Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells

被引：334

作者：

Anderson, HA

Maylock, CA

Williams, JA

Paweletz, CP

Shu, HJ

Shacter, E ^{[1
]}

机构：

[1] US FDA, Biochem Lab, Ctr Biol Evaluat & Res, Div Therapeut Prot, Bethesda, MD 20892 USA

[2] Uniformed Serv Univ Hlth Sci, Dept Pediat, Bethesda, MD 20815 USA

[3] NCI, Expt Immunol Branch, NIH, Bethesda, MD 20892 USA

[4] NCI, Pathol Lab, NIH, Bethesda, MD 20892 USA

[5] Univ Texas, Dept Pharmacol, SW Med Ctr, Dallas, TX 75390 USA

来源：

NATURE IMMUNOLOGY | 2003年 / 4卷 / 01期

关键词：

D O I：

10.1038/ni871

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

引用

页码：87 / 91

页数：5

共 42 条

[21] Oxidative stress inhibits apoptosis in human lymphoma cells [J].