人类巨噬细胞的纤连蛋白受体识别序列精氨酸-甘氨酸-天冬氨酸-丝氨酸。
Fibronectin receptor of human macrophages recognizes the sequence Arg-Gly-Asp-Ser.
作者信息
Wright S D, Meyer B C
出版信息
J Exp Med. 1985 Aug 1;162(2):762-7. doi: 10.1084/jem.162.2.762.
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.
摘要
当培养的人单核细胞（MO）铺展在纤连蛋白（Fn）包被的表面时，MO上的C3受体表现出促进吞噬作用的能力显著增强。Fn对C3受体的激活是由一种识别Fn细胞结合域中存在的序列Arg-Gly-Asp-Ser（RGDS）的受体介导的。可溶性含RGDS肽可抑制表面结合的Fn引起的C3受体激活，而表面结合的含RGDS肽本身可引起附着MO的C3受体激活。尽管可溶性含RGDS肽与Fn受体结合，但这种单价连接不足以激活C3受体。
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