Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors

Autores
Arias, Hugo Rubén; Bhumireddy, Pankaj
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The nicotinic acetylcholine receptor (AChR) is the archetype of the Cys-loop ligand-gated ion channel'receptor superfamily. Noncompetitive antagonists inhibit the AChR without interacting directly with agonist sites. Among non-competitive antagonists, general and local anesthetics have been used for decades to study the structure and function of muscle- as well as neurorial-type AChRs. In this review, we address and update all information regarding the characterization of binding sites and the mechanism of action for n-alkanols, barbiturates, inhalational and dissociative general anesthetics, as well as for tertiary and quaternary local anesthetics. The experimental evidence outlined in this review suggest that: (1) several neuronal-type AChRs might be targets for the pharmacological action of distinct anesthetics; (2) the molecular components of a specific anesthetic locus on a certain receptor type are different from the structural determinants of the site for the same anesthetic on a different receptor type; (3) there are unique binding sites for distinct anesthetics in the same receptor; (4) the affinity of a specific anesthetic depends on the AChR conformational state; (5) anesthetics may inhibit AChRs by different mechanisms including open-channel-blocking, augmenting the desensitization process, and/or inactivating the opening of resting receptors; and (6) some anesthetics may potentiate AChR activity.
Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Western University of Health Sciences; Estados Unidos
Fil: Bhumireddy, Pankaj. Western University of Health Sciences; Estados Unidos
Materia
MUSCLE-TYPE NICOTINIC ACETYCHOLINE RECEPTOR
LIGAND-GATED ION CHANNEL
TRASMEMBRANE DOMAIN
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:11336/97075
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptorsArias, Hugo RubénBhumireddy, PankajMUSCLE-TYPE NICOTINIC ACETYCHOLINE RECEPTORLIGAND-GATED ION CHANNELTRASMEMBRANE DOMAINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The nicotinic acetylcholine receptor (AChR) is the archetype of the Cys-loop ligand-gated ion channel'receptor superfamily. Noncompetitive antagonists inhibit the AChR without interacting directly with agonist sites. Among non-competitive antagonists, general and local anesthetics have been used for decades to study the structure and function of muscle- as well as neurorial-type AChRs. In this review, we address and update all information regarding the characterization of binding sites and the mechanism of action for n-alkanols, barbiturates, inhalational and dissociative general anesthetics, as well as for tertiary and quaternary local anesthetics. The experimental evidence outlined in this review suggest that: (1) several neuronal-type AChRs might be targets for the pharmacological action of distinct anesthetics; (2) the molecular components of a specific anesthetic locus on a certain receptor type are different from the structural determinants of the site for the same anesthetic on a different receptor type; (3) there are unique binding sites for distinct anesthetics in the same receptor; (4) the affinity of a specific anesthetic depends on the AChR conformational state; (5) anesthetics may inhibit AChRs by different mechanisms including open-channel-blocking, augmenting the desensitization process, and/or inactivating the opening of resting receptors; and (6) some anesthetics may potentiate AChR activity.Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Western University of Health Sciences; Estados UnidosFil: Bhumireddy, Pankaj. Western University of Health Sciences; Estados UnidosBentham Science Publishers2005-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/97075Arias, Hugo Rubén; Bhumireddy, Pankaj; Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors; Bentham Science Publishers; Current Protein and Peptide Science; 6; 5; 10-2005; 451-4721389-2037CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.2174/138920305774329331info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/79467/articleinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:02:58Zoai:ri.conicet.gov.ar:11336/97075instacron: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:34982025-10-22 12:02:58.923CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
title Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
spellingShingle Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
Arias, Hugo Rubén
MUSCLE-TYPE NICOTINIC ACETYCHOLINE RECEPTOR
LIGAND-GATED ION CHANNEL
TRASMEMBRANE DOMAIN
title_short Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
title_full Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
title_fullStr Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
title_full_unstemmed Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
title_sort Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
dc.creator.none.fl_str_mv Arias, Hugo Rubén
Bhumireddy, Pankaj
author Arias, Hugo Rubén
author_facet Arias, Hugo Rubén
Bhumireddy, Pankaj
author_role author
author2 Bhumireddy, Pankaj
author2_role author
dc.subject.none.fl_str_mv MUSCLE-TYPE NICOTINIC ACETYCHOLINE RECEPTOR
LIGAND-GATED ION CHANNEL
TRASMEMBRANE DOMAIN
topic MUSCLE-TYPE NICOTINIC ACETYCHOLINE RECEPTOR
LIGAND-GATED ION CHANNEL
TRASMEMBRANE DOMAIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The nicotinic acetylcholine receptor (AChR) is the archetype of the Cys-loop ligand-gated ion channel'receptor superfamily. Noncompetitive antagonists inhibit the AChR without interacting directly with agonist sites. Among non-competitive antagonists, general and local anesthetics have been used for decades to study the structure and function of muscle- as well as neurorial-type AChRs. In this review, we address and update all information regarding the characterization of binding sites and the mechanism of action for n-alkanols, barbiturates, inhalational and dissociative general anesthetics, as well as for tertiary and quaternary local anesthetics. The experimental evidence outlined in this review suggest that: (1) several neuronal-type AChRs might be targets for the pharmacological action of distinct anesthetics; (2) the molecular components of a specific anesthetic locus on a certain receptor type are different from the structural determinants of the site for the same anesthetic on a different receptor type; (3) there are unique binding sites for distinct anesthetics in the same receptor; (4) the affinity of a specific anesthetic depends on the AChR conformational state; (5) anesthetics may inhibit AChRs by different mechanisms including open-channel-blocking, augmenting the desensitization process, and/or inactivating the opening of resting receptors; and (6) some anesthetics may potentiate AChR activity.
Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Western University of Health Sciences; Estados Unidos
Fil: Bhumireddy, Pankaj. Western University of Health Sciences; Estados Unidos
description The nicotinic acetylcholine receptor (AChR) is the archetype of the Cys-loop ligand-gated ion channel'receptor superfamily. Noncompetitive antagonists inhibit the AChR without interacting directly with agonist sites. Among non-competitive antagonists, general and local anesthetics have been used for decades to study the structure and function of muscle- as well as neurorial-type AChRs. In this review, we address and update all information regarding the characterization of binding sites and the mechanism of action for n-alkanols, barbiturates, inhalational and dissociative general anesthetics, as well as for tertiary and quaternary local anesthetics. The experimental evidence outlined in this review suggest that: (1) several neuronal-type AChRs might be targets for the pharmacological action of distinct anesthetics; (2) the molecular components of a specific anesthetic locus on a certain receptor type are different from the structural determinants of the site for the same anesthetic on a different receptor type; (3) there are unique binding sites for distinct anesthetics in the same receptor; (4) the affinity of a specific anesthetic depends on the AChR conformational state; (5) anesthetics may inhibit AChRs by different mechanisms including open-channel-blocking, augmenting the desensitization process, and/or inactivating the opening of resting receptors; and (6) some anesthetics may potentiate AChR activity.
publishDate 2005
dc.date.none.fl_str_mv 2005-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/97075
Arias, Hugo Rubén; Bhumireddy, Pankaj; Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors; Bentham Science Publishers; Current Protein and Peptide Science; 6; 5; 10-2005; 451-472
1389-2037
CONICET Digital
CONICET
url http://hdl.handle.net/11336/97075
identifier_str_mv Arias, Hugo Rubén; Bhumireddy, Pankaj; Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors; Bentham Science Publishers; Current Protein and Peptide Science; 6; 5; 10-2005; 451-472
1389-2037
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2174/138920305774329331
info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/79467/article
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/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
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 12.982451

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