Abstract
Interleukin-1 (IL-1), a peptide hormone produced by activated macrophages, possesses the ability to modulate the proliferation, maturation and functional activation of a broad spectrum of cell types1–7 and may play a major role in the initiation and amplification of immune and inflammatory responses through its action on these diverse cell populations8. IL-1 exhibits microheterogeneity in terms of its relative molecular mass (Mr, 13,000–19,000) and charge properties8, and although murine IL-1 has been purified9,10 and some of its basic structure–function relationships have been elucidated8, it has proved difficult to prepare sufficient amounts of IL-1 for direct and detailed sequence and structural studies. Here we report the cloning, sequence analysis and expression of murine IL-1 cDNA in Escherichia coli. The IL-1 cDNA codes for a polypeptide precursor of 270 amino acids. Biologically active IL-1 was produced in E. coli by expressing the carboxy-terminal 156 amino acids of the IL-1 precursor.
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Lomedico, P., Gubler, U., Hellmann, C. et al. Cloning and expression of murine interleukin-1 cDNA in Escherichia coli. Nature 312, 458–462 (1984). https://doi.org/10.1038/312458a0
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DOI: https://doi.org/10.1038/312458a0
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