TY - JOUR
T1 - β-2-glycoprotein 1-dependent macrophage uptake of apoptotic cells
T2 - Binding to lipoprotein receptor-related protein receptor family members
AU - Maiti, Sourindra N.
AU - Balasubramanian, Krishnakumar
AU - Ramoth, Johanna A.
AU - Schroit, Alan J.
PY - 2008/2/15
Y1 - 2008/2/15
N2 - The recognition and removal of apoptotic cells is critical to development, tissue homeostasis, and the resolution of inflammation. Many studies have shown that phagocytosis is regulated by signaling mechanisms that involve distinct ligand-receptor interactions that drive the engulfment of apoptotic cells. Studies from our laboratory have shown that the plasma protein β-2-glycoprotein 1 (β2GP1), a member of the short consensus repeat superfamily, binds phosphatidylserine-containing vesicles and apoptotic cells and promotes their bridging and subsequent engulfment by phagocytes. The phagocyte receptor for the protein/apoptotic cell complex, however, is unknown. Here we report that a member of the low density lipoprotein receptor-related protein family on phagocytes binds and facilitates engulfment of β2GP1-phosphatidylserine and β2GP1-apoptotic cell complexes. Using recombinant β2GP1, we also show that β2GP1-dependent uptake is mediated by bridging of the target cell to the phagocyte through the protein C- and N-terminal domains, respectively.
AB - The recognition and removal of apoptotic cells is critical to development, tissue homeostasis, and the resolution of inflammation. Many studies have shown that phagocytosis is regulated by signaling mechanisms that involve distinct ligand-receptor interactions that drive the engulfment of apoptotic cells. Studies from our laboratory have shown that the plasma protein β-2-glycoprotein 1 (β2GP1), a member of the short consensus repeat superfamily, binds phosphatidylserine-containing vesicles and apoptotic cells and promotes their bridging and subsequent engulfment by phagocytes. The phagocyte receptor for the protein/apoptotic cell complex, however, is unknown. Here we report that a member of the low density lipoprotein receptor-related protein family on phagocytes binds and facilitates engulfment of β2GP1-phosphatidylserine and β2GP1-apoptotic cell complexes. Using recombinant β2GP1, we also show that β2GP1-dependent uptake is mediated by bridging of the target cell to the phagocyte through the protein C- and N-terminal domains, respectively.
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U2 - 10.1074/jbc.M704990200
DO - 10.1074/jbc.M704990200
M3 - Article
C2 - 18073216
AN - SCOPUS:42949144324
SN - 0021-9258
VL - 283
SP - 3761
EP - 3766
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -