Low-density lipoproteins interact with liposome-binding sites on the cell surface.
Under physiological conditions significant amounts of low-density lipoprotein LDL particles ar taken up by cells independently of specific high-affinity LDL receptors (apo-B receptors). Previously it was established that some cells contain surface sites capable of binding liposomes. We proposed that liposome-binding sites could contribute to LDL interaction with the cell surface via phospholipid molecules of LDL particles. To check this hypothesis we studied the competitive interaction of human LDL and DPPC liposomes with mouse embryo fibroblasts depleted of apo-B receptors by preliminary incubation with LDL. We have found that after removal of the liposome-binding sites from cell lamellae these areas of the cell surface lose their ability to bind LDL.
Galkina
S I
SI
Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Ivanov
V V
VV
Preobrazhensky
S N
SN
Margolis
L B
LB
Bergelson
L D
LD
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D004622:Embryo, Mammalian; D005347:Fibroblasts / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006801:Humans; D007150:Immunohistochemistry; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism*; D051379:Mice; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning
D008077:Lipoproteins, LDL; D008081:Liposomes; D015060:1,2-Dipalmitoylphosphatidylcholine