cDNA cloning and characterization of the human interleukin 13 receptor alpha chain

We have cloned cDNAs corresponding to the human interleukin 13 receptor alpha chain (IL-13Ralpha). The protein has 76% homology to murine IL-13Ralpha, with 95% amino acid identity in the cytoplasmic domain. Only weak IL-13 binding activity was found in cells transfected with only IL-13Ralpha; howeve...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-11, Vol.271 (46), p.29265-29270
Main Authors: Aman, M J, Tayebi, N, Obiri, N I, Puri, R K, Modi, W S, Leonard, W J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Binding, Competitive
Cell Line, Transformed
Cloning, Molecular
DNA, Complementary
Humans
Hybrid Cells
Interleukin-13 - metabolism
Interleukin-13 Receptor alpha1 Subunit
Iodine Radioisotopes
Mice
Molecular Sequence Data
Protein Binding
Receptors, Interleukin - chemistry
Receptors, Interleukin - genetics
Receptors, Interleukin - metabolism
Receptors, Interleukin-13
Sequence Homology, Amino Acid
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Summary:We have cloned cDNAs corresponding to the human interleukin 13 receptor alpha chain (IL-13Ralpha). The protein has 76% homology to murine IL-13Ralpha, with 95% amino acid identity in the cytoplasmic domain. Only weak IL-13 binding activity was found in cells transfected with only IL-13Ralpha; however, the combination of both IL-13Ralpha and IL-4Ralpha resulted in substantial binding activity, with a Kd of approximately 400 pM, indicating that both chains are essential components of the IL-13 receptor. Whereas IL-13Ralpha serves as an alternative accessory protein to the common cytokine receptor gamma chain (gammac) for IL-4 signaling, it could not replace the function of gammac in allowing enhanced IL-2 binding activity. Nevertheless, the overall size and length of the cytoplasmic domain of IL-13Ralpha and gammac are similar, and like gammac, IL-13Ralpha is located on chromosome X.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.46.29265