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首页> 外文期刊>Molecular and Cellular Biology >Epidermal Growth Factor-Like Domain Repeat of Stabilin-2 Recognizes Phosphatidylserine during Cell Corpse Clearance
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Epidermal Growth Factor-Like Domain Repeat of Stabilin-2 Recognizes Phosphatidylserine during Cell Corpse Clearance

机译：Stabilin-2的表皮生长因子样结构域重复识别细胞尸体清除过程中的磷脂酰丝氨酸。

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Exposure of phosphatidylserine (PS) on the cell surface occurs early during apoptosis and serves as a recognition signal for phagocytes. Clearance of apoptotic cells by a membrane PS receptor is one of the critical anti-inflammatory functions of macrophages. However, the PS binding receptors and their recognition mechanisms have not been fully investigated. Recently, we reported that stabilin-2 is a PS receptor that mediates the clearance of apoptotic cells, thus releasing the anti-inflammatory cytokine, transforming growth factor β. In this study, we showed that epidermal growth factor (EGF)-like domain repeats (EGFrp) in stabilin-2 can directly and specifically recognize PS. The EGFrps also competitively impaired apoptotic cell uptake by macrophages in in vivo models. We also showed that calcium ions are required for stabilin-2 to mediate phagocytosis via EGFrp. Interestingly, at least four tandem repeats of EGF-like domains were required to recognize PS, and the second atypical EGF-like domain in EGFrp was critical for calcium-dependent PS recognition. Considering that PS itself is an important target molecule for both apoptotic cells and nonapoptotic cells during various cellular processes, our results should help elucidate the molecular mechanism by which apoptotic cell clearance in the human body occurs and also have implications for targeting PS externalization of nonapoptotic cells.
机译：磷脂酰丝氨酸（PS）在细胞表面的暴露发生在细胞凋亡的早期，并作为吞噬细胞的识别信号。膜PS受体清除凋亡细胞是巨噬细胞的关键抗炎功能之一。但是，PS结合受体及其识别机制尚未得到充分研究。最近，我们报道了stabilin-2是一种PS受体，可介导凋亡细胞的清除，从而释放出抗炎细胞因子，从而转化生长因子β。在这项研究中，我们表明，stabilin-2中的表皮生长因子（EGF）样结构域重复序列（EGFrp）可以直接和特异性识别PS。在体内模型中，EGFrps还竞争性损害巨噬细胞对凋亡细胞的吸收。我们还表明，钙稳定蛋白2通过EGFrp介导吞噬作用需要钙离子。有趣的是，至少需要四个串联的EGF样结构域重复序列才能识别PS，而EGFrp中的第二个非典型EGF样结构域对于钙依赖性PS识别至关重要。考虑到PS本身是各种细胞过程中凋亡细胞和非凋亡细胞的重要靶分子，我们的研究结果应有助于阐明人体内凋亡细胞清除的分子机制，并且对靶向非凋亡细胞的PS外化有影响。

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