Expanding our knowledge about the structure and function of the serotonin type 3 receptor

Autores
Corradi, Jeremias
Año de publicación
2018
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Serotonin (5-hydroxytryptamine: 5-HT) is a monoamine with diverse and important functions in nearly every living organism in the Earth. 5-HT3 receptors are the only members of the 5-HT receptors subfamily (5-HT1-7) that belong to the Cys-loop receptor family. They are ligand-gated ion channels that mediate fast synaptic responses in the central and peripheral nervous system and are implicated in many physiological and pathological processes, such as cognition, pain, vomiting reflex, depression, anxiety, among others. Five subunits have been identified in humans (A-E), where the A is the only capable of forming homomeric receptors (5- HT3A), and the B-E are accessory subunits that only form receptors by combining with A. Since its discovery, the 5-HT3A receptor has been widely studied through electrophysiological methods limited to the acquisition of macroscopic currents due to its very low conductance. By incorporation of a triple mutation in the intracellular loop we obtained a high-conductance receptor (5-HT3AHC). Using this model receptor, we were able to record single-channel events which, in combination with macroscopic currents, kinetics analysis and in silico studies, allowed us to reveal the mechanisms for receptor activation by full and partial agonists, and to identify sites and mechanisms of modulation. Our results also showed that the AHC subunit is a valuable tool for the elucidation of the stoichiometry of heteromeric receptors. All this information provides new clues for understanding about 5-HT3 receptors implication in human health and for the designing of more selective drugs.
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
XLVII Reunión Anual de la Sociedad Argentina de Biofísica
La Plata
Argentina
Sociedad Argentina de Biofísica
Materia
SEROTONIN
PATCH-CLAMP
HETEROMERIC RECEPTORS
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:11336/220083
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Expanding our knowledge about the structure and function of the serotonin type 3 receptorCorradi, JeremiasSEROTONINPATCH-CLAMPHETEROMERIC RECEPTORShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Serotonin (5-hydroxytryptamine: 5-HT) is a monoamine with diverse and important functions in nearly every living organism in the Earth. 5-HT3 receptors are the only members of the 5-HT receptors subfamily (5-HT1-7) that belong to the Cys-loop receptor family. They are ligand-gated ion channels that mediate fast synaptic responses in the central and peripheral nervous system and are implicated in many physiological and pathological processes, such as cognition, pain, vomiting reflex, depression, anxiety, among others. Five subunits have been identified in humans (A-E), where the A is the only capable of forming homomeric receptors (5- HT3A), and the B-E are accessory subunits that only form receptors by combining with A. Since its discovery, the 5-HT3A receptor has been widely studied through electrophysiological methods limited to the acquisition of macroscopic currents due to its very low conductance. By incorporation of a triple mutation in the intracellular loop we obtained a high-conductance receptor (5-HT3AHC). Using this model receptor, we were able to record single-channel events which, in combination with macroscopic currents, kinetics analysis and in silico studies, allowed us to reveal the mechanisms for receptor activation by full and partial agonists, and to identify sites and mechanisms of modulation. Our results also showed that the AHC subunit is a valuable tool for the elucidation of the stoichiometry of heteromeric receptors. All this information provides new clues for understanding about 5-HT3 receptors implication in human health and for the designing of more selective drugs.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; ArgentinaXLVII Reunión Anual de la Sociedad Argentina de BiofísicaLa PlataArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2018info: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/11336/220083Expanding our knowledge about the structure and function of the serotonin type 3 receptor; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 33-33978-987-27591-6-2CONICET DigitalCONICETenginfo: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 Técnicas2025-09-03T09:49:21Zoai:ri.conicet.gov.ar:11336/220083instacron: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 09:49:21.971CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Expanding our knowledge about the structure and function of the serotonin type 3 receptor
title Expanding our knowledge about the structure and function of the serotonin type 3 receptor
spellingShingle Expanding our knowledge about the structure and function of the serotonin type 3 receptor
Corradi, Jeremias
SEROTONIN
PATCH-CLAMP
HETEROMERIC RECEPTORS
title_short Expanding our knowledge about the structure and function of the serotonin type 3 receptor
title_full Expanding our knowledge about the structure and function of the serotonin type 3 receptor
title_fullStr Expanding our knowledge about the structure and function of the serotonin type 3 receptor
title_full_unstemmed Expanding our knowledge about the structure and function of the serotonin type 3 receptor
title_sort Expanding our knowledge about the structure and function of the serotonin type 3 receptor
dc.creator.none.fl_str_mv Corradi, Jeremias
author Corradi, Jeremias
author_facet Corradi, Jeremias
author_role author
dc.subject.none.fl_str_mv SEROTONIN
PATCH-CLAMP
HETEROMERIC RECEPTORS
topic SEROTONIN
PATCH-CLAMP
HETEROMERIC RECEPTORS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Serotonin (5-hydroxytryptamine: 5-HT) is a monoamine with diverse and important functions in nearly every living organism in the Earth. 5-HT3 receptors are the only members of the 5-HT receptors subfamily (5-HT1-7) that belong to the Cys-loop receptor family. They are ligand-gated ion channels that mediate fast synaptic responses in the central and peripheral nervous system and are implicated in many physiological and pathological processes, such as cognition, pain, vomiting reflex, depression, anxiety, among others. Five subunits have been identified in humans (A-E), where the A is the only capable of forming homomeric receptors (5- HT3A), and the B-E are accessory subunits that only form receptors by combining with A. Since its discovery, the 5-HT3A receptor has been widely studied through electrophysiological methods limited to the acquisition of macroscopic currents due to its very low conductance. By incorporation of a triple mutation in the intracellular loop we obtained a high-conductance receptor (5-HT3AHC). Using this model receptor, we were able to record single-channel events which, in combination with macroscopic currents, kinetics analysis and in silico studies, allowed us to reveal the mechanisms for receptor activation by full and partial agonists, and to identify sites and mechanisms of modulation. Our results also showed that the AHC subunit is a valuable tool for the elucidation of the stoichiometry of heteromeric receptors. All this information provides new clues for understanding about 5-HT3 receptors implication in human health and for the designing of more selective drugs.
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
XLVII Reunión Anual de la Sociedad Argentina de Biofísica
La Plata
Argentina
Sociedad Argentina de Biofísica
description Serotonin (5-hydroxytryptamine: 5-HT) is a monoamine with diverse and important functions in nearly every living organism in the Earth. 5-HT3 receptors are the only members of the 5-HT receptors subfamily (5-HT1-7) that belong to the Cys-loop receptor family. They are ligand-gated ion channels that mediate fast synaptic responses in the central and peripheral nervous system and are implicated in many physiological and pathological processes, such as cognition, pain, vomiting reflex, depression, anxiety, among others. Five subunits have been identified in humans (A-E), where the A is the only capable of forming homomeric receptors (5- HT3A), and the B-E are accessory subunits that only form receptors by combining with A. Since its discovery, the 5-HT3A receptor has been widely studied through electrophysiological methods limited to the acquisition of macroscopic currents due to its very low conductance. By incorporation of a triple mutation in the intracellular loop we obtained a high-conductance receptor (5-HT3AHC). Using this model receptor, we were able to record single-channel events which, in combination with macroscopic currents, kinetics analysis and in silico studies, allowed us to reveal the mechanisms for receptor activation by full and partial agonists, and to identify sites and mechanisms of modulation. Our results also showed that the AHC subunit is a valuable tool for the elucidation of the stoichiometry of heteromeric receptors. All this information provides new clues for understanding about 5-HT3 receptors implication in human health and for the designing of more selective drugs.
publishDate 2018
dc.date.none.fl_str_mv 2018
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/11336/220083
Expanding our knowledge about the structure and function of the serotonin type 3 receptor; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 33-33
978-987-27591-6-2
CONICET Digital
CONICET
url http://hdl.handle.net/11336/220083
identifier_str_mv Expanding our knowledge about the structure and function of the serotonin type 3 receptor; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 33-33
978-987-27591-6-2
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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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score 13.13397

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