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

Autores
Perillo, Vanesa L.; Peñalva, Daniel A.; Vitale, Alejandro J.; Barrantes, Francisco José; Antollini, Silvia S.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Perillo, Vanesa L. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Perillo, Vanesa L. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peñalva, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peñalva, Daniel A. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Vitale, Alejandro J. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Vitale, Alejandro J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Antollini, Silvia S. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia S. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: 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.
Fuente
Archives of Biochemistry and Biophysics. 2016, 591
Materia
PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/15256
Acceder
id RIUCA_2f68bceb03e45f63711c06017f0adad1
oai_identifier_str oai:ucacris:123456789/15256
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domainsPerillo, Vanesa L.Peñalva, Daniel A.Vitale, Alejandro J.Barrantes, Francisco JoséAntollini, Silvia S.PROTEINASFLUORESCENCIALIPIDOSRECEPTORES NICOTINICOSFil: Perillo, Vanesa L. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Perillo, Vanesa L. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Peñalva, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Peñalva, Daniel A. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Vitale, Alejandro J. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; ArgentinaFil: Vitale, Alejandro J. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; ArgentinaFil: Antollini, Silvia S. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Antollini, Silvia S. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAbstract: 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.Elsevier2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/152560003-986110.1016/j.abb.2015.12.00326702544Perillo, 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/123456789/15256Archives of Biochemistry and Biophysics. 2016, 591reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:58:53Zoai:ucacris:123456789/15256instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:58:54.139Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
spellingShingle Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
Perillo, Vanesa L.
PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
title_short Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_full Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_fullStr Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_full_unstemmed Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_sort Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
dc.creator.none.fl_str_mv Perillo, Vanesa L.
Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
author Perillo, Vanesa L.
author_facet Perillo, Vanesa L.
Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
author_role author
author2 Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
author2_role author
author
author
author
dc.subject.none.fl_str_mv PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
topic PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
dc.description.none.fl_txt_mv Fil: Perillo, Vanesa L. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Perillo, Vanesa L. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peñalva, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peñalva, Daniel A. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Vitale, Alejandro J. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Vitale, Alejandro J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Antollini, Silvia S. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia S. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: 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.
description Fil: Perillo, Vanesa L. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://repositorio.uca.edu.ar/handle/123456789/15256
0003-9861
10.1016/j.abb.2015.12.003
26702544
Perillo, 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
url https://repositorio.uca.edu.ar/handle/123456789/15256
identifier_str_mv 0003-9861
10.1016/j.abb.2015.12.003
26702544
Perillo, 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.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Archives of Biochemistry and Biophysics. 2016, 591
reponame:Repositorio Institucional (UCA)
instname:Pontificia Universidad Católica Argentina
reponame_str Repositorio Institucional (UCA)
collection Repositorio Institucional (UCA)
instname_str Pontificia Universidad Católica Argentina
repository.name.fl_str_mv Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina
repository.mail.fl_str_mv claudia_fernandez@uca.edu.ar
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score 13.22299

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