TI  - Cloning and characterization of a specific <prot>interleukin (IL)-13</prot> binding
      protein structurally related to the <prot><prot>IL-5</prot> receptor</prot> alpha chain.
PG  - 16921-6
AB  - <prot>Interleukin-13</prot> (<prot>IL-13</prot>) is a cytokine secreted by activated T lymphocytes
      that shares many, but not all, biological activities with <prot>IL-4</prot>. These
      overlapping activities are probably due to the existence of common
      receptor components. Two proteins have been described as constituents of
      the <prot>IL-4</prot> receptor, a approximately 140-kDa glycoprotein ( <prot>IL-4R</prot> ) and the
       gamma chain (gammac)  of the <prot><prot>IL-2</prot> receptor</prot>, but neither of these proteins
      binds <prot>IL-13</prot>. We have cloned a cDNA encoding an  <prot>IL-13</prot>  binding protein
      ( <prot>IL-13R</prot> ) 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 <prot>IL-13R</prot> shows homology with the <prot>IL-5</prot> receptor, and to
      a lesser extent, with the prolactin receptor. COS-7 cells transfected with
      the  <prot>IL-13R</prot>  cDNA bind  <prot>IL-13</prot>  with high affinity but do not bind <prot>IL-4</prot>. COS-7
      cells co-transfected with the cloned <prot>IL-13R</prot> cDNA and <prot>IL-4R</prot> cDNA resulted
      in the reconstitution of a small number of receptors that recognized both
      <prot>IL-4</prot> and <prot>IL-13</prot>. Reverse transcription-polymerase chain reaction analysis
      detected the receptor transcript only in cell lines known to bind <prot>IL-13</prot>.
AD  - Sanofi Recherche, BP 137, 31676 Labege Cedex, France.
