Two‐chain structure of the interleukin 1 receptor
- 29 February 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 229 (1) , 59-62
- https://doi.org/10.1016/0014-5793(88)80797-x
Abstract
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 bindingKeywords
This publication has 7 references indexed in Scilit:
- The two-chain structure of high-affinity IL-2 receptorsImmunology Today, 1987
- Identification of the plasma membrane receptor for interleukin‐1 on mouse thymoma cellsFEBS Letters, 1987
- Studies on the fate of receptor-bound 125I-interleukin 1 beta in porcine synovial fibroblasts.The Journal of Immunology, 1987
- Expression in Escherichia coli of fully active recombinant human IL 1 beta: comparison with native human IL 1 beta.The Journal of Immunology, 1987
- Properties of a specific interleukin 1 (IL 1) receptor on human Epstein Barr virus-transformed B lymphocytes: identity of the receptor for IL 1-alpha and IL 1-beta.The Journal of Immunology, 1986
- Similarity between the interleukin 1 receptors on a murine T-lymphoma cell line and on a murine fibroblast cell line.Proceedings of the National Academy of Sciences, 1986
- Nucleotide sequence of human monocyte interleukin 1 precursor cDNA.Proceedings of the National Academy of Sciences, 1984