High affinity binding of human interleukin 4 to cell lines

Cabrillat, H.; Galizzi, Jean‐Pierre; Djossou, Odile; Arai, Naoko; Yokota, Takashi; Arai, Kohei; Banchereau, Jacques

doi:10.1016/0006-291x(87)90507-9

Cited by 66 publications

(20 citation statements)

References 11 publications

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“…Originally described as a B cell growth and differentiation factor, IL4 has been shown to stimulate the production of IgG, IgM [3] and IgE [4] by B cells as well as inducing the expression of low-affinity IgE receptors (FceR/CD23) . Recently, IL4 has been recognized as a T cell growth factor in human [8,91 and murine [lo-141 systems where it probably acts in an autocrine manner similar to IL 2 [13, 141. Studies on IL4R in murine [15][16][17] and human [7,181 T cells have revealed 100-1000 high-affinity receptors (& -100 pM/ cell). The IL4R, like the IL2R, is up-regulated by its ligand [16].…”

Section: Introductionmentioning

confidence: 99%

Identification of interleukin 4 receptor‐associated proteins and expression of both high‐ and low‐affinity binding on human lymphoid cells

1989

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Interleukin 4 (IL4) produced by activated T cells expresses its biological effects on T and B lymphocytes by binding to specific membrane receptors. Cross-linking of human recombinant 125I-IL4 to peripheral blood mononuclear cells identifies a trimolecular complex consisting of a 65/70-kDa doublet and a 110-kDa protein. Scatchard analysis reveals about 300 IL4 binding sites/cell on resting cells with an equilibrium binding constant (Kd) of approximately 100 pM. Stimulation by anti-CD3 antibodies causes an up-regulation of IL4 receptors by a factor of 2 to 3 without any change in binding affinity. In addition to this high-affinity binding site a second class of a previously unidentified, low-affinity receptor (Kd approximately 30 nM, approximately 9000 sites/cell) is expressed on resting lymphocytes. The number of low-affinity binding sites for IL 4 also increases twofold upon cell activation. Exogenous IL 4 enhances the expression of its receptor on resting lymphocytes and this effect is further increased by anti-CD3 activation. Binding of IL4 to its receptor is specific, being only inhibited by IL 4 and not by IL2. By contrast, the gibbon leukemia cell line MLA 144 expresses only high-affinity receptors for IL4. Cross-linking studies reveal a 45/50-kDa IL 4 receptor-associated doublet in addition to the three proteins identified in human peripheral blood mononuclear cells. The functional significance of the different proteins composing the receptor for IL4 is discussed.

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Section: Introductionmentioning

confidence: 99%

Identification of interleukin 4 receptor‐associated proteins and expression of both high‐ and low‐affinity binding on human lymphoid cells

1989

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“…Iodination of recornbinant human and murine IL-4 was performed as described (Cabrillat et al, 1987). The specific activity of radiolabelled hIL-4 was determined by competion binding measurements using a solid-phase binding assay based o n the recombinant extracellular domain of hlL-4Rn (Kruse et al, 1993): the specific activity of mIL-4 was estimated by analogy.…”

Section: Stable Transfection Of Mouse Cells Fdc-4g and Ba/f3mentioning

confidence: 99%

Different Human Interleukin‐4 Mutants Preferentially Activate Human or Murine Common Receptor γ Chain

Lischke

Kammer

Friedrich

1995

European Journal of Biochemistry

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Interleukin-4 (IL-4) shows species-specific activity due to species-restricted interaction with the IL-4 receptor a (IL-4Ra) chain. The second subunit of a functional IL-4 receptor, the common 7 chain (yJ, is more promiscuous, since human IL-4 is able to activate IL-4 receptor complexes containing either human or murine common 7 receptor chain (yJ. We have stably transfected factor-dependent mouse cells of myeloid and lymphoid origin with combinations of human IL-4Ra and yc derivatives. In these cell lines, both human and murine yc receptors as well as IL-4Ra chains from both species are simultaneously expressed. Both versions of' yc readily form ternary complexes with either human IL-4 and human IL-4Ra or murine I t -4 and murine IL-4Ra. Due to distinct ligand-binding properties of human and murine yL, the two receptor complexes can be activated preferentially by different mutant variants of human IL-4. The contribution of murine common 7 chain to human TL-4-induced signal transduction is suppressed by an inhibitory antibody directed to the extracellular domain of the mouse yC. We present evidence that the two IL-4R complexes functionally interfere with each other and compete for responselimiting signalling components.

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“…Interleukin 4 (IL4) produced by T lymphocytes [21] and mast cells [22], displays a wide range of biological effects [23,24] as suggested by the expression of its specific receptor in nearly all the cell types [25,26]. Up to now, the effects of IL4 on the production of acute-phase proteins by hepatocytes have not been studied.…”

Section: Introductionmentioning

confidence: 99%

Interleukin 4 inhibits the production of some acute‐phase proteins by human hepatocytes in primary culture

et al. 1993

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Interleukin 4 (X4) has been shown to exhibit anti-inflammatory effects by inhibiting the secretion by monocytes of proinflammatory cytokines such as interleukin 1 (ILl), interleukin 6 (IL6), and tumor necrosis factor (TNF) and by inducing the secretion of the IL1 receptor antagonist. We investigated the role of this cytokine on the production of acute-phase proteins in primary human hepatocyte cultures. Cells were. exposed to either IL4 and/or IL6, the most potent mediator of hepatic acute phase proteins. IL4 led to decreased production of haptoglobin, C-reactive protein and albumin while ccl-antitrypsin and fibrinogen remained unaffected. These inhibitory effects of IL4 were also observed at the mRNA level. In addition, IL4 inhibited the IL6-induced production of haptoglobin although it had no effect on the induced C-reactive protein and fibrinogen. Our results demonstrate that IL4 can affect the production of a subset of acute-phase proteins by human hepatocytes and can antagonize some of the effects of IL6. These observations reinforce the notion that IL4 can be considered as an anti-inflammatory cytokine.

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High affinity binding of human interleukin 4 to cell lines

Cited by 66 publications

References 11 publications

Identification of interleukin 4 receptor‐associated proteins and expression of both high‐ and low‐affinity binding on human lymphoid cells

Identification of interleukin 4 receptor‐associated proteins and expression of both high‐ and low‐affinity binding on human lymphoid cells

Different Human Interleukin‐4 Mutants Preferentially Activate Human or Murine Common Receptor γ Chain

Interleukin 4 inhibits the production of some acute‐phase proteins by human hepatocytes in primary culture

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