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Published 12 November 2001. doi:10.1083/jcb.200108080
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© The Rockefeller University Press, 0021-9525/2001/11/649 $5.00
The Journal of Cell Biology, Volume 155, Number 4, November 12, 2001 649-660

Article

 Phosphatidylserine (PS) induces PS receptor–mediated macropinocytosis and promotes clearance of apoptotic cells

Peter R. Hoffmann1, Aimee M. deCathelineau1, Carol Anne Ogden1, Yann Leverrier2, Donna L. Bratton1, David L. Daleke3, Anne J. Ridley2, Valerie A. Fadok1 and Peter M. Henson1

1 Program in Cell Biology, Department of Pediatrics, National Jewish Medical and Research Center, Denver, CO 80206
2 Ludwig Institute for Cancer Research, London W1P 8BT, UK
3 Department of Biochemistry and Molecular Biology/Medical Sciences, Indiana University, Bloomington, IN 47405

Address correspondence to Peter Henson, National Jewish Medical and Research Center, D508, 1400 Jackson Street, Denver, CO 80206. Tel.: (303) 398-1380. Fax: (303) 398-1381. E-mail: hensonp{at}njc.org

Efficient phagocytosis of apoptotic cells is important for normal tissue development, homeostasis, and the resolution of inflammation. Although many receptors have been implicated in the clearance of apoptotic cells, the roles of these receptors in the engulfment process have not been well defined. We developed a novel system to distinguish between receptors involved in tethering of apoptotic cells versus those inducing their uptake. Our results suggest that regardless of the receptors engaged on the phagocyte, ingestion does not occur in the absence of phosphatidylserine (PS). Further, recognition of PS was found to be dependent on the presence of the PS receptor (PSR). Both PS and anti-PSR antibodies stimulated membrane ruffling, vesicle formation, and "bystander" uptake of cells bound to the surface of the phagocyte. We propose that the phagocytosis of apoptotic cells requires two events: tethering followed by PS-stimulated, PSR-mediated macropinocytosis.

Key Words: macropinocytosis; phagocytosis; apoptotic cells; phosphatidylserine; phosphatidylserine receptor


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