Extracellular Allosteric Na+ Binding to the Na+,K+-ATPase in Cardiac Myocytes
Extracellular Allosteric Na+ Binding to the Na+,K+-ATPase in Cardiac Myocytes
Loading...
Date
2013
Authors
Garcia, Alvaro
Fry, Natasha A.S.
Karimi, Keyvan
Liu, Chia-chi
Rasmussen, Helge
Clarke, Ronald
Editors
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
URI (citable link)
DOI (citable link)
International patent number
Link to the license
EU project number
Project
Open Access publication
Collections
Title in another language
Publication type
Journal article
Publication status
Published in
Biophysical Journal ; 105 (2013), 12. - pp. 2695-2705. - ISSN 0006-3495. - eISSN 1542-0086
Abstract
Whole-cell patch-clamp measurements of the current, Ip, produced by the Na+,K+-ATPase across the plasma membrane of rabbit cardiac myocytes show an increase in Ip over the extracellular Na+ concentration range 0–50 mM. This is not predicted by the classical Albers-Post scheme of the Na+,K+-ATPase mechanism, where extracellular Na+ should act as a competitive inhibitor of extracellular K+ binding, which is necessary for the stimulation of enzyme dephosphorylation and the pumping of K+ ions into the cytoplasm. The increase in Ip is consistent with Na+ binding to an extracellular allosteric site, independent of the ion transport sites, and an increase in turnover via an acceleration of the rate-determining release of K+ to the cytoplasm, E2(K+)2 → E1 + 2K+. At normal physiological concentrations of extracellular Na+ of 140 mM, it is to be expected that binding of Na+ to the allosteric site would be nearly saturated. Its purpose would seem to be simply to optimize the enzyme’s ion pumping rate under its normal physiological conditions. Based on published crystal structures, a possible location of the allosteric site is within a cleft between the α- and β-subunits of the enzyme
Summary in another language
Subject (DDC)
570 Biosciences, Biology
Keywords
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690
GARCIA, Alvaro, Natasha A.S. FRY, Keyvan KARIMI, Chia-chi LIU, Hans-Jürgen APELL, Helge RASMUSSEN, Ronald CLARKE, 2013. Extracellular Allosteric Na+ Binding to the Na+,K+-ATPase in Cardiac Myocytes. In: Biophysical Journal. 105(12), pp. 2695-2705. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2013.11.004BibTex
@article{Garcia2013-12-17Extra-25574, year={2013}, doi={10.1016/j.bpj.2013.11.004}, title={Extracellular Allosteric Na<sup>+</sup> Binding to the Na<sup>+</sup>,K<sup>+</sup>-ATPase in Cardiac Myocytes}, number={12}, volume={105}, issn={0006-3495}, journal={Biophysical Journal}, pages={2695--2705}, author={Garcia, Alvaro and Fry, Natasha A.S. and Karimi, Keyvan and Liu, Chia-chi and Apell, Hans-Jürgen and Rasmussen, Helge and Clarke, Ronald} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/25574"> <dc:contributor>Rasmussen, Helge</dc:contributor> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/25574/1/Garcia_255748.pdf"/> <dc:contributor>Garcia, Alvaro</dc:contributor> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dcterms:issued>2013-12-17</dcterms:issued> <dc:contributor>Fry, Natasha A.S.</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:contributor>Karimi, Keyvan</dc:contributor> <dc:language>eng</dc:language> <dcterms:title>Extracellular Allosteric Na<sup>+</sup> Binding to the Na<sup>+</sup>,K<sup>+</sup>-ATPase in Cardiac Myocytes</dcterms:title> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-01-10T10:54:02Z</dc:date> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dc:creator>Fry, Natasha A.S.</dc:creator> <dc:contributor>Liu, Chia-chi</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/25574"/> <dc:rights>terms-of-use</dc:rights> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Liu, Chia-chi</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:abstract xml:lang="eng">Whole-cell patch-clamp measurements of the current, Ip, produced by the Na+,K+-ATPase across the plasma membrane of rabbit cardiac myocytes show an increase in Ip over the extracellular Na+ concentration range 0–50 mM. This is not predicted by the classical Albers-Post scheme of the Na+,K+-ATPase mechanism, where extracellular Na+ should act as a competitive inhibitor of extracellular K+ binding, which is necessary for the stimulation of enzyme dephosphorylation and the pumping of K+ ions into the cytoplasm. The increase in Ip is consistent with Na+ binding to an extracellular allosteric site, independent of the ion transport sites, and an increase in turnover via an acceleration of the rate-determining release of K+ to the cytoplasm, E2(K+)2 → E1 + 2K+. At normal physiological concentrations of extracellular Na+ of 140 mM, it is to be expected that binding of Na+ to the allosteric site would be nearly saturated. Its purpose would seem to be simply to optimize the enzyme’s ion pumping rate under its normal physiological conditions. Based on published crystal structures, a possible location of the allosteric site is within a cleft between the α- and β-subunits of the enzyme</dcterms:abstract> <dc:creator>Clarke, Ronald</dc:creator> <dc:creator>Rasmussen, Helge</dc:creator> <dc:creator>Karimi, Keyvan</dc:creator> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/25574/1/Garcia_255748.pdf"/> <dc:creator>Garcia, Alvaro</dc:creator> <dcterms:bibliographicCitation>Biophysical Journal ; 105 (2013), 12. - S. 2695-2705</dcterms:bibliographicCitation> <dc:contributor>Clarke, Ronald</dc:contributor> </rdf:Description> </rdf:RDF>
Internal note
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Examination date of dissertation
Method of financing
Comment on publication
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
Yes