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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/232473
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:38:55Zoai: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:34982025-09-29 10:38:55.431CONICET 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 |
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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 |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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