Two-chain structure of the interleukin 1 receptor

By crosslinking radioiodinated recombinant human IL1 α to mouse EL4 thymoma cells we have identified in addition to the known IL1-binding proteins of 80 kDa, a second IL1-binding protein of about 40 kDa. This second binding protein could be demonstrated most easily when crosslinking to higher protei...

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Bibliographic Details
Published in:FEBS letters 1988-02, Vol.229 (1), p.59-62
Main Authors: Kroggel, Roswitha, Martin, M., Pingoud, Vera, Dayer, J.M., Resch, K.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cell Line
Cell receptors
Cell structures and functions
Cross-linking
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Interleukin 1 receptor
Interleukin-1 - metabolism
Macromolecular Substances
Mice
Molecular and cellular biology
Molecular Weight
Receptors, Immunologic - analysis
Receptors, Interleukin-1
Recombinant interleukin 1
Recombinant Proteins - metabolism
Thymoma - metabolism
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Summary:By crosslinking radioiodinated recombinant human IL1 α to mouse EL4 thymoma cells we have identified in addition to the known IL1-binding proteins of 80 kDa, a second IL1-binding protein of about 40 kDa. This second binding protein could be demonstrated most easily when crosslinking to higher protein complexes was inhibited. This finding suggests that the IL1 receptor, similar to the receptor for other cytokines such as interleukin 2, is composed of a heterodimer, of which both polypeptides contribute to ligand binding.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80797-X