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dc.contributor.author
Kamerbeek, Constanza Belén
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Borroni, Maria Virginia
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Pediconi, Maria Filomena
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Barrantes, Francisco Jose
dc.date.available
2024-01-17T14:59:44Z
dc.date.issued
2012
dc.identifier.citation
Cell-surface and internalized nicotinic acetylcholine receptor platforms distribute between liquid-ordered and liquid-disordered cholesterol sensitive domains; 5th Special Conference of the International Society for Neurochemistry, Synapses and Dendritic Spines in Health and Disease; Buenos Aires; Argentina; 2012; 17-17
dc.identifier.issn
1471-4159
dc.identifier.uri
http://hdl.handle.net/11336/224004
dc.description.abstract
The correlation between the physical state of the membrane andnicotinic acetylcholine receptor (AChR) clusters was studied inCHO-K1/A5 cells using fluorescence microscopy. For this purposedi-4-ANEPPDHQ, a fluorescent probe that differentiates liquid-ordered (Lo) from liquid-disordered (Ld) phases in model mem-branes (Jin et al., 2005), was used in combination with AChRlabeling of live cells with anti-AChR antibodies. The latter results inthe formation of AChR spots visible with conventional wide-fieldmicroscopy, consisting of nanometer-sized clusters which can beresolved by superresolution microscopy (Kellner et al., 2007). Theso-called generalized polarization (‘‘GP’’) of di-4-ANEPPDHQ wasmeasured in regions of the cell-surface membrane associated with ordevoid of AChR spots, respectively. Under control conditionsAChR spots were almost equally distributed between Lo and Lddomains. This distribution was independent of AChR surface levelsand antagonist binding. Cholesterol depletion mediated by methyl-b-cyclodextrin treatment produced a diminution in the mean GP ofdi-4-ANEPPDHQ in the plasmalemma and a concomitant increasein the number of AChR spots associated with Ld membranedomains. Disruption of the actin cytoskeleton with Latrunculin Ahad the opposite effect. The fate of AChR-lipid domain associationwas further followed upon internalization of the fluorescent spots.Upon endocytosis, the AChR was found in large, aggregatedvesicles and in small, individual vesicles. AChR-containing largevesicles had a higher GP value and a higher cholesterol content, asevidenced by the fluorescence of the probe fPEG-cholesterol. Uponcholesterol depletion, AChR internalization occurred via smallvesicles, and no colocalization with fPEG-cholesterol was observed.The association of AChR aggregates with lipid domains of differentcholesterol content may thus bear on the organization of the AChRat the cell surface and on the ensuing receptor endocytic routes(Borroni et al., 2007; Kumari et al., 2008; Borroni and Barrantes,2011)
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ACETYLCHOLINE RECEPTOR
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LIPID DOMAINS
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CHOLESTEROL
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DIANNEPP
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Cell-surface and internalized nicotinic acetylcholine receptor platforms distribute between liquid-ordered and liquid-disordered cholesterol sensitive domains
dc.type
info:eu-repo/semantics/publishedVersion
dc.type
info:eu-repo/semantics/conferenceObject
dc.type
info:ar-repo/semantics/documento de conferencia
dc.date.updated
2024-01-16T14:31:26Z
dc.identifier.eissn
0022-3042
dc.journal.volume
122
dc.journal.pagination
17-17
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
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
dc.description.fil
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
dc.description.fil
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
dc.description.fil
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/loi/14714159/year/2012
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info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/epdf/10.1111/j.1471-4159.2012.07849.x
dc.conicet.rol
Autor
dc.conicet.rol
Autor
dc.conicet.rol
Autor
dc.conicet.rol
Autor
dc.coverage
Internacional
dc.type.subtype
Conferencia
dc.description.nombreEvento
5th Special Conference of the International Society for Neurochemistry, Synapses and Dendritic Spines in Health and Disease
dc.date.evento
2012-09-12
dc.description.ciudadEvento
Buenos Aires
dc.description.paisEvento
Argentina
dc.type.publicacion
Journal
dc.description.institucionOrganizadora
International Society for Neurochemistry
dc.source.revista
Journal of Neurochemestry
dc.date.eventoHasta
2012-09-15
dc.type
Conferencia
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