Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor

Autores
Perillo, Vanesa Liliana; Barrantes, Francisco Jose; Antollini, Silvia Susana
Año de publicación
2010
Idioma
español castellano
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Free fatty acids (FFA) are non-competitive antagonists of the nicotinic acetylcholine receptor (AChR) and their site of action is supposedly located at the lipid-AChR interface, where lipids can be annular or non-annular. It is known that the cis-unsaturated FFA, and not trans-unsaturated FFA, produce conformational modifications in the AChR resting state. Using T. californica receptor-rich membranes, we studied the changes in AChR conformational state generated by differences in the double-bond position of monounsaturated FFA. Using the higher affinity of the fluorescent AChR blocker crystal violet for the desensitized than for the resting state, it was observed that a double bond in positions ù 6 or ù 9 increased the KD values of the AChR in the desensitized state whereas no effect was observed in ù 11 or ù 13. Only FFAwith an ù 9 double bond changed the KD values in the resting state. DPH and Laurdan fluorescence studies showed that fluidity increased the most in FFAwith ù 9 and ù 11 double bonds and that ù 6 and ù 13 had less effect. Fluorescence resonance energy transfer experiments showed that the FFAwith an ù 6 double bond remained as an annular lipid whereas all the others also interact at non-annular sites. Thus, the location of the unsaturated double bond appears to be of critical importance for FFA-AChR interaction.
Fil: Perillo, Vanesa Liliana. 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
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
XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Puerto Madryn
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Materia
FLUORESCENCE
NICOTINIC ACETYLCHONE RECEPTOR
FREE FATTY ACIDS
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:11336/232473
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/232473
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine ReceptorPerillo, Vanesa LilianaBarrantes, Francisco JoseAntollini, Silvia SusanaFLUORESCENCENICOTINIC ACETYLCHONE RECEPTORFREE FATTY ACIDShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Free fatty acids (FFA) are non-competitive antagonists of the nicotinic acetylcholine receptor (AChR) and their site of action is supposedly located at the lipid-AChR interface, where lipids can be annular or non-annular. It is known that the cis-unsaturated FFA, and not trans-unsaturated FFA, produce conformational modifications in the AChR resting state. Using T. californica receptor-rich membranes, we studied the changes in AChR conformational state generated by differences in the double-bond position of monounsaturated FFA. Using the higher affinity of the fluorescent AChR blocker crystal violet for the desensitized than for the resting state, it was observed that a double bond in positions ù 6 or ù 9 increased the KD values of the AChR in the desensitized state whereas no effect was observed in ù 11 or ù 13. Only FFAwith an ù 9 double bond changed the KD values in the resting state. DPH and Laurdan fluorescence studies showed that fluidity increased the most in FFAwith ù 9 and ù 11 double bonds and that ù 6 and ù 13 had less effect. Fluorescence resonance energy transfer experiments showed that the FFAwith an ù 6 double bond remained as an annular lipid whereas all the others also interact at non-annular sites. Thus, the location of the unsaturated double bond appears to be of critical importance for FFA-AChR interaction.Fil: Perillo, Vanesa Liliana. 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; ArgentinaFil: 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; ArgentinaXLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología MolecularPuerto MadrynArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularBiocell2010info: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/11336/232473Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor; XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Puerto Madryn; Argentina; 2010; 129-1290327-95451667-5746CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/https://saib.org.ar/archivos/biocell-34.pdfinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:11:06Zoai:ri.conicet.gov.ar:11336/232473instacron: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:34982025-10-22 12:11:07.174CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
title Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
spellingShingle Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
Perillo, Vanesa Liliana
FLUORESCENCE
NICOTINIC ACETYLCHONE RECEPTOR
FREE FATTY ACIDS
title_short Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
title_full Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
title_fullStr Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
title_full_unstemmed Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
title_sort Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor
dc.creator.none.fl_str_mv Perillo, Vanesa Liliana
Barrantes, Francisco Jose
Antollini, Silvia Susana
author Perillo, Vanesa Liliana
author_facet Perillo, Vanesa Liliana
Barrantes, Francisco Jose
Antollini, Silvia Susana
author_role author
author2 Barrantes, Francisco Jose
Antollini, Silvia Susana
author2_role author
author
dc.subject.none.fl_str_mv FLUORESCENCE
NICOTINIC ACETYLCHONE RECEPTOR
FREE FATTY ACIDS
topic FLUORESCENCE
NICOTINIC ACETYLCHONE RECEPTOR
FREE FATTY ACIDS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Free fatty acids (FFA) are non-competitive antagonists of the nicotinic acetylcholine receptor (AChR) and their site of action is supposedly located at the lipid-AChR interface, where lipids can be annular or non-annular. It is known that the cis-unsaturated FFA, and not trans-unsaturated FFA, produce conformational modifications in the AChR resting state. Using T. californica receptor-rich membranes, we studied the changes in AChR conformational state generated by differences in the double-bond position of monounsaturated FFA. Using the higher affinity of the fluorescent AChR blocker crystal violet for the desensitized than for the resting state, it was observed that a double bond in positions ù 6 or ù 9 increased the KD values of the AChR in the desensitized state whereas no effect was observed in ù 11 or ù 13. Only FFAwith an ù 9 double bond changed the KD values in the resting state. DPH and Laurdan fluorescence studies showed that fluidity increased the most in FFAwith ù 9 and ù 11 double bonds and that ù 6 and ù 13 had less effect. Fluorescence resonance energy transfer experiments showed that the FFAwith an ù 6 double bond remained as an annular lipid whereas all the others also interact at non-annular sites. Thus, the location of the unsaturated double bond appears to be of critical importance for FFA-AChR interaction.
Fil: Perillo, Vanesa Liliana. 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
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
XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Puerto Madryn
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
description Free fatty acids (FFA) are non-competitive antagonists of the nicotinic acetylcholine receptor (AChR) and their site of action is supposedly located at the lipid-AChR interface, where lipids can be annular or non-annular. It is known that the cis-unsaturated FFA, and not trans-unsaturated FFA, produce conformational modifications in the AChR resting state. Using T. californica receptor-rich membranes, we studied the changes in AChR conformational state generated by differences in the double-bond position of monounsaturated FFA. Using the higher affinity of the fluorescent AChR blocker crystal violet for the desensitized than for the resting state, it was observed that a double bond in positions ù 6 or ù 9 increased the KD values of the AChR in the desensitized state whereas no effect was observed in ù 11 or ù 13. Only FFAwith an ù 9 double bond changed the KD values in the resting state. DPH and Laurdan fluorescence studies showed that fluidity increased the most in FFAwith ù 9 and ù 11 double bonds and that ù 6 and ù 13 had less effect. Fluorescence resonance energy transfer experiments showed that the FFAwith an ù 6 double bond remained as an annular lipid whereas all the others also interact at non-annular sites. Thus, the location of the unsaturated double bond appears to be of critical importance for FFA-AChR interaction.
publishDate 2010
dc.date.none.fl_str_mv 2010
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/11336/232473
Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor; XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Puerto Madryn; Argentina; 2010; 129-129
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/232473
identifier_str_mv Effects Of Unsaturated Fatty Acids On The Conformational State Of Nicotinic Acetylcholine Receptor; XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Puerto Madryn; Argentina; 2010; 129-129
0327-9545
1667-5746
CONICET Digital
CONICET
dc.language.none.fl_str_mv spa
language spa
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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.publisher.none.fl_str_mv Biocell
publisher.none.fl_str_mv Biocell
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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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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