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(Journal of Leukocyte Biology. 2002;72:810-818.)
© 2002 by Society for Leukocyte Biology

The chemoattractant Trp-Lys-Tyr-Met-Val-D-Met activates eosinophils through the formyl peptide receptor and one of its homologues, formyl peptide receptor-like 1

Lena Svensson*, Claes Dahlgren{dagger} and Christine Wennerås*

* Department of Clinical Bacteriology, Sahlgrenska University Hospital, Göteborg, Sweden; and
{dagger} Department of Rheumatology and Inflammation Research, Göteborg University, Sweden

Correspondence: Christine Wennerås, Department of Clinical Bacteriology, Sahlgrenska University Hospital, Guldhedsgatan 10, S-413 46 Göteborg, Sweden. E-mail: christine.wenneras{at}microbio.gu.se

Whereas prokaryotes use L- and D-isomers of amino acids in their protein synthesis, eukaryotic proteins as a rule incorporate only L-isomers. Hence, D-isomers may constitute danger signals to the innate immune system. A D-methionine-containing peptide, Trp-Lys-Tyr-Met-Val-D-Met-NH2 (WKYMVm), has been shown to be a stronger activator of neutrophils than f-Met-Leu-Phe. The aim of this study was to compare the responsiveness of eosinophils to WKYMVm with that of neutrophils. The peptide was found to induce chemotaxis and respiratory burst in eosinophils. However, it did not mobilize granule constituents, as evidenced by a lack of eosinophil cationic protein, eosinophil peroxidase, and interleukin-5 in the supernatants of stimulated eosinophils. In contrast, WKYMVm caused the release of complement receptor 3 from secretory vesicles in neutrophils. Different members of the formyl peptide receptor family were preferentially engaged by the peptide in the two classes of granulocytes: the formyl peptide receptor itself in eosinophils and formyl peptide receptor-like 1 in neutrophils.

Key Words: degranulation • chemotaxis • respiratory burst • eosinophil cationic protein • eosinophil peroxidase




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