Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane

Autores
Antollini, Silvia Susana; Barrantes, Francisco Jose
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
To study the effects produced by free fatty acids (FFA) on the biophysical properties of Torpedo marmorata nicotinic acetylcholine receptor-rich native membranes and to investigate the topology of their binding site(s), fluorescence measurements were carried out using the fluorescent probe Laurdan (6-dodecanoyl-2-(dimethyl-amino) naphthalene) and ADIFAB, an Acrylodan-derivatized intestinal fatty acid-binding protein. The generalized polarization (GP) of the former probe was used to learn about the physical state of the membrane upon FFA binding. Saturated FFA induced a slight increase in GP, whereas cis-unsaturated fatty acids decreased GP. Double bond isomerism could also be distinguished; oleic acid (18:1cis) induced a net disordering effect, whereas elaidic acid (18:1trans) produced no changes in GP. The changes in the efficiency of the Förster energy transfer from the protein to Laurdan brought about by addition of FFA, together with the distances involved in this process, indicate that all FFA studied share a common site at the lipid-protein interface. However, despite being located at the same site, each class of FFA differs in its effect on the physical properties of the membrane. These data lead us to suggest that it is the direct action of FFA at the lipid-protein interface, displacing essential lipids from their sites rather than changes in bulk properties such as membrane fluidity that accounts for the effect of FFA on the acetylcholine receptor membrane.
Fil: Antollini, Silvia Susana. 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. Unesco; 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. Unesco; Argentina
Materia
Ácido Graso
AChR
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/53079
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membraneAntollini, Silvia SusanaBarrantes, Francisco JoseÁcido GrasoAChRhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1To study the effects produced by free fatty acids (FFA) on the biophysical properties of Torpedo marmorata nicotinic acetylcholine receptor-rich native membranes and to investigate the topology of their binding site(s), fluorescence measurements were carried out using the fluorescent probe Laurdan (6-dodecanoyl-2-(dimethyl-amino) naphthalene) and ADIFAB, an Acrylodan-derivatized intestinal fatty acid-binding protein. The generalized polarization (GP) of the former probe was used to learn about the physical state of the membrane upon FFA binding. Saturated FFA induced a slight increase in GP, whereas cis-unsaturated fatty acids decreased GP. Double bond isomerism could also be distinguished; oleic acid (18:1cis) induced a net disordering effect, whereas elaidic acid (18:1trans) produced no changes in GP. The changes in the efficiency of the Förster energy transfer from the protein to Laurdan brought about by addition of FFA, together with the distances involved in this process, indicate that all FFA studied share a common site at the lipid-protein interface. However, despite being located at the same site, each class of FFA differs in its effect on the physical properties of the membrane. These data lead us to suggest that it is the direct action of FFA at the lipid-protein interface, displacing essential lipids from their sites rather than changes in bulk properties such as membrane fluidity that accounts for the effect of FFA on the acetylcholine receptor membrane.Fil: Antollini, Silvia Susana. 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. Unesco; 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; Argentina. Unesco; ArgentinaAmerican Society for Biochemistry and Molecular Biology2002-01-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/53079Antollini, Silvia Susana; Barrantes, Francisco Jose; Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 277; 2; 11-1-2002; 1249-12540021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M106618200info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/277/2/1249.fullinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:15:04Zoai:ri.conicet.gov.ar:11336/53079instacron: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:34982025-09-10 13:15:04.772CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
title Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
spellingShingle Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
Antollini, Silvia Susana
Ácido Graso
AChR
title_short Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
title_full Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
title_fullStr Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
title_full_unstemmed Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
title_sort Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
dc.creator.none.fl_str_mv Antollini, Silvia Susana
Barrantes, Francisco Jose
author Antollini, Silvia Susana
author_facet Antollini, Silvia Susana
Barrantes, Francisco Jose
author_role author
author2 Barrantes, Francisco Jose
author2_role author
dc.subject.none.fl_str_mv Ácido Graso
AChR
topic Ácido Graso
AChR
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv To study the effects produced by free fatty acids (FFA) on the biophysical properties of Torpedo marmorata nicotinic acetylcholine receptor-rich native membranes and to investigate the topology of their binding site(s), fluorescence measurements were carried out using the fluorescent probe Laurdan (6-dodecanoyl-2-(dimethyl-amino) naphthalene) and ADIFAB, an Acrylodan-derivatized intestinal fatty acid-binding protein. The generalized polarization (GP) of the former probe was used to learn about the physical state of the membrane upon FFA binding. Saturated FFA induced a slight increase in GP, whereas cis-unsaturated fatty acids decreased GP. Double bond isomerism could also be distinguished; oleic acid (18:1cis) induced a net disordering effect, whereas elaidic acid (18:1trans) produced no changes in GP. The changes in the efficiency of the Förster energy transfer from the protein to Laurdan brought about by addition of FFA, together with the distances involved in this process, indicate that all FFA studied share a common site at the lipid-protein interface. However, despite being located at the same site, each class of FFA differs in its effect on the physical properties of the membrane. These data lead us to suggest that it is the direct action of FFA at the lipid-protein interface, displacing essential lipids from their sites rather than changes in bulk properties such as membrane fluidity that accounts for the effect of FFA on the acetylcholine receptor membrane.
Fil: Antollini, Silvia Susana. 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. Unesco; 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. Unesco; Argentina
description To study the effects produced by free fatty acids (FFA) on the biophysical properties of Torpedo marmorata nicotinic acetylcholine receptor-rich native membranes and to investigate the topology of their binding site(s), fluorescence measurements were carried out using the fluorescent probe Laurdan (6-dodecanoyl-2-(dimethyl-amino) naphthalene) and ADIFAB, an Acrylodan-derivatized intestinal fatty acid-binding protein. The generalized polarization (GP) of the former probe was used to learn about the physical state of the membrane upon FFA binding. Saturated FFA induced a slight increase in GP, whereas cis-unsaturated fatty acids decreased GP. Double bond isomerism could also be distinguished; oleic acid (18:1cis) induced a net disordering effect, whereas elaidic acid (18:1trans) produced no changes in GP. The changes in the efficiency of the Förster energy transfer from the protein to Laurdan brought about by addition of FFA, together with the distances involved in this process, indicate that all FFA studied share a common site at the lipid-protein interface. However, despite being located at the same site, each class of FFA differs in its effect on the physical properties of the membrane. These data lead us to suggest that it is the direct action of FFA at the lipid-protein interface, displacing essential lipids from their sites rather than changes in bulk properties such as membrane fluidity that accounts for the effect of FFA on the acetylcholine receptor membrane.
publishDate 2002
dc.date.none.fl_str_mv 2002-01-11
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 http://hdl.handle.net/11336/53079
Antollini, Silvia Susana; Barrantes, Francisco Jose; Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 277; 2; 11-1-2002; 1249-1254
0021-9258
CONICET Digital
CONICET
url http://hdl.handle.net/11336/53079
identifier_str_mv Antollini, Silvia Susana; Barrantes, Francisco Jose; Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 277; 2; 11-1-2002; 1249-1254
0021-9258
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M106618200
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/277/2/1249.full
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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