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B During Primary B Cell Differentiation1
*
MSZ, Institut für Medizinische Strahlenkunde und Zellforschung, and
Pathologisches Institut, Universität Würzburg, Wurzburg, Germany;
Institute for Immunology, Basel, Switzerland
We have investigated activation of nuclear factor-
B (NF-B) in
the process of primary B cell differentiation in vitro. In this system,
NF-B is strongly induced when B cells develop from the pre-B cell to
the immature B cell stage. Unlike the typical NF-B activation in
response to exogenous stimuli, induction proceeds with a slow time
course. NF-B induction is only observed in B cells that undergo
differentiation, not in Rag2-deficient cells. Nuclear DNA binding
complexes predominantly comprise p50/RelA heterodimers and, to a lesser
extent, c-Rel-containing dimers. The increase in NF-B binding
activity is accompanied by a slow and steady decrease in IBß
protein levels. Interestingly, absolute RelA protein levels remain
unaffected, whereas RelB and c-Rel synthesis is induced. The reason for
preferential nuclear translocation of RelA complexes appears to be
selective inhibition by the IBß protein. IBß can efficiently
inhibit p50/RelA complexes, but has a much reduced ability to interfere
with p50/c-Rel DNA binding both in vitro and in vivo. Interestingly,
p50/RelB complexes are not at all targeted by IBß, and
coimmunoprecipitation experiments show no evidence for an association
of IBß and RelB in vivo. Consistent with these observations,
IBß cotransfection can inhibit p50/RelA-mediated
trans-activation, but barely affects p50/RelB mediated
trans-activation.
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