Mostrar el registro sencillo del ítem
dc.contributor.author
Arias, Hugo Rubén
dc.contributor.author
McCardy, Elizabeth A
dc.contributor.author
Bayer, Erin Z.
dc.contributor.author
Gallagher, Martin J.
dc.contributor.author
Blanton, Michael P.
dc.date.available
2019-07-01T21:12:11Z
dc.date.issued
2002-07-01
dc.identifier.citation
Arias, Hugo Rubén; McCardy, Elizabeth A; Bayer, Erin Z.; Gallagher, Martin J.; Blanton, Michael P.; Allosterically linked noncompetitive antagonist binding sites in the resting nicotinic acetylcholine receptor ion channel; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 403; 1; 1-7-2002; 121-131
dc.identifier.issn
0003-9861
dc.identifier.uri
http://hdl.handle.net/11336/78992
dc.description.abstract
Previous studies have established the presence of overlapping binding sites for the noncompetitive antagonists (NCAs) amobarbital, tetracaine, and 3-trifluoromethyl-3-(m-[ 125 I]iodophenyl) diazirine ([ 125 I]TID) within the ion channel of the Torpedo nicotinic acetylcholine receptor (AChR) in the resting state. These well-characterized NCAs and competitive radioligand binding and photolabeling experiments were employed to better characterize the interaction of the dissociative anesthetics ketamine and thienylcycloexylpiperidine (TCP) with the resting AChR. Our experiments yielded what appear to be conflicting results: (i) both ketamine and TCP potentiated [ 125 I]TID photoincorporation into AChR subunits; and (ii) ketamine and TCP had very little effect on [ 14 C]amobarbital binding. Nevertheless, (iii) both ketamine and TCP completely displaced [ 3 H]tetracaine binding (K i s ∼ 20.9 and 2.0 μM, respectively) by a mutually exclusive mechanism. To reconcile these results we propose that, in the resting ion channel, TCP and ketamine bind to a site that is spatially distinct from the TID and barbiturate locus, while tetracaine bridges both binding sites.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Conformational States
dc.subject
Equilibrium Binding
dc.subject
Ketamine And Phencyclidine Binding Sites
dc.subject
Photoaffinity Labeling
dc.subject
Torpedo Nicotinic Acetylcholine Receptor
dc.subject.classification
Farmacología y Farmacia
dc.subject.classification
Medicina Básica
dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Allosterically linked noncompetitive antagonist binding sites in the resting nicotinic acetylcholine receptor ion channel
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-06-12T14:21:58Z
dc.journal.volume
403
dc.journal.number
1
dc.journal.pagination
121-131
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Massachusetts
dc.description.fil
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. University of Florida; Estados Unidos
dc.description.fil
Fil: McCardy, Elizabeth A. Texas Tech University Health Sciences Center; Estados Unidos
dc.description.fil
Fil: Bayer, Erin Z.. Texas Tech University Health Sciences Center; Estados Unidos
dc.description.fil
Fil: Gallagher, Martin J.. Washington University in St. Louis; Estados Unidos
dc.description.fil
Fil: Blanton, Michael P.. Texas Tech University Health Sciences Center; Estados Unidos
dc.journal.title
Archives of Biochemistry and Biophysics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S000398610200214X
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/S0003-9861(02)00214-X
Archivos asociados