Molecular cloning of a cDNA encoding the human interleukin 4 receptor

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Abstract
Using the mouse interleukin 4 (IL-4) receptor cDNA as a probe, we Isolated a cDNA encoding the human IL-4 receptor (hlL-4 receptor) from a multlfactor-responsive human myeloid cell line, TF1. The cDNA encodes for an open reading frame of 825 amino acids Including a signal sequence (25 amino acids), the external domain (207 amlno acids), a transmembrane domain (24 amlno acids), and a large cytoplasmlc domain (569 amino acids). The human IL-4 receptor has a 65% identity with the mouse IL-4 receptor at the nucleic acid level and retains the typical structural motif of the previously described cytokine receptor family. COS7 cells transfected with the full-length cDNA expressed high levels (140, 000 sites/cell) of IL-4 binding sites, with a Kd = 80 pM, an affinity Identical to that of the original TF1 cells. Similar to IL-4 responsive cells, cross-linking of [125l]IL-4 to COS7 cells transfected with the cDNA showed a major protein of 130–150 kd and minor species of 55–85 kd.