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Formation of ceramide‐enriched domains in lipid particles enhances the binding of apolipoprotein E
Author(s) -
Morita Shin-ya,
Nakano Minoru,
Sakurai Atsushi,
Deharu Yuko,
Vertut-Doï Aline,
Handa Tetsurou
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.02.018
Subject(s) - sphingomyelin , ceramide , apolipoprotein e , chemistry , apolipoprotein b , biophysics , sphingomyelin phosphodiesterase , emulsion , particle (ecology) , confocal microscopy , fusion , biochemistry , microbiology and biotechnology , membrane , cholesterol , biology , medicine , apoptosis , ecology , linguistics , philosophy , disease , pathology
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.