Cloning and characterization of a specific interleukin (IL)-13 binding protein structurally related to the IL-5 receptor alpha chain.
J Biol Chem
; 271(28): 16921-6, 1996 Jul 12.
Article
de En
| MEDLINE
| ID: mdl-8663118
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 approximately 140-kDa glycoprotein (IL-4R) and the gamma chain (gammac) 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.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Antigènes CD
/
Récepteurs aux interleukines
/
Interleukine-13
Limites:
Animals
/
Humans
Langue:
En
Journal:
J Biol Chem
Année:
1996
Type de document:
Article
Pays d'affiliation:
France