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.

We have employed the baculovirus expression system for the production of insect cell membranes having GABA/benzodiazepine binding sites. Three recombinant baculoviruses each harboring a different GABAA receptor cDNA were introduced into insect cells by simultaneous infection. Infected cells expressed GABA responsive Cl- channels and benzodiazepine binding sites with the same pharmacological specificity as animal cells expressing these receptor subunits.

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