RGD-containing ankyrin externalized onto the cell surface triggers αVβ3 integrin-mediated erythrophagocytosis.
RGD-containing ankyrin externalized onto the cell surface triggers αVβ3 integrin-mediated erythrophagocytosis.
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含有 RGD 的锚蛋白外化到细胞表面触发 αVβ3 整合素介导的噬红细胞作用。
DOI：
10.1016/j.bbrc.2011.03.035
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发表时间：
2011
影响因子：
3.1
通讯作者：
Sung,LanpingAmy
中科院分区：
文献类型：
--
作者：
Peng,Weiyan;Sung,LanpingAmy
细胞外基质或细胞表面的RGD基序及其整合素受体构成了细胞粘附的主要识别系统。有几种主要的红细胞膜骨架蛋白，如α谱蛋白、锚蛋白和蛋白4.2，具有RGD基序。然而，在红细胞吞噬过程中，RGD/整合素识别系统是否参与红细胞-巨噬细胞粘附尚不清楚。在这里，我们报道锚蛋白的RGD基序，而不是其他，被αvβ3整合素受体识别。此外，锚蛋白（一种外周膜蛋白）的RGD基序可以在红细胞与钙孵育并在生理水平上剪切时外化到细胞表面。此外，锚蛋白和/或αvβ3可特异性抑制红细胞-巨噬细胞的粘附。因此，锚蛋白外化后RGD/整合素识别可能是红细胞在吞噬前粘附巨噬细胞的新机制。
The RGD motif on the extracellular matrix or cell surface, together with its integrin receptors, constitutes a major recognition system for cell adhesion. There are several erythrocyte major membrane skeletal proteins, e.g., α spectrin, ankyrin, and protein 4.2, that bear an RGD motif. However, it is not known whether the RGD/integrin recognition system is utilized in the erythrocyte-macrophage adhesion during erythrophagocytosis. Here we report that the RGD motif of ankyrin, but not others, is recognized by the αvβ3integrin receptor. In addition, the RGD motif of ankyrin, a peripheral membrane protein, can be externalized onto the cell surface when erythrocytes are incubated with calcium and sheared both at physiological levels. Furthermore, the erythrocyte-macrophage adhesion can be specifically inhibited by ankyrin and/or αvβ3. Thus, externalization of ankyrin followed by RGD/integrin recognition may be a novel mechanism by which erythrocytes adhere to macrophages preceding phagocytosis.