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Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/122890
Caveolin-1-mediated apolipoprotein A-I membrane binding sites are not required for cholesterol efflux
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Caveolin-1 (Cav1), a structural protein required for the formation of invaginated membrane domains known as caveolae, has been implicated in cholesterol trafficking and homeostasis. Here we investigated the contribution of Cav1 to apolipoprotein A-I (apoA-I) cell surface binding and intracellular processing using mouse embryonic fibroblasts (MEFs) derived from wild type (WT) or Cav1-deficient (Cav1−/−) animals. We found that cells expressing Cav1 have 2.6-fold more apoA-I binding sites than Cav1−/− cells although these additional binding sites are not associated with detergent-free lipid rafts. Further, Cav1-mediated binding targets apoA-I for internalization and degradation and these processes are not correlated to cholesterol efflux. Despite lower apoA-I binding, cholesterol efflux from Cav1−/− MEFs is 1.7-fold higher than from WT MEFs. Stimulation of ABCA1 expression with an LXR agonist enhances cholesterol efflux from both WT and Cav1−/− cells without increasing apoA-I surface binding or affecting apoA-I processing. Our results indicate that there are at least two independent lipid binding sites for apoA-I; Cav1-mediated apoA-I surface binding and uptake is not linked to cholesterol efflux, indicating that membrane domains other than caveolae regulate ABCA1-mediated cholesterol efflux.
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LE LAY, Soazig, RODRIGUEZ, Macarena, JESSUP, Wendy, RENTERO ALFONSO, Carles, LI, Qiong, CARTLAND, Siân, GREWAL, Thomas, GAUS, Katharina. Caveolin-1-mediated apolipoprotein A-I membrane binding sites are not required for cholesterol efflux. _PLoS One_. 2011. Vol. 6, núm. 8, pàgs. e23353. [consulta: 21 de gener de 2026]. ISSN: 1932-6203. [Disponible a: https://hdl.handle.net/2445/122890]