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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1810-1818
The synthetic chemoattractant Trp-Lys-Tyr-Met-Val-DMet activates
neutrophils preferentially through the lipoxin A4 receptor
Claes Dahlgren,
Thierry Christophe,
Francois Boulay,
Phoebus N. Madianos,
Marie J. Rabiet, and
Anna Karlsson
From the The Phagocyte Research Laboratory, Department of Medical
Microbiology and Immunology, and Department of Oral Microbiology,
University of Göteborg, Göteborg, Sweden, and DBMS/BBSI
(UMR 314, CEA/CNRS) CEA-Grenoble, France.
A D-methionine-containing peptide,
Trp-Lys-Tyr-Met-Val-D-Met-NH2 (WKYMVm), featuring a unique
receptor specificity was investigated with respect to its ability to
activate neutrophil effector functions. The peptide was found to be
more potent than the N-formylated peptide N-formyl-Met-Leu-Phe (fMLF)
at inducing neutrophil chemotaxis, mobilization of neutrophil
complement receptor 3 (CR3), and activation of the neutrophil
NADPH-oxidase. The fact that binding of fML[3H]F was
inhibited by both fMLF and WKYMVm suggests that N-formyl peptide
receptor (FPR) is shared by these peptides. However, the neutrophil
response induced by the WKYMVm peptide was insensitive to the fMLF
antagonists, cyclosporin H, and Boc-FLFLF that specifically block the
function of the FPR. These results suggest that even though WKYMVm may
bind FPR the cells are activated preferentially through a receptor
distinct from the FPR. Using transfected HL-60 cells expressing either
the FPR or its neutrophil homologue FPRL1, also referred to as
LXA4R because it has been shown to bind lipoxin A4, we show that WKYMVm is about 300-fold more active at
mobilizing intracellular calcium through FPRL1 than through FPR. The
WKYMVm activates FPRL1-expressing cells in a cyclosporin H-independent manner with an EC50 of around 75 pmol/L, whereas it
activates FPR-expressing cells with an EC50 of around 25 nmol/L. The observation that exudated cells are primed in their
response to WKYMVm suggests that FPRL1/LXA4R like FPR is
stored in mobilizable organelles.
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