Open AccessReceptor-specific induction of NF-kappaB components in primary B cells
Author(s) -
Delicia A. Francis,
Ranjan Sen,
Nancy R. Rice,
Thomas L. Rothstein
Publication year - 1998
Publication title -
international immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.86
H-Index - 134
eISSN - 1460-2377
pISSN - 0953-8178
DOI - 10.1093/intimm/10.3.285
Subject(s) - relb , cd40 , nf κb , transcription factor , microbiology and biotechnology , receptor , nfkb1 , western blot , electrophoretic mobility shift assay , biology , signal transduction , intracellular , jurkat cells , immune system , chemistry , t cell , immunology , gene , biochemistry , cytotoxic t cell , in vitro
The NF-kappaB transcription factor complex plays a key role in the expression of genes involved in immune responses. Nuclear NF-kappaB is induced in B lymphocytes by engagement of either the antigen receptor (sIg) or the CD40 receptor for a T cell activation antigen, although different intracellular pathways appear to be involved. In the present study the protein composition of NF-kappaB complexes triggered by sIg and CD40 was probed by electrophoretic mobility shift, supershift, shift-Western, and Western blot analyses. At the time of peak NF-kappaB induction (2 h), the NF-kappaB components detected in the complexes induced through sIg and through CD40 were the same. However, with continued stimulation RelB completely disappeared from anti-Ig-stimulated kappaB binding material, but remained a component of CD40L-induced NF-kappaB. The loss of DNA-binding RelB from anti-Ig-induced NF-kappaB did not result from depletion of RelB from B cell nuclei, suggesting specific regulation of RelB function which is not directly attributed to IkappaB function. These results indicate that NF-kappaB complexes may undergo protein-specific alterations in a time- and receptor-dependent fashion that may be associated with differences in the outcomes of B cell stimulation through sIg and CD40.