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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/237739

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spelling 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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language spa
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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/
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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
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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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