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Reductions in IB and Changes in NF-B Activity during B Lymphocyte Differentiation¹

Stefan Doerre^*, Kristin Perkins Mesires^*, Kylle M. Daley^*, Thomas McCarty, Sonja Knoetig and Ronald B. Corley^2,*

^* Department of Microbiology, Boston University School of Medicine, Boston, MA 02118; and Laboratory of Immunopathology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892

The levels and stability of IB have been examined in unstimulated and stimulated splenic B cells and compared with that of IB and IB. Primary murine splenic B cells but not T cells were found to contain high levels of IB protein, equivalent to levels of the abundant IB. Most agents that activate IB and IB degradation do not induce rapid degradation of IB. Interestingly, however, the levels of IB, but not of IB or IB, are dramatically reduced upon the stimulation of B cells both in vivo and in vitro. Since IB exhibits substrate specificity for NF-B Rel homodimers, this suggested the possibility that changes in NF-B-responsive genes might also occur during this transition. Consistent with this hypothesis, we found that a NF-B reporter construct sensitive to p65/RelA homodimers is activated at the time that IB levels decline following B cell stimulation. In IgG⁺ B cell lines, which contain low levels of IB, this same reporter construct was inactive, suggesting that the increases in Rel homodimer activity that accompany B cell stimulation are transient. However, there are differences in the level of expression of NF-B-responsive genes in these IgG⁺ B cell lines compared with their IgM⁺ counterparts. From these data, we conclude that there are transient changes in NF-B activity due to reductions in IB, which might contribute to long-term, persistent changes that accompany B cell differentiation. We propose an important role for IB in the differential regulation of nuclear NF-B activity in stimulated B cells.

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