Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein
- 1 April 1990
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 344 (6267) , 633-638
- https://doi.org/10.1038/344633a0
Abstract
A human myelomonocytic cell line, U937, produced an interleukin-1 (IL-1) receptor antagonist protein (IRAP) which was purified and partially sequenced. A complementary DNA coding for IRAP was cloned and sequenced. The mature translation product of the cDNA has been expressed in Escherichia coli and was an active competitive inhibitor of the binding of IL-1 to the T-cell/fibroblast form of the IL-1 receptor. Recombinant IRAP specifically inhibited IL-1 bioactivity on ¤ cells and endothelial cells in vitro and was a potent inhibitor of IL-1 induced corticosterone production in vivoKeywords
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