Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains

We have previously shown that the intact nicotinic acetylcholine receptor (AChR) lacks preference for Lo domains when reconstituted in a sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model system (Bermúdez V, Antollini SS, Fernandez-Nievas GA, Avelda no MI, Barrantes FJ. J. Lipid Res. 2010...

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Detalles Bibliográficos
Autores: Perillo, Vanesa Liliana, Peñalva, Daniel Alejandro, Vitale, Alejandro José, Barrantes, Francisco Jose, Antollini, Silvia Susana
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/25186
Acceso en línea:http://hdl.handle.net/11336/25186
Access Level:acceso abierto
Palabra clave:Nicotinic Acetylcholine Receptors
Transbilayer Asymmetry
Lipid Raft
Fluorescence
Sphingolipids
Liposomes
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Descripción
Sumario:We have previously shown that the intact nicotinic acetylcholine receptor (AChR) lacks preference for Lo domains when reconstituted in a sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model system (Bermúdez V, Antollini SS, Fernandez-Nievas GA, Avelda no MI, Barrantes FJ. J. Lipid Res. 2010; 51: 2629 ~ e2641). Here, we have furthered our studies by characterizing the influence of different lipid host compositions on the distribution of purified AChR reconstituted in two model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1), involving a) different SM species (porcine brain SM (bSM), 16:0-SM, 18:0-SM or 24:1-SM); or b) induced transbilayer asymmetry, resulting from enrichment in bSM in the external hemilayer. AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and by analyzing the distribution of AChR in detergent-resistant and detergent-soluble fractions (1% Triton X-100, 4 C). bSM-induced transbilayer asymmetry or the presence of 16:0-SM and/or 18:0-SM (unlike bSM or 24:1- SM) resulted in the preferential partitioning of AChR in Lo domains, suggesting that the localization of AChR in ordered domains strongly depends on the characteristics of the host lipid membrane, and in particular on the sphingolipid composition and transbilayer asymmetry.