Interleukin-1β as a potent hyperalgesic agent antagonized by a tripeptide analogue

@article{Ferreira1988Interleukin1AA,
  title={Interleukin-1$\beta$ as a potent hyperalgesic agent antagonized by a tripeptide analogue},
  author={S{\'e}rgio H. Ferreira and Berenice B. Lorenzetti and Adrian F. Bristow and Stephen Poole},
  journal={Nature},
  year={1988},
  volume={334},
  pages={698-700}
}
Interleukin-1 (IL-1) describes two inflammatory proteins1, IL-1α and IL-1β, produced by activated macrophages and other cell types2 and encoded by two genes. Their amino acid sequences have only 26% similarity1, but their biological activities are comparable, with a few exceptions3,4; indeed, both molecules appear to act at the same receptor5,6. As IL-1 releases prostaglandins7 which sensitize nociceptors in man and in experimental animals8, we tested IL-1α and IL-1β in rats for hyperalgesic… 
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Interleukin-1 and interleukin-1 fragments as vaccine adjuvants.
TLDR
Human interleukin-1beta domain in position 163-171, comprising the amino acids VQGEESNDK, has been synthesized as a nine-amino-acid-long peptide and used in vivo as a nontoxic HCl salt, and the DNA sequence encoding the IL-1 beta domain has been included in an experimental DNA vaccine with positive results.
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It is shown here that the receptor for IL-1α on both murine and human cells is identical to that forIL-1β, which raises the issue of what separation, if any, there might be between the biological activities of IL- 1α and IL-2β.
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The iodination, to high specific activity and with retention of full biological potency, of the two types of natural porcine IL-1 are reported, and the two different II-1 proteins show a similar affinity for a common class of receptors.
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