Not just any free fatty acid inhibits the nicotinic acetylcholine receptor
- Autores
- Perillo, Vanesa Liliana; Valles, Ana Sofia; Barrantes, Francisco Jose; Antollini, Silvia Susana
- Año de publicación
- 2011
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- To elucidate the mechanism involved in the non-competitive inhibition of the nicotinic acetylcholine receptor (AChR) caused by free fatty acids (FFAs), we studied the effect of FFAs with a single double-bond at different positions ( 6, 9, 11 and 13, cis-18:1) on different AChR properties. Two FFAs ( 6 and 9) reduced the duration of the channel open-state. The briefest component of the closed-time distribution remained unaltered, suggesting that 6 and 9 do not behave as typical open-channel blockers but rather as allosteric blockers. Fluorescence resonance energy transfer studies showed that all FFAs locate at the lipid-AChR interface, 6 being restricted to annular sites and all others occupying non-annular sites. Fluorescence quenching studies of pyrene-labeled AChR indicate that all cis-FFAs produce AChR conformational changes at the transmembrane level. Using the AChR conformationalsensitive probe crystal violet, we observed that all unsaturated FFAs increase its K in the AChR desensitized state, but only 9, D 11 and 13 cis-18:1 decrease its K in the resting state. In D conclusion, some FFAs appear to directly inhibit AChR function probably by localizing at superficial sites inside the membrane, whereas other FFAs modulate the receptor´s conformational states by a different mechanism.
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: Valles, Ana Sofia. 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
XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Potrero de los Funes
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular - Materia
-
RECEPTOR DE ACETILCOLINA NICOTINICO
ESPECTROSCOPIA DE FLUORESCENCIA
INTERACCION LIPIDO-PROTEICA
ACIDOS GRASOS LIBRES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/244982
Ver los metadatos del registro completo
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Not just any free fatty acid inhibits the nicotinic acetylcholine receptorPerillo, Vanesa LilianaValles, Ana SofiaBarrantes, Francisco JoseAntollini, Silvia SusanaRECEPTOR DE ACETILCOLINA NICOTINICOESPECTROSCOPIA DE FLUORESCENCIAINTERACCION LIPIDO-PROTEICAACIDOS GRASOS LIBREShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1To elucidate the mechanism involved in the non-competitive inhibition of the nicotinic acetylcholine receptor (AChR) caused by free fatty acids (FFAs), we studied the effect of FFAs with a single double-bond at different positions ( 6, 9, 11 and 13, cis-18:1) on different AChR properties. Two FFAs ( 6 and 9) reduced the duration of the channel open-state. The briefest component of the closed-time distribution remained unaltered, suggesting that 6 and 9 do not behave as typical open-channel blockers but rather as allosteric blockers. Fluorescence resonance energy transfer studies showed that all FFAs locate at the lipid-AChR interface, 6 being restricted to annular sites and all others occupying non-annular sites. Fluorescence quenching studies of pyrene-labeled AChR indicate that all cis-FFAs produce AChR conformational changes at the transmembrane level. Using the AChR conformationalsensitive probe crystal violet, we observed that all unsaturated FFAs increase its K in the AChR desensitized state, but only 9, D 11 and 13 cis-18:1 decrease its K in the resting state. In D conclusion, some FFAs appear to directly inhibit AChR function probably by localizing at superficial sites inside the membrane, whereas other FFAs modulate the receptor´s conformational states by a different mechanism.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: Valles, Ana Sofia. 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; ArgentinaXLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología MolecularPotrero de los FunesArgentinaSociedad 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/11336/244982Not just any free fatty acid inhibits the nicotinic acetylcholine receptor; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes; Argentina; 2011; 123-1230327-95451667-5746CONICET DigitalCONICETenginfo: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 Técnicas2025-09-03T09:46:50Zoai:ri.conicet.gov.ar:11336/244982instacron: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 09:46:50.295CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| title |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| spellingShingle |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor Perillo, Vanesa Liliana RECEPTOR DE ACETILCOLINA NICOTINICO ESPECTROSCOPIA DE FLUORESCENCIA INTERACCION LIPIDO-PROTEICA ACIDOS GRASOS LIBRES |
| title_short |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| title_full |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| title_fullStr |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| title_full_unstemmed |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| title_sort |
Not just any free fatty acid inhibits the nicotinic acetylcholine receptor |
| dc.creator.none.fl_str_mv |
Perillo, Vanesa Liliana Valles, Ana Sofia Barrantes, Francisco Jose Antollini, Silvia Susana |
| author |
Perillo, Vanesa Liliana |
| author_facet |
Perillo, Vanesa Liliana Valles, Ana Sofia Barrantes, Francisco Jose Antollini, Silvia Susana |
| author_role |
author |
| author2 |
Valles, Ana Sofia Barrantes, Francisco Jose Antollini, Silvia Susana |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
RECEPTOR DE ACETILCOLINA NICOTINICO ESPECTROSCOPIA DE FLUORESCENCIA INTERACCION LIPIDO-PROTEICA ACIDOS GRASOS LIBRES |
| topic |
RECEPTOR DE ACETILCOLINA NICOTINICO ESPECTROSCOPIA DE FLUORESCENCIA INTERACCION LIPIDO-PROTEICA ACIDOS GRASOS LIBRES |
| 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 elucidate the mechanism involved in the non-competitive inhibition of the nicotinic acetylcholine receptor (AChR) caused by free fatty acids (FFAs), we studied the effect of FFAs with a single double-bond at different positions ( 6, 9, 11 and 13, cis-18:1) on different AChR properties. Two FFAs ( 6 and 9) reduced the duration of the channel open-state. The briefest component of the closed-time distribution remained unaltered, suggesting that 6 and 9 do not behave as typical open-channel blockers but rather as allosteric blockers. Fluorescence resonance energy transfer studies showed that all FFAs locate at the lipid-AChR interface, 6 being restricted to annular sites and all others occupying non-annular sites. Fluorescence quenching studies of pyrene-labeled AChR indicate that all cis-FFAs produce AChR conformational changes at the transmembrane level. Using the AChR conformationalsensitive probe crystal violet, we observed that all unsaturated FFAs increase its K in the AChR desensitized state, but only 9, D 11 and 13 cis-18:1 decrease its K in the resting state. In D conclusion, some FFAs appear to directly inhibit AChR function probably by localizing at superficial sites inside the membrane, whereas other FFAs modulate the receptor´s conformational states by a different mechanism. 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: Valles, Ana Sofia. 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 XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular Potrero de los Funes Argentina Sociedad Argentina de Investigación en Bioquímica y Biología Molecular |
| description |
To elucidate the mechanism involved in the non-competitive inhibition of the nicotinic acetylcholine receptor (AChR) caused by free fatty acids (FFAs), we studied the effect of FFAs with a single double-bond at different positions ( 6, 9, 11 and 13, cis-18:1) on different AChR properties. Two FFAs ( 6 and 9) reduced the duration of the channel open-state. The briefest component of the closed-time distribution remained unaltered, suggesting that 6 and 9 do not behave as typical open-channel blockers but rather as allosteric blockers. Fluorescence resonance energy transfer studies showed that all FFAs locate at the lipid-AChR interface, 6 being restricted to annular sites and all others occupying non-annular sites. Fluorescence quenching studies of pyrene-labeled AChR indicate that all cis-FFAs produce AChR conformational changes at the transmembrane level. Using the AChR conformationalsensitive probe crystal violet, we observed that all unsaturated FFAs increase its K in the AChR desensitized state, but only 9, D 11 and 13 cis-18:1 decrease its K in the resting state. In D conclusion, some FFAs appear to directly inhibit AChR function probably by localizing at superficial sites inside the membrane, whereas other FFAs modulate the receptor´s conformational states by a different mechanism. |
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2011 |
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2011 |
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http://hdl.handle.net/11336/244982 Not just any free fatty acid inhibits the nicotinic acetylcholine receptor; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes; Argentina; 2011; 123-123 0327-9545 1667-5746 CONICET Digital CONICET |
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Not just any free fatty acid inhibits the nicotinic acetylcholine receptor; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Potrero de los Funes; Argentina; 2011; 123-123 0327-9545 1667-5746 CONICET Digital CONICET |
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