Localization of the binding sites of native and acetylated low-density lipoprotein (LDL) in human monocyte-derived macrophages.
Human monocyte-derived macrophages were demonstrated to have separate and morphologically distinct binding sites for low density lipoprotein (LDL) and acetylated LDL (AcLDL). Using an indirect immunoperoxidase technique and electron microscopy, only LDL was shown to bind to its receptor in coated pits on the macrophage membrane, whereas the distribution of AcLDL-receptor complexes was dependent upon whether or not the cells were fixed prior to incubation with AcLDL. In cells incubated with AcLDL, then fixed, electron-dense precipitate was found in aggregates, sometimes near pseudopodia; fixed cells incubated with AcLDL had electron-dense precipitate more uniformly spread along the membrane. These data suggest that the 'scavenger' receptor is diffusely distributed in the membrane and that following AcLDL binding the receptors cluster in regions of the membrane which do not contain coated pits.
D000107:Acetylation; D002478:Cells, Cultured; D006801:Humans; D007700:Kinetics; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008264:Macrophages / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009000:Monocytes / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011973:Receptors, LDL; D013329:Structure-Activity Relationship; D013696:Temperature
D008077:Lipoproteins, LDL; D011956:Receptors, Cell Surface; D011973:Receptors, LDL