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ABSTRACT: 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 ∼140-kDa glycoprotein (IL-4R) and the γ chain (γc) 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-4R 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.
Journal of Biological Chemistry 07/1996; 271(28):16921-16926. · 4.77 Impact Factor
