Formation of ceramide-enriched domains in lipid particles enhances the binding of apolipoprotein E

Shin Ya Morita; Minoru Nakano; Atsushi Sakurai; Yuko Deharu; Aline Vertut-Doï; Tetsurou Handa

doi:10.1016/j.febslet.2005.02.018

Formation of ceramide-enriched domains in lipid particles enhances the binding of apolipoprotein E

Shin Ya Morita, Minoru Nakano, Atsushi Sakurai, Yuko Deharu, Aline Vertut-Doï, Tetsurou Handa^*

^*Corresponding author for this work

Biointerface Chemistry

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

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.

Original language	English
Pages (from-to)	1759-1764
Number of pages	6
Journal	FEBS Letters
Volume	579
Issue number	7
DOIs	https://doi.org/10.1016/j.febslet.2005.02.018
State	Published - 2005/03/14

Keywords

Apolipoprotein E
Ceramide
Confocal fluorescence microscopy
Microdomain
Sphingomyelinase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2005.02.018

Cite this

@article{ca0e07140e3c41d4a9ac17422263c06e,

title = "Formation of ceramide-enriched domains in lipid particles enhances the binding of apolipoprotein E",

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 = "Apolipoprotein E, Ceramide, Confocal fluorescence microscopy, Microdomain, Sphingomyelinase",

author = "Morita, {Shin Ya} and Minoru Nakano and Atsushi Sakurai and Yuko Deharu and Aline Vertut-Do{\"i} and Tetsurou Handa",

note = "Funding Information: This work was supported in part by a grant from the Pharmaceuticals and Medical Devices Agency, a grant from Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists, and 21st Century COE Program “Knowledge Information Infrastructure for Genome Science”.",

year = "2005",

month = mar,

day = "14",

doi = "10.1016/j.febslet.2005.02.018",

language = "英語",

volume = "579",

pages = "1759--1764",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "7",

}

TY - JOUR

T1 - Formation of ceramide-enriched domains in lipid particles enhances the binding of apolipoprotein E

AU - Morita, Shin Ya

AU - Nakano, Minoru

AU - Sakurai, Atsushi

AU - Deharu, Yuko

AU - Vertut-Doï, Aline

AU - Handa, Tetsurou

N1 - Funding Information: This work was supported in part by a grant from the Pharmaceuticals and Medical Devices Agency, a grant from Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists, and 21st Century COE Program “Knowledge Information Infrastructure for Genome Science”.

PY - 2005/3/14

Y1 - 2005/3/14

N2 - 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.

AB - 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.

KW - Apolipoprotein E

KW - Ceramide

KW - Confocal fluorescence microscopy

KW - Microdomain

KW - Sphingomyelinase

UR - http://www.scopus.com/inward/record.url?scp=14844318000&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2005.02.018

DO - 10.1016/j.febslet.2005.02.018

M3 - 学術論文

C2 - 15757672

AN - SCOPUS:14844318000

SN - 0014-5793

VL - 579

SP - 1759

EP - 1764

JO - FEBS Letters

JF - FEBS Letters

IS - 7

ER -

Formation of ceramide-enriched domains in lipid particles enhances the binding of apolipoprotein E

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Fingerprint

Cite this