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pubmed-article:7532676pubmed:abstractTextStimulation of B and T cells via the antigen receptor, by phorbol ester or by phorbol ester and ionomycin, leads to nuclear translocation of the inducible transcription factor NF-kappa B, comprising the p50 and p65 rel-related polypeptides. In this report we show that c-rel is a component of the antigen receptor-induced kappa B binding proteins in both B and T cells. Whereas NF-kappa B can be induced by phorbol ester alone, optimal induction of c-rel requires stimulation by both phorbol ester and ionomycin, the dual signal that is necessary for proliferation of untransformed lymphocytes. Furthermore, c-rel induction is blocked by the immunosuppressive drug FK506 that is known to inhibit B and T cell activation. c-rel-dependent transactivation of the interleukin-2 receptor alpha chain (IL-2R alpha) promoter is augmented by coexpression of calcineurin, suggesting the involvement of a calcineurin-dependent intracellular pathway. Our results identify c-rel as a target of immunosuppressive agents and illustrate the similarity of activation pathways in both B and T cells.lld:pubmed
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pubmed-article:7532676pubmed:authorpubmed-author:BurakoffS JSJlld:pubmed
pubmed-article:7532676pubmed:authorpubmed-author:SenRRlld:pubmed
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pubmed-article:7532676pubmed:articleTitleFK506 inhibits antigen receptor-mediated induction of c-rel in B and T lymphoid cells.lld:pubmed
pubmed-article:7532676pubmed:affiliationRosenstiel Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.lld:pubmed
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