title: Isolation and partial characterization of the formyl peptide receptor components on human neutrophils.
abstract: The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and approximately 40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa greater than approximately 40 kDa greater than 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP.
authors.affiliation: Department of Oral Biology, State University of New York, Buffalo.
authors.forename: E
authors.initials: E
authors.lastname: De Nardin
authors.forename: S J
authors.initials: SJ
authors.lastname: Radel
authors.forename: R J
authors.initials: RJ
authors.lastname: Genco
mesh_terms: D001667:Binding, Competitive; D006801:Humans; D008970:Molecular Weight; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000378:metabolism; D009504:Neutrophils / Q000378:metabolism*; D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic / Q000378:metabolism*; D012995:Solubility
chemical_list: D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic; D009240:N-Formylmethionine Leucyl-Phenylalanine