Formation of ceramide‐enriched domains in lipid particles enhances the binding of apolipoprotein E
Open Access
- 19 February 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (7) , 1759-1764
- https://doi.org/10.1016/j.febslet.2005.02.018
Abstract
We investigated the interaction between apolipoprotein E (apoE) and ceramide (CER)‐enriched domains on the particles, by using lipid emulsions containing sphingomyelin (SM) or CER as model particles of lipoproteins. The sphingomyelinase (SMase)‐induced aggregation of emulsion particles was prevented by apoE. CER increased the amount of apoE bound to emulsion particles. The confocal images of CER‐containing large emulsions with two fluorescent probes showed three‐dimensional microdomains enriched in CER. SMase also induced the formation of CER‐enriched domains. We propose apoE prefers to bind on CER‐enriched domains exposed on particle surface, and thus inhibits the aggregation or fusion of the particles.Keywords
This publication has 38 references indexed in Scilit:
- Effects of sphingomyelin on apolipoprotein E- and lipoprotein lipase-mediated cell uptake of lipid particlesBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2003
- Evidence for a physiological role for membrane rafts in human plateletsJournal of Cellular Physiology, 2001
- Sphingomyelinase Activity Associated with Human Plasma Low Density LipoproteinJournal of Biological Chemistry, 2000
- Modification of Type III VLDL, Their Remnants, and VLDL From ApoE-Knockout Mice by p -Hydroxyphenylacetaldehyde, a Product of Myeloperoxidase Activity, Causes Marked Cholesteryl Ester Accumulation in MacrophagesArteriosclerosis, Thrombosis, and Vascular Biology, 1999
- Sphingomyelinase Induces Lipid Microdomain Formation in a Fluid Phosphatidylcholine/Sphingomyelin MembraneBiochemistry, 1998
- Secretory Sphingomyelinase, a Product of the Acid Sphingomyelinase Gene, Can Hydrolyze Atherogenic Lipoproteins at Neutral pHJournal of Biological Chemistry, 1998
- Uptake by J774 Macrophages of Very-Low-Density Lipoproteins Isolated From ApoE-Deficient Mice Is Mediated by a Distinct Receptor and Stimulated by Lipoprotein LipaseArteriosclerosis, Thrombosis, and Vascular Biology, 1997
- Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low-density lipoprotein. Proposed role for arterial-wall sphingomyelinase in subendothelial retention and aggregation of atherogenic lipoproteins.Journal of Clinical Investigation, 1996
- Ceramide Induces Structural Defects into Phosphatidylcholine Bilayers and Activates Phospholipase A2Biochemical and Biophysical Research Communications, 1996
- Macrophage-specific expression of human apolipoprotein E reduces atherosclerosis in hypercholesterolemic apolipoprotein E-null mice.Journal of Clinical Investigation, 1995