence of aberrant NF-B signaling, as measured by IKK/IB phosphorylation and IB degradation. There were no appreciable defects in nuclear translocation of p65/Rel using ImageStream, a flow-based imaging cytometer. Pretreatment with benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone, a potent caspase inhibitor, also failed to impede canonical NF-B signaling. Secretion of IL-2 and up-regulation of various activation markers occurred normally. Thus, FADD does not play an essential role in NF-B activation, suggesting an alternative route by which this adaptor promotes the clonal expansion of T cells.
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