Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein.
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Carter DB, Deibel MR Jr, Dunn CJ, Tomich CS, Laborde AL, Slightom JL, Berger AE, Bienkowski MJ, Sun FF, McEwan RN, et al.
Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein.
Nature. 1990 Apr 12;344(6267):633-8.
- PubMed ID
- 2139180 [ View in PubMed]
- 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 T cells and endothelial cells in vitro and was a potent inhibitor of IL-1 induced corticosterone production in vivo.