Neutrophil activation by monomeric interleukin-8.

Rajarathnam, K; Sykes, B D; Kay, C M; Dewald, B; Geiser, T; Baggiolini, M; Clark-Lewis, I · Science · 1994

basic_science · Level V

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Abstract

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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