dc.creatorPerillo, Vanesa L.
dc.creatorPeñalva, Daniel A.
dc.creatorVitale, Alejandro J.
dc.creatorBarrantes, Francisco José
dc.creatorAntollini, Silvia S.
dc.date2022-10-20T12:58:04Z
dc.date2022-10-20T12:58:04Z
dc.date2016
dc.date.accessioned2023-08-30T15:35:36Z
dc.date.available2023-08-30T15:35:36Z
dc.identifierPerillo, V.L., et al. Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains [en línea]. Archives of Biochemistry and Biophysics. 2016, 591 doi:10.1016/j.abb.2015.12.003 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15256
dc.identifier0003-9861
dc.identifierhttps://repositorio.uca.edu.ar/handle/123456789/15256
dc.identifier10.1016/j.abb.2015.12.003
dc.identifier26702544
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8525458
dc.descriptionAbstract: 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, Fernández-Nievas GA, Aveldaño MI, Barrantes FJ. J. Lipid Res. 2010; 51: 2629-2641). 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.sourceArchives of Biochemistry and Biophysics. 2016, 591
dc.subjectPROTEINAS
dc.subjectFLUORESCENCIA
dc.subjectLIPIDOS
dc.subjectRECEPTORES NICOTINICOS
dc.titleTransbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
dc.typeArtículo


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