Cloning and characterization of a specific interleukin (IL)-13 binding protein structurally related to the IL-5 receptor alpha chain

Interleukin-13 (IL-13) is a cytokine secreted by activated T lymphocytes that shares many, but not all, biological activities with IL-4. These overlapping activities are probably due to the existence of common receptor components, Two proteins have been described as constituents of the IL-4 receptor, a similar to 140-kDa glycoprotein (IL-4R) and the gamma chain (gamma c) of the IL-2 receptor, but neither of these proteins binds IL-13, We have cloned a cDNA encoding an IL-13 binding protein (IL-13R) from the Caki-1 human renal carcinoma cell line. The cloned cDNA encodes a 380-amino acid protein with two consensus patterns characteristic of the hematopoietic cytokine receptor family and a short cytoplasmic tail, The IL-13R shows homology with the IL-5 receptor, and to a lesser extent, with the prolactin receptor, COS-7 cells transfected with the IL-13R cDNA bind IL-13 with high affinity but do not bind IL-4, COS-7 cells co transfected with the cloned IL-13R cDNA and IL-CR cDNA resulted in the reconstitution of a small number of receptors that recognized both IL-4 and IL-13, Reverse transcription-polymerase chain reaction analysis detected the receptor transcript only in cell lines known to bind IL-13.