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*
Department of Pharmacology, College of Medicine, University of Illinois, Chicago, IL 60612; and
Laboratory of Molecular Immunoregulation, Division of Basic Sciences, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, MD 21702
Formyl peptides are potent neutrophil chemoattractants. In humans
and rabbits, the formyl peptide receptor (FPR) binds
N-formyl-Met-Leu-Phe (fMLF) with high affinity
(Kd 
1 nM). The mouse FPR (mFPR) is
a low-affinity receptor for fMLF (Kd
100 nM); therefore, other agonists for this receptor may exist.
Using mFPR-transfected rat basophilic leukemia cells, we found that a
recently identified synthetic peptide
Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm) is a potent agonist for
mFPR. WKYMVm induced calcium mobilization with an EC50 of
1.2–1.5 nM. Optimal chemotaxis was achieved with 1 nM of WKYMVm, but
it required 100 nM of fMLF. WKYMVm stimulated rapid and potent
phosphorylation of the mitogen-activated protein kinases extracellular
signal-related kinases 1 and 2 when used at 50 nM. Pertussis toxin only
partially blocked calcium mobilization and production of inositol
1,4,5-trisphosphate in the stimulated mFPR cells, suggesting the
possibility that this receptor couples to G
proteins other than Gi
and Go. Competitive binding and desensitization data suggest that both
peptides interact with the same receptor but may use nonoverlapping
binding sites because WKYMVm was unable to effectively displace
[3H]fMLF bound to mFPR. These results provide evidence
for the presence of an alternative potent agonist for mFPR, and suggest
a potential usage of WKYMVm for probing the ligand-receptor
interactions with the murine formyl peptide receptor
homologs.
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