scholarly journals Low-Density Lipoprotein From Apolipoprotein E-Deficient Mice Induces Macrophage Lipid Accumulation in a CD36 and Scavenger Receptor Class A-Dependent Manner

2005 ◽  
Vol 25 (1) ◽  
pp. 168-173 ◽  
Author(s):  
Zhenze Zhao ◽  
Maria C. de Beer ◽  
Lei Cai ◽  
Reto Asmis ◽  
Frederick C. de Beer ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Lipid Accumulation ◽  
Low Density Lipoprotein ◽  
Scavenger Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Dependent Manner ◽  
Class A ◽  
Scavenger Receptor Class ◽  
Deficient Mice

scholarly journals LOX-1 scavenger receptor mediates calcium-dependent recognition of phosphatidylserine and apoptotic cells

2005 ◽  
Vol 393 (1) ◽  
pp. 107-115 ◽  
Author(s):  
Jane E. Murphy ◽  
Daryl Tacon ◽  
Philip R. Tedbury ◽  
Jonathan M. Hadden ◽  
Stuart Knowling ◽  
...  
Keyword(s):  
Cultured Cells ◽  
Low Density Lipoprotein ◽  
Scavenger Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Dependent Manner ◽  
Oxidized Low Density Lipoprotein ◽  
Bivalent Cation ◽  
Calcium Dependent

The LOX-1 (lectin-like oxidized low-density lipoprotein receptor-1) scavenger receptor regulates vascular responses to oxidized-low-density-lipoprotein particles implicated in atherosclerotic plaque formation. LOX-1 is closely related to C-type lectins, but the mechanism of ligand recognition is not known. Here we show that human LOX-1 recognizes a key cellular phospholipid, PS (phosphatidylserine), in a Ca2+-dependent manner, both in vitro and in cultured cells. A recombinant, folded and glycosylated LOX-1 molecule binds PS, but not other phospholipids. LOX-1 recognition of PS was maximal in the presence of millimolar Ca2+ levels. Mg2+ was unable to substitute for Ca2+ in LOX-1 binding to PS, indicating a Ca2+-specific requirement for bivalent cations. LOX-1-mediated recognition of PS-containing apoptotic bodies was dependent on Ca2+ and was decreased to background levels by bivalent-cation chelation, LOX-1-blocking antibodies or PS-containing liposomes. The LOX-1 membrane protein is thus a Ca2+-dependent phospholipid receptor, revealing novel recognition of phospholipids by mammalian lectins.

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