Abstract
When cultured human monocytes (MO) were spread on fibronectin (Fn)-coated surfaces, C3 receptors on the MO exhibited markedly enhanced capacity to promote phagocytosis. The activation of C3 receptors by Fn was mediated by a receptor that recognizes a sequence, Arg-Gly-Asp-Ser (RGDS), present in the cell-binding domain of Fn. Soluble, RGDS-containing peptides inhibited the activation of C3 receptors caused by surface-bound Fn, and surface-bound, RGDS-containing peptides themselves caused activation of the C3 receptors of attached MO. Although soluble, RGDS-containing peptides bound to Fn receptors, such monovalent ligation was insufficient to activate C3 receptors.
MeSH Terms
Amino Acid Sequence
Fibronectins/pharmacology
Humans
In Vitro Techniques
Macrophage-1 Antigen
Macrophages/drug effects,immunology,metabolism
Oligopeptides/metabolism,pharmacology
Phagocytosis/drug effects
Receptors, Complement/metabolism
Receptors, Fibronectin
Receptors, Immunologic/metabolism
Chemicals
Fibronectins
Macrophage-1 Antigen
Oligopeptides
Receptors, Complement
Receptors, Fibronectin
Receptors, Immunologic
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wright S D
Meyer B C
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