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J. Biol. Chem., Vol. 268, Issue 10, 7125-7128, 04, 1993
B Moser, B Dewald, L Barella, C Schumacher, M Baggiolini and I Clark-Lewis
We have previously shown that the residues Glu4-Leu5-Arg6 (ELR) preceding
the first cysteine at the N terminus of the 72-residue form of
interleukin-8 (IL-8) are essential for receptor binding and neutrophil
activation (Clark-Lewis, I., Schumacher, C., Baggiolini, M., and Moser, B.
(1991) J. Biol. Chem. 266, 23128-23134). We have now synthesized a series
of analogs of IL-8(4-72), the truncated form of IL- 8 with the N-terminal
sequence ELRC, as potential IL-8 antagonists. Among 26 analogs with
deletions or amino acid replacements in the ELR region several inhibited
IL-8 function. The most potent were IL-8(6- 72), with Arg6 at the N
terminus, and IL-8,AAR(7-72) with N-terminal Ala4-Ala5 instead of
Glu4-Leu5. They inhibited IL-8 receptor binding, exocytosis (IC50 0.3
microM), as well as chemotaxis and the respiratory burst. Inhibition was
restricted to responses elicited by IL-8, GRO alpha, or NAP-2, and no
effect was observed when the unrelated agonists fMet-Leu-Phe or C5a were
used as stimuli. These results demonstrate that selective antagonists that
prevent or attenuate the action of IL-8 and its related chemotactic
cytokines are obtained by modification of the ELR sequence at the N
terminus.
Interleukin-8 antagonists generated by N-terminal modification
Theodor-Kocher Institute, University of Bern, Switzerland.
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