A recombinant extracellular domain of the human interleukin 4 receptor inhibits the biological effects of interleukin 4 on T and B lymphocytes

Eur J Immunol. 1991 Jun;21(6):1365-9. doi: 10.1002/eji.1830210606.


Human interleukin 4 (IL4) acts on various hematopoietic cell types through interaction with a specific cell surface receptor (IL4R), whose cDNA has been cloned. We have produced a cDNA encoding a soluble form of the extracellular domain of the human IL 4R (sIL4R) and describe here the capacity of sIL4R to antagonize the in vitro activities of IL4 on normal B and T lymphocytes. sIL4R inhibited IL4-induced proliferation of both phytohemagglutinin-preactivated peripheral blood mononuclear cells (PBMC) and anti-IgM co-stimulated tonsil B cells with similar efficiency. This inhibitory activity was specific since sIL4R did not affect IL2-dependent proliferation of these cells. sIL4R also blocked IL4-dependent induction of the low-affinity receptor for IgE on B cells and inhibited IgE production by IL4-activated PBMC. Thus, in contrast to the IL6R extracellular domain which stimulates IL6 biological activity, the IL4R extracellular domain is a powerful antagonist of its specific ligand.

MeSH terms

  • Antibodies, Anti-Idiotypic / immunology
  • Antigens, Differentiation, B-Lymphocyte / analysis
  • B-Lymphocytes / drug effects*
  • Cells, Cultured
  • Humans
  • Immunoglobulin E / biosynthesis
  • Immunoglobulin M / immunology
  • Interleukin-2 / pharmacology
  • Interleukin-4 / antagonists & inhibitors*
  • Lymphocyte Activation / drug effects
  • Receptors, Fc / analysis
  • Receptors, IgE
  • Receptors, Interleukin-4
  • Receptors, Mitogen / physiology*
  • Recombinant Proteins / pharmacology
  • T-Lymphocytes / drug effects*


  • Antibodies, Anti-Idiotypic
  • Antigens, Differentiation, B-Lymphocyte
  • Immunoglobulin M
  • Interleukin-2
  • Receptors, Fc
  • Receptors, IgE
  • Receptors, Interleukin-4
  • Receptors, Mitogen
  • Recombinant Proteins
  • Interleukin-4
  • Immunoglobulin E