Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells
Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells
复制标题
DOI：
10.1038/ni871
复制
发表时间：
2003-01-01
影响因子：
30.5
通讯作者：
Shacter, E
中科院分区：
文献类型：
--
作者：
Anderson, HA;Maylock, CA;Shacter, E
凋亡细胞的快速吞噬作用被认为限制了炎症和自身免疫性疾病的发展。血清增强巨噬细胞吞噬凋亡细胞。在这里，我们确定了蛋白S的因素负责血清刺激吞噬凋亡细胞。蛋白S以其抗血栓形成活性而闻名，作为蛋白C的辅因子。纯化的蛋白S在其刺激巨噬细胞吞噬凋亡淋巴瘤细胞的能力方面与血清相当，并且蛋白S的免疫耗竭消除了血清的原噬细胞活性。蛋白S通过与凋亡细胞表面表达的磷脂酰丝氨酸结合而起作用。因此，蛋白S是一种多功能蛋白，除了调节血液凝固外，还可以促进早期凋亡细胞的清除。
Rapid phagocytosis of apoptotic cells is thought to limit the development of inflammation and autoimmune disease. Serum enhances macrophage phagocytosis of apoptotic cells. Here we identified protein S as the factor responsible for serum-stimulated phagocytosis of apoptotic cells. Protein S is best known for its anti-thrombotic activity, serving as a cofactor for protein C. Purified protein S was equivalent to serum in its ability to stimulate macrophage phagocytosis of apoptotic lymphoma cells, and immunodepletion of protein S eliminated the prophagocytic activity of serum. Protein S acted by binding to phosphatidylserine expressed on the apoptotic cell surface. Protein S is thus a multifunctional protein that can facilitate clearance of early apoptotic cells in addition to regulating blood coagulation.