Caveolin-1-dependent and -independent membrane domains.

TitreCaveolin-1-dependent and -independent membrane domains.
Type de publicationArticle de revue
AuteurLe Lay, Soazig , Li, Qiong, Proschogo, Nicholas, Rodriguez, Macarena, Gunaratnam, Krishanthi, Cartland, Siân, Rentero, Carles, Jessup, Wendy, Mitchell, Todd, Gaus, Katharina
EditeurAmerican Society for Biochemistry and Molecular Biology
TypeArticle scientifique dans une revue à comité de lecture
Année2009
LangueAnglais
Date08/2009
Pagination1609-20
Volume50
Titre de la revueJournal of Lipid Research
ISSN0022-2275
Mots-clésAnimals, Caveolae, Caveolin 1, Caveolin 2, Cell Membrane Structures, Cells, Cultured, Cholesterol, Cholesterol Esters, Cholesterol Oxidase, Fatty Acids, Female, Male, Membrane Microdomains, Mice, Mice, Knockout, Phosphatidylcholines, Phospholipids, Proto-Oncogene Proteins c-yes, Sphingomyelins
Résumé en anglais

Lipid rafts defined as cholesterol- and sphingomyelin-rich domains have been isolated from different cell types that vary greatly in their lipid profiles. Here, we investigated the contribution of the structural protein caveolin-1 (Cav1) to the overall lipid composition and domain abundance in mouse embryonic fibroblasts (MEFs) from wild-type (WT) or Cav1-deficient (Cav1(-/-)) animals. Our findings show that Cav1 expression had no effect on free (membrane-associated) cholesterol levels. However, Cav1(-/-)-deficient cells did have a higher proportion of sphingomyelin, decreased abundance of unsaturated phospholipids, and a trend toward shorter fatty acid chains in phosphatidylcholine. We isolated detergent-resistant membranes (DRMs), nondetergent raft domains (NDR), and cholesterol oxidase (CO)-sensitive domains and assessed the abundance of ordered domains in intact cells using the fluorescent dye Laurdan. Despite differences in phospholipid composition, we found that cholesterol levels in DRMs, NDR, and CO-sensitive domains were similar in both cell types. The data suggest that Cav1 is not required to target cholesterol to lipid rafts and that CO does not specifically oxidize caveolar cholesterol. In contrast, the abundance of ordered domains in adherent cells is reduced in Cav1(-/-) compared with WT MEFs, suggesting that cell architecture is critical in maintaining Cav1-induced lipid rafts.

URL de la noticehttp://okina.univ-angers.fr/publications/ua7117
DOI10.1194/jlr.M800601-JLR200
Lien vers le document

http://dx.doi.org/10.1194/jlr.M800601-JLR200

Autre titreJ. Lipid Res.
Identifiant (ID) PubMed19074371