Fibronectin receptor of human macrophages recognizes the sequence Arg-Gly-Asp-Ser.

作者：Samuel D. Wright, B C Meyer · 发表于：The Journal of Experimental Medicine · 年份：1985 · DOI：10.1084/jem.162.2.762 · 被引用次数：109 · 研究领域：Cell Adhesion Molecules Research、Monoclonal and Polyclonal Antibodies Research、Peptidase Inhibition and Analysis

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.