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Science 1 April 1994:
Vol. 264. no. 5155, pp. 90 - 92
DOI: 10.1126/science.8140420
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Articles

Science, Vol 264, Issue 5155, 90-92
Copyright © 1994 by American Association for the Advancement of Science

articles

Neutrophil activation by monomeric interleukin-8

K Rajarathnam, BD Sykes, CM Kay, B Dewald, T Geiser, M Baggiolini, and I Clark-Lewis

Protein Engineering Network of Centres of Excellence (PENCE), University of Alberta, Edmonton, Canada.

Interleukin-8 (IL-8), a pro-inflammatory protein, has been shown by nuclear magnetic resonance (NMR) and x-ray techniques to exist as a homodimer. An IL-8 analog was chemically synthesized, with the amide nitrogen of leucine-25 methylated to selectivity block formation of hydrogen bonds between monomers and thereby prevent dimerization. This analog was shown to be a monomer, as assessed by analytical ultracentrifugation and NMR. Nevertheless, it was equivalent to IL-8 in assays of neutrophil activation, which indicates that the monomer is a functional form of IL-8.


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