Determination of a specific receptor for formyl-methionyl-leucyl-phenylalanine on the pulmonary alveolar macrophage and its relationship to chemotaxis and superoxide production

I. Spilberg, J. Mehta, C. Daughaday, L. Simchowitz

Research output: Contribution to journalArticle

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Abstract

3H-FMLP, a chemotactic peptide that resembles Escherichia coli chemotactic factor, is chemotactic for PAM, binds specifically to a site on the cell, and induces the generation of superoxide radicals by the cell. Scatchard analysis revealed an equilibrium dissociation constant at 26°C of 1.45 x 10-8M and the presence of 1.7 x 10-5 receptors per cell. Binding was not inhibited by a partially purified C5a preparation or by the neutrophil-derived CCF but was inhibited by various N-formylated peptides. The order of potency of each peptide to inhibit 3H-FMLP binding was identical to the order of potency of each peptide to induce generation of superoxide by the PAM. Only small amounts of β-glucuronidase activity and no lysozyme were detected in the supernatant after incubation of the cells for 30 min with varying concentrations of FMLP.

Original languageEnglish
Pages (from-to)602-609
Number of pages8
JournalJournal of Laboratory and Clinical Medicine
Volume97
Issue number5
StatePublished - Jan 1 1981

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