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American Journal of Pathology, Vol 111, 273-281, Copyright © 1983 by American Society for Investigative Pathology


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Characterization of the rat neutrophil formyl peptide chemotaxis receptor

WA Marasco, JC Fantone, RJ Freer and PA Ward

Numerous synthetic N-formylated peptides, believed to be the analogs of the naturally occurring initiating signal peptides produced by bacteria, are potent chemotactic agents for phagocytic cells in several species. The authors have characterized the receptor with moderately high affinity for the chemotactic peptide f-Met-Leu-[3H]Phe on the rat peritoneal neutrophils. When neutrophils are incubated with f-Met-Leu- [3H]Phe at 24 C, the binding is saturable and reversible. The receptor on the inflammatory rat neutrophils has an equilibrium dissociation constant (KD) of 3.4 x 10(-8) M at 24 C, and there are approximately 65,000 sites per cell. In addition, the potency of several of these chemotactic peptides in inducing lysosomal enzyme secretion and superoxide production correlated well with their ability to compete with f-Met-Leu-[3H]Phe for receptor binding. Structure activity studies further demonstrate that the fine specificity of the formyl peptide receptor has been conserved across species lines.


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J. S. Mills, H. M. Miettinen, D. Barnidge, M. J. Vlases, S. Wimer-Mackin, E. A. Dratz, J. Sunner, and A. J. Jesaitis
Identification of a Ligand Binding Site in the Human Neutrophil Formyl Peptide Receptor Using a Site-specific Fluorescent Photoaffinity Label and Mass Spectrometry
J. Biol. Chem., April 24, 1998; 273(17): 10428 - 10435.
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Copyright © 1983 by the American Society for Investigative Pathology.