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Cell Immunol. 2000 Jan 10;199(1):50-7.

Induction of interleukin-12/p40 by superantigens in macrophages is mediated by activation of nuclear factor-kappaB.

Author information

1
Department of Neurology, Multiple Sclerosis Research Center, Vanderbilt University Medical Center, Nashville, Tennessee 37212, USA.

Abstract

Multimerization of the MHC class II molecule by superantigens results in activation of cellular signal transduction pathways in macrophage and B cells. Here we show that superantigen staphylococcal enterotoxin B (SEB) induces IL-12/p40 secretion in macrophages. SEB-induced expression of the IL-12/p40 gene involves activation and nuclear translocation of nuclear factor kappaB (NF-kappaB). The NF-kappaB heterodimer bound to the NF-kappaB consensus sequence of the IL-12/p40 gene promoter is p50/C-Rel. Inhibition of PKC and PKA activation results in suppression of activation and translocation of NF-kappaB. We conclude that signals for IL-12/p40 gene transcription from MHC class II molecules follow activation of PKC and PKA, which in turn leads to the activation and translocation of NF-kappaB to the nucleus. Our study suggests that superantigens are capable of influencing the nature of the immune response by regulating cytokine production. Induction of IL-12 production by superantigens may therefore play a role in the regulation of Th 1-mediated immune response and autoimmune disease.

PMID:
10675275
DOI:
10.1006/cimm.1999.1595
[Indexed for MEDLINE]

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