Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma

Autores
Kamerbeek, Constanza Belén; Borroni, Maria Virginia; Pediconi, Maria Filomena; Barrantes, Francisco Jose
Año de publicación
2011
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
In the present work we have attempted to establish whether there is a correlation between antibody-induced nicotinic acetylcholine receptor (AChR)-rich clusters and the physical state of the underlying cell membrane in living cells. For this purpose di-4- ANEPPDHQ, a fluorescent probe that differentiates liquid-ordered from liquid-disordered phases in model membranes was used in combination with labeling of the AChR in CHO-K1/A5, a clonal cell line expressing adult muscle-type AChR. The so-called generalized polarization (“GP”) of di-4-ANEPPDHQ was measured in regions of the cell-surface membrane associated with the AChR platforms clearly identified using conventional widefield fluorescence microscopy. Under control conditions AChR clusters are roughly equally distributed among liquid-ordered and liquid-disordered domains. This distribution changes upon cyclodextrin-mediated cholesterol depletion or by Latrunculin disruption of the actin cytoskeleton. Association of AChR clusters with lipid domains with different biophysical properties may have consequences on AChR trafficking processe.
Fil: Kamerbeek, Constanza Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Pediconi, Maria Filomena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Potrero de los Funes San Luis
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Materia
ACETYLCHOLINE NICOTINIC RECEPTOR
LIPID DOMAINS
DI-4-ANEPPDHQ
CHOLESTEROL
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/244884

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network_name_str CONICET Digital (CONICET)
spelling Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The PlasmalemmaKamerbeek, Constanza BelénBorroni, Maria VirginiaPediconi, Maria FilomenaBarrantes, Francisco JoseACETYLCHOLINE NICOTINIC RECEPTORLIPID DOMAINSDI-4-ANEPPDHQCHOLESTEROLhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In the present work we have attempted to establish whether there is a correlation between antibody-induced nicotinic acetylcholine receptor (AChR)-rich clusters and the physical state of the underlying cell membrane in living cells. For this purpose di-4- ANEPPDHQ, a fluorescent probe that differentiates liquid-ordered from liquid-disordered phases in model membranes was used in combination with labeling of the AChR in CHO-K1/A5, a clonal cell line expressing adult muscle-type AChR. The so-called generalized polarization (“GP”) of di-4-ANEPPDHQ was measured in regions of the cell-surface membrane associated with the AChR platforms clearly identified using conventional widefield fluorescence microscopy. Under control conditions AChR clusters are roughly equally distributed among liquid-ordered and liquid-disordered domains. This distribution changes upon cyclodextrin-mediated cholesterol depletion or by Latrunculin disruption of the actin cytoskeleton. Association of AChR clusters with lipid domains with different biophysical properties may have consequences on AChR trafficking processe.Fil: Kamerbeek, Constanza Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Pediconi, Maria Filomena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología MolecularPotrero de los Funes San LuisArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularInstituto de Histología y Embriología “Dr. Mario H. Burgos”2011info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/244884Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma; 47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes San Luis; Argentina; 2011; 71-710327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v47nSuppl.1/50703/pdfinfo:eu-repo/semantics/altIdentifier/url/https://newsite.saib.org.ar/publicaciones/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:58:32Zoai:ri.conicet.gov.ar:11336/244884instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:58:32.774CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
title Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
spellingShingle Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
Kamerbeek, Constanza Belén
ACETYLCHOLINE NICOTINIC RECEPTOR
LIPID DOMAINS
DI-4-ANEPPDHQ
CHOLESTEROL
title_short Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
title_full Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
title_fullStr Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
title_full_unstemmed Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
title_sort Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma
dc.creator.none.fl_str_mv Kamerbeek, Constanza Belén
Borroni, Maria Virginia
Pediconi, Maria Filomena
Barrantes, Francisco Jose
author Kamerbeek, Constanza Belén
author_facet Kamerbeek, Constanza Belén
Borroni, Maria Virginia
Pediconi, Maria Filomena
Barrantes, Francisco Jose
author_role author
author2 Borroni, Maria Virginia
Pediconi, Maria Filomena
Barrantes, Francisco Jose
author2_role author
author
author
dc.subject.none.fl_str_mv ACETYLCHOLINE NICOTINIC RECEPTOR
LIPID DOMAINS
DI-4-ANEPPDHQ
CHOLESTEROL
topic ACETYLCHOLINE NICOTINIC RECEPTOR
LIPID DOMAINS
DI-4-ANEPPDHQ
CHOLESTEROL
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In the present work we have attempted to establish whether there is a correlation between antibody-induced nicotinic acetylcholine receptor (AChR)-rich clusters and the physical state of the underlying cell membrane in living cells. For this purpose di-4- ANEPPDHQ, a fluorescent probe that differentiates liquid-ordered from liquid-disordered phases in model membranes was used in combination with labeling of the AChR in CHO-K1/A5, a clonal cell line expressing adult muscle-type AChR. The so-called generalized polarization (“GP”) of di-4-ANEPPDHQ was measured in regions of the cell-surface membrane associated with the AChR platforms clearly identified using conventional widefield fluorescence microscopy. Under control conditions AChR clusters are roughly equally distributed among liquid-ordered and liquid-disordered domains. This distribution changes upon cyclodextrin-mediated cholesterol depletion or by Latrunculin disruption of the actin cytoskeleton. Association of AChR clusters with lipid domains with different biophysical properties may have consequences on AChR trafficking processe.
Fil: Kamerbeek, Constanza Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Pediconi, Maria Filomena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Potrero de los Funes San Luis
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
description In the present work we have attempted to establish whether there is a correlation between antibody-induced nicotinic acetylcholine receptor (AChR)-rich clusters and the physical state of the underlying cell membrane in living cells. For this purpose di-4- ANEPPDHQ, a fluorescent probe that differentiates liquid-ordered from liquid-disordered phases in model membranes was used in combination with labeling of the AChR in CHO-K1/A5, a clonal cell line expressing adult muscle-type AChR. The so-called generalized polarization (“GP”) of di-4-ANEPPDHQ was measured in regions of the cell-surface membrane associated with the AChR platforms clearly identified using conventional widefield fluorescence microscopy. Under control conditions AChR clusters are roughly equally distributed among liquid-ordered and liquid-disordered domains. This distribution changes upon cyclodextrin-mediated cholesterol depletion or by Latrunculin disruption of the actin cytoskeleton. Association of AChR clusters with lipid domains with different biophysical properties may have consequences on AChR trafficking processe.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/244884
Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma; 47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes San Luis; Argentina; 2011; 71-71
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/244884
identifier_str_mv Nicotinic Acetylcholine Receptor Clusters Localization On Lipid Domains Of The Plasmalemma; 47th Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology Research; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes San Luis; Argentina; 2011; 71-71
0327-9545
1667-5746
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v47nSuppl.1/50703/pdf
info:eu-repo/semantics/altIdentifier/url/https://newsite.saib.org.ar/publicaciones/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Instituto de Histología y Embriología “Dr. Mario H. Burgos”
publisher.none.fl_str_mv Instituto de Histología y Embriología “Dr. Mario H. Burgos”
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
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repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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