IL-4, a pleiotropic cytokine produced by T lymphocytes, plays an important role in immune responsiveness by regulating proliferation and differentiation of a variety of lymphoid and myeloid cells via binding to high affinity receptors. In this report we describe the isolation and functional expression of a human IL-4-R cDNA. When transfected into COS-7 cells, the cDNA encodes a 140-kD cell-surface protein. After transfection into a murine T cell line, the cDNA encodes a protein that binds human IL-4 with high affinity and can confer responsiveness to human IL-4. The predicted extracellular domain of the IL-4-R exhibits significant amino acid sequence homology with the beta subunit of the IL-2-R (p75), and the receptors for IL-6, erythropoietin, and prolactin. These receptors comprise a novel superfamily with extracellular domains characterized by four conserved cysteine residues and a double tryptophan-serine (WSXWS) motif located proximal to the transmembrane region.
Human interleukin 4 receptor confers biological responsiveness and defines a novel receptor superfamily.
R L Idzerda, C J March, B Mosley, S D Lyman, T Vanden Bos, S D Gimpel, W S Din, K H Grabstein, M B Widmer, L S Park; Human interleukin 4 receptor confers biological responsiveness and defines a novel receptor superfamily.. J Exp Med 1 March 1990; 171 (3): 861–873. doi: https://doi.org/10.1084/jem.171.3.861
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