Structural and functional characterization of human heteromeric 5-HT3 receptors
- Autores
- Corradi, Jeremias; Bouzat Cecilia
- Año de publicación
- 2016
- Idioma
- español castellano
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- 5-HT3 receptors are members of the Cys-loop receptor family that mediate fast excitatory transmission in central and peripheral nervous system. Genes for five different subunits (A-E) have been identified in humans, and most of the subunits have multiple isoforms. The A subunit is capable of forming functional homomeric (5-HT3A), or heteromeric receptors with the B subunit (5-HT3AB). Here we combine singlechannel and macroscopic current recordings to determine if other 5- HT3 subunits, Br1, Br2, C, D and E (B-E), can combine with the A subunit to form heteromeric receptors. After co-expression of the A subunit with each of the tested subunits, single-channel events with different conductance and kinetic properties with respect to those of 5-HT3A receptors were detected, except for the Br2 subunit. These results indicate that B-E subunits can assemble into functional heteromeric receptors with the A subunit. From the corresponding recordings, the analysis of the single-channel amplitude of the opening events suggests a possible stoichiometry for each heteromeric receptor, since each subunit (B-E).
Fil: Corradi, Jeremias. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Bouzat Cecilia. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
III Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016
Tucumán
Argentina
Sociedad Argentina de Biofísica - Materia
-
SEROTONIN
RECEPTORS
PATCH-CLAMP - 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:11336/237739
Ver los metadatos del registro completo
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Structural and functional characterization of human heteromeric 5-HT3 receptorsCorradi, JeremiasBouzat CeciliaSEROTONINRECEPTORSPATCH-CLAMPhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/15-HT3 receptors are members of the Cys-loop receptor family that mediate fast excitatory transmission in central and peripheral nervous system. Genes for five different subunits (A-E) have been identified in humans, and most of the subunits have multiple isoforms. The A subunit is capable of forming functional homomeric (5-HT3A), or heteromeric receptors with the B subunit (5-HT3AB). Here we combine singlechannel and macroscopic current recordings to determine if other 5- HT3 subunits, Br1, Br2, C, D and E (B-E), can combine with the A subunit to form heteromeric receptors. After co-expression of the A subunit with each of the tested subunits, single-channel events with different conductance and kinetic properties with respect to those of 5-HT3A receptors were detected, except for the Br2 subunit. These results indicate that B-E subunits can assemble into functional heteromeric receptors with the A subunit. From the corresponding recordings, the analysis of the single-channel amplitude of the opening events suggests a possible stoichiometry for each heteromeric receptor, since each subunit (B-E).Fil: Corradi, Jeremias. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaFil: Bouzat Cecilia. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaIII Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016TucumánArgentinaSociedad Argentina de BiofísicaSociedad Argentina de BiofísicaSica, Mauricio Pablo2016info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/237739Structural and functional characterization of human heteromeric 5-HT3 receptors; III Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016; Tucumán; Argentina; 2016; 240-240CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:56Zoai:ri.conicet.gov.ar:11336/237739instacron: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 10:01:57.193CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
title |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
spellingShingle |
Structural and functional characterization of human heteromeric 5-HT3 receptors Corradi, Jeremias SEROTONIN RECEPTORS PATCH-CLAMP |
title_short |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
title_full |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
title_fullStr |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
title_full_unstemmed |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
title_sort |
Structural and functional characterization of human heteromeric 5-HT3 receptors |
dc.creator.none.fl_str_mv |
Corradi, Jeremias Bouzat Cecilia |
author |
Corradi, Jeremias |
author_facet |
Corradi, Jeremias Bouzat Cecilia |
author_role |
author |
author2 |
Bouzat Cecilia |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Sica, Mauricio Pablo |
dc.subject.none.fl_str_mv |
SEROTONIN RECEPTORS PATCH-CLAMP |
topic |
SEROTONIN RECEPTORS PATCH-CLAMP |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
5-HT3 receptors are members of the Cys-loop receptor family that mediate fast excitatory transmission in central and peripheral nervous system. Genes for five different subunits (A-E) have been identified in humans, and most of the subunits have multiple isoforms. The A subunit is capable of forming functional homomeric (5-HT3A), or heteromeric receptors with the B subunit (5-HT3AB). Here we combine singlechannel and macroscopic current recordings to determine if other 5- HT3 subunits, Br1, Br2, C, D and E (B-E), can combine with the A subunit to form heteromeric receptors. After co-expression of the A subunit with each of the tested subunits, single-channel events with different conductance and kinetic properties with respect to those of 5-HT3A receptors were detected, except for the Br2 subunit. These results indicate that B-E subunits can assemble into functional heteromeric receptors with the A subunit. From the corresponding recordings, the analysis of the single-channel amplitude of the opening events suggests a possible stoichiometry for each heteromeric receptor, since each subunit (B-E). Fil: Corradi, Jeremias. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Bouzat Cecilia. 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina III Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016 Tucumán Argentina Sociedad Argentina de Biofísica |
description |
5-HT3 receptors are members of the Cys-loop receptor family that mediate fast excitatory transmission in central and peripheral nervous system. Genes for five different subunits (A-E) have been identified in humans, and most of the subunits have multiple isoforms. The A subunit is capable of forming functional homomeric (5-HT3A), or heteromeric receptors with the B subunit (5-HT3AB). Here we combine singlechannel and macroscopic current recordings to determine if other 5- HT3 subunits, Br1, Br2, C, D and E (B-E), can combine with the A subunit to form heteromeric receptors. After co-expression of the A subunit with each of the tested subunits, single-channel events with different conductance and kinetic properties with respect to those of 5-HT3A receptors were detected, except for the Br2 subunit. These results indicate that B-E subunits can assemble into functional heteromeric receptors with the A subunit. From the corresponding recordings, the analysis of the single-channel amplitude of the opening events suggests a possible stoichiometry for each heteromeric receptor, since each subunit (B-E). |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Congreso Book 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/11336/237739 Structural and functional characterization of human heteromeric 5-HT3 receptors; III Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016; Tucumán; Argentina; 2016; 240-240 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/237739 |
identifier_str_mv |
Structural and functional characterization of human heteromeric 5-HT3 receptors; III Latin American Federation of Biophysical Societies; IX IberoAmerican Congress of Biophysics; XLV Reunion Anual Sociedad Argentina de Biofísica 2016; Tucumán; Argentina; 2016; 240-240 CONICET Digital CONICET |
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spa |
language |
spa |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/ |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
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.coverage.none.fl_str_mv |
Internacional |
dc.publisher.none.fl_str_mv |
Sociedad Argentina de Biofísica |
publisher.none.fl_str_mv |
Sociedad Argentina de Biofísica |
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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13.13397 |