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Volume 272, Number 49, Issue of December 5, 1997 pp. 31113-31117
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Immune Clearance of Phosphatidylserine-expressing Cells by Phagocytes
THE ROLE OF ₂-GLYCOPROTEIN I IN MACROPHAGE RECOGNITION

(Received for publication, April 7, 1997, and in revised form, August 21, 1997)

From the Department of Cell Biology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030

The function of ₂-glycoprotein I (₂GPI), a 50-kDa serum glycoprotein, is not completely understood but has been suggested to be involved in the regulation of thrombosis (Brighton, T. A., Hogg, P. J., Dai, Y.-P., Murray, B. H., Choing, B. H., and Chesterman, C. N. (1996) Br. J. Haematol. 93, 185-194) and the clearance of phosphatidylserine (PS)-expressing cells (Chonn, A., Semple S. C., and Cullis P. R. (1995) J. Biol. Chem. 270, 25845-25849). To further understand the role of this protein, we characterized the ability of ₂GPI to interact with PS vesicles and influence their uptake by macrophages in vitro. ₂GPI bound to and precipitated vesicles containing anionic but not zwitterionic phospholipids in a gel diffusion assay. ₂GPI also inhibited the procoagulant activity of PS liposomes. In vitro phagocytosis studies showed 20-fold greater uptake of PS liposomes over phosphatidylcholine liposomes. This enhanced uptake was maintained even after PS was "shielded" with ₂GPI and further increased upon the addition of ₂GPI antibodies. Similar to liposomes, PS-expressing apoptotic thymocytes and lipid symmetric red blood cell ghosts bound ₂GPI. Macrophage uptake of these cells was also maintained or enhanced in the presence of ₂GPI and further increased upon the addition of ₂GPI antibodies. It is concluded that ₂GPI can play a critical role in hemostasis by influencing both thrombosis and the clearance of PS-expressing cells.

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