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The Central Role of Phosphatidylserine in the Phagocytosis of Apoptotic Thymocytes
Author(s) -
SCHLEGEL ROBERT A.,
CALLAHAN MELISSA K.,
WILLIAMSON PATRICK
Publication year - 2000
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2000.tb05614.x
Subject(s) - phosphatidylserine , phospholipid scramblase , phagocytosis , microbiology and biotechnology , translocase , receptor , apoptosis , chemistry , cell surface receptor , cell , cell membrane , biology , biochemistry , membrane , phospholipid , chromosomal translocation , gene
A bstract : Apoptotic thymocytes inactivate the aminophospholipid translocase, which transports phosphatidylserine (PS) to the inner leaflet of the plasma membrane, and activate the scramblase, which randomizes phospholipids across the membrane and brings PS to the cell surface. Although different macrophages use at least two different systems to recognize and engulf apoptotic thymocytes, both systems recognize PS on the apoptotic target. Thymocytes treated with Ca 2+ and ionophore to inactivate the translocase and activate the scramblase immediately expose PS on their surface and are immediately recognized and phagocytosed. These targets, on which PS has been artificially exposed, are recognized by the PS exposed on their surface. However, they apparently also engage the vitronectic receptor, a lectin‐like receptor and CD14. All of these receptors are implicated in the phagocytosis of apoptotic thymocytes, suggesting that loss of asymmetry and/or exposure of PS is sufficient to generate the ligands recognized by those receptors. The role of PS is not confined to the target cell surface, however. PS is constitutively exposed on the surface of macrophages and is as necessary for apoptotic cell engulfment as is recognition of PS on the target cell surface.