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...
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Published in | FEBS letters Vol. 287; no. 1; pp. 19 - 22 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
05.08.1991
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(91)80006-O |