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PMID: 9022011 Published · ppublish English Journal Article

Regulation of interleukin-12 receptor beta1 chain expression and interleukin-12 binding by human peripheral blood mononuclear cells.

European journal of immunology ·Vol. 27 ·No. 1 ·1997-01-00 ·Pages 147-54

Wu C, Warrier RR, Wang X, Presky DH, Gately MK

Abstract

The interleukin-12 receptor (IL-12R)beta1 chain is an essential component of the functional IL-12R on both human T and natural killer cells. In this report it is shown that activation of human peripheral blood mononuclear cells (PBMC) with anti-CD3 monoclonal antibody (mAb) or phytohemagglutinin resulted in the up-regulation of IL-12Rbeta1 expression and IL-12 binding. Kinetic studies revealed that maximum expression of IL-12Rbeta1 and IL-12 binding occurred on days 3-4. Anti-CD3-induced expression of IL-12Rbeta1 chain and IL-12 binding by PBMC was augmented by anti-CD28 mAb, indicating that the potentiating effect of anti-CD28 on T cell responses to IL-12 could be mediated, at least in part, by the enhancement of IL-12R expression. Among 16 cytokines tested, IL-2, IL-7 and IL-15 markedly induced IL-12Rbeta1 expression and IL-12 binding on resting PBMC, whereas IL-1alpha and tumor necrosis factor-alpha had a minimal enhancing effect. In contrast, IL-3, IL-4, IL-5, IL-6, IL-8, IL-10, IL-12, interferon (IFN)-alpha, IFN-gamma, granulocyte/macrophage colony-stimulating factor and transforming growth factor (TGF)-beta2 had no detectable enhancing effect. Anti-CD3-induced expression of IL-12Rbeta1 and of low-affinity IL-12 binding sites was partially inhibited by TGF-beta2, IL-10 and IL-4; however, TGF-beta2 and IL-10 completely abolished anti-CD3-induced expression of high-affinity IL-12 binding sites. Consistent with the reduction of high affinity IL-12 binding sites, PBMC activated with anti-CD3 mAb in the presence of TGF-beta2 or IL-10 failed to produce IFN-gamma or to proliferate in response to IL-12. These results suggest that Th2 cell-derived cytokines can inhibit IL-12-induced biological functions by inhibiting IL-12R expression and that expression of a second subunit of the IL-12R (IL-12Rbeta2), required for the formation of high-affinity IL-12 binding sites, may be more highly regulated by TGF-beta2 and IL-10 than is expression of IL-12Rbeta1.

MeSH Terms
CD28 Antigens/physiology CD3 Complex/physiology Cells, Cultured Humans Interferon-gamma/biosynthesis Interleukin-10/physiology Interleukin-12/physiology Interleukin-4/physiology Leukocytes, Mononuclear/immunology Lymphocyte Activation Receptors, Interleukin/physiology Receptors, Interleukin-12 Signal Transduction T-Lymphocytes/immunology Transforming Growth Factor beta/physiology
Chemicals
CD28 Antigens CD3 Complex IL12RB1 protein, human IL12RB2 protein, human Receptors, Interleukin Receptors, Interleukin-12 Transforming Growth Factor beta Interleukin-10 Interleukin-12 Interleukin-4 Interferon-gamma
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wu C
Department of Inflammation/Autoimmune Diseases, Hoffmann-La Roche Inc., Nutley, NJ 07110, USA.
Warrier R R
Wang X
Presky D H
Gately M K
Article Info
Journal
European journal of immunology
Abbr.
Eur J Immunol
ISSN
0014-2980
Published
1997-01-00
Pages
147-54
Language
English
Region
Germany
NLM ID
1273201
Subset
IM
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