The Production and Characterization of a Modified Recombinant Interleukin-1 Receptor Antagonist

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Abstract
The increasingly complex cytokine network involves both positive and negative regulatory pathways. Natural inhibitors of cytokines are of great importance both as analytical tools and as potential therapeutic agents. Interleukin-1 (IL-1) inhibitory bioactivity including a specific receptor antagonist of IL-1 (IL-lra) has been described both in cultured cell supernatants and in human body fluids. In the current studies, the cDNA of IL-lra from human monocytes was obtained by the techniques of mRNA isolation and reverse transcription/polymerase chain reaction (RT/PCR). The IL-lra cDNA/pET-15b was transfected into DE3 cells and the recombinant protein expressed. The purified protein was demonstrated as a single band with molecular mass of 20KD by SDS-PAGE; it had strong IL-1 inhibitory activity. This IL-1 inhibitor competed with IL-1 for their receptor as assesed by flow cytometer. The existence of this naturally occurring specific cytokine receptor antagonist may lead to a different perspective of the cytokine network. The availability of this recombinant IL-1 receptor antagonist allows us to test its role on the cytokine network, and on possible disease modification.

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