Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study

Detalhes bibliográficos
Autor(a) principal: Srinivasan, Chandra
Data de Publicação: 1999
Outros Autores: Minadeo, Nicole, Toon, Jason, Graham, Daniel, Freitas, Duarte Mota de, Geraldes, Carlos F. G. C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/3897
https://doi.org/10.1006/jmre.1999.1813
Resumo: Evidence for competition between Li+ and Na+ for binding sites of human unsealed and cytoskeleton-depleted human red blood cell (csdRBC) membranes was obtained from the effect of added Li+ upon the 23Na double quantum filtered (DQF) and triple quantum filtered (TQF) NMR signals of Na+-containing red blood cell (RBC) membrane suspensions. We found that, at low ionic strength, the observed quenching effect of Li+ on the 23Na TQF and DQF signal intensity probed Li+/Na+ competition for isotropic binding sites only. Membrane cytoskeleton depletion significantly decreased the isotropic signal intensity, strongly affecting the binding of Na+ to isotropic membrane sites, but had no effect on Li+/Na+ competition for those sites. Through the observed 23Na DQF NMR spectra, which allow probing of both isotropic and anisotropic Na+ motion, we found anisotropic membrane binding sites for Na+ when the total ionic strength was higher than 40 mM. This is a consequence of ionic strength effects on the conformation of the cytoskeleton, in particular on the dimer-tetramer equilibrium of spectrin. The determinant involvement of the cytoskeleton in the anisotropy of Na+ motion at the membrane surface was demonstrated by the isotropy of the DQF spectra of csdRBC membranes even at high ionic strength. Li+ addition initially quenched the isotropic signal the most, indicating preferential Li+/Na+ competition for the isotropic membrane sites. High ionic strength also increased the intensity of the anisotropic signal, due to its effect on the restructuring of the membrane cytoskeleton. Further Li+ addition competed with Na+ for those sites, quenching the anisotropic signal.
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spelling Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Studylithium; human red blood cell membranes; cytoskeleton; multiple-quantum-filtered 23Na NMR; 7Li relaxation timesEvidence for competition between Li+ and Na+ for binding sites of human unsealed and cytoskeleton-depleted human red blood cell (csdRBC) membranes was obtained from the effect of added Li+ upon the 23Na double quantum filtered (DQF) and triple quantum filtered (TQF) NMR signals of Na+-containing red blood cell (RBC) membrane suspensions. We found that, at low ionic strength, the observed quenching effect of Li+ on the 23Na TQF and DQF signal intensity probed Li+/Na+ competition for isotropic binding sites only. Membrane cytoskeleton depletion significantly decreased the isotropic signal intensity, strongly affecting the binding of Na+ to isotropic membrane sites, but had no effect on Li+/Na+ competition for those sites. Through the observed 23Na DQF NMR spectra, which allow probing of both isotropic and anisotropic Na+ motion, we found anisotropic membrane binding sites for Na+ when the total ionic strength was higher than 40 mM. This is a consequence of ionic strength effects on the conformation of the cytoskeleton, in particular on the dimer-tetramer equilibrium of spectrin. The determinant involvement of the cytoskeleton in the anisotropy of Na+ motion at the membrane surface was demonstrated by the isotropy of the DQF spectra of csdRBC membranes even at high ionic strength. Li+ addition initially quenched the isotropic signal the most, indicating preferential Li+/Na+ competition for the isotropic membrane sites. High ionic strength also increased the intensity of the anisotropic signal, due to its effect on the restructuring of the membrane cytoskeleton. Further Li+ addition competed with Na+ for those sites, quenching the anisotropic signal.http://www.sciencedirect.com/science/article/B6WJX-45FKRY3-38/1/bc487aa2e53ceb4bdc5b795e1fbc7ee41999info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleaplication/PDFhttp://hdl.handle.net/10316/3897http://hdl.handle.net/10316/3897https://doi.org/10.1006/jmre.1999.1813engJournal of Magnetic Resonance. 140:1 (1999) 206-217Srinivasan, ChandraMinadeo, NicoleToon, JasonGraham, DanielFreitas, Duarte Mota deGeraldes, Carlos F. G. C.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2020-11-06T16:48:38Zoai:estudogeral.uc.pt:10316/3897Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:55:47.561617Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
title Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
spellingShingle Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
Srinivasan, Chandra
lithium; human red blood cell membranes; cytoskeleton; multiple-quantum-filtered 23Na NMR; 7Li relaxation times
title_short Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
title_full Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
title_fullStr Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
title_full_unstemmed Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
title_sort Competition between Na+ and Li+ for Unsealed and Cytoskeleton-Depleted Human Red Blood Cell Membrane: A 23Na Multiple Quantum Filtered and 7Li NMR Relaxation Study
author Srinivasan, Chandra
author_facet Srinivasan, Chandra
Minadeo, Nicole
Toon, Jason
Graham, Daniel
Freitas, Duarte Mota de
Geraldes, Carlos F. G. C.
author_role author
author2 Minadeo, Nicole
Toon, Jason
Graham, Daniel
Freitas, Duarte Mota de
Geraldes, Carlos F. G. C.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Srinivasan, Chandra
Minadeo, Nicole
Toon, Jason
Graham, Daniel
Freitas, Duarte Mota de
Geraldes, Carlos F. G. C.
dc.subject.por.fl_str_mv lithium; human red blood cell membranes; cytoskeleton; multiple-quantum-filtered 23Na NMR; 7Li relaxation times
topic lithium; human red blood cell membranes; cytoskeleton; multiple-quantum-filtered 23Na NMR; 7Li relaxation times
description Evidence for competition between Li+ and Na+ for binding sites of human unsealed and cytoskeleton-depleted human red blood cell (csdRBC) membranes was obtained from the effect of added Li+ upon the 23Na double quantum filtered (DQF) and triple quantum filtered (TQF) NMR signals of Na+-containing red blood cell (RBC) membrane suspensions. We found that, at low ionic strength, the observed quenching effect of Li+ on the 23Na TQF and DQF signal intensity probed Li+/Na+ competition for isotropic binding sites only. Membrane cytoskeleton depletion significantly decreased the isotropic signal intensity, strongly affecting the binding of Na+ to isotropic membrane sites, but had no effect on Li+/Na+ competition for those sites. Through the observed 23Na DQF NMR spectra, which allow probing of both isotropic and anisotropic Na+ motion, we found anisotropic membrane binding sites for Na+ when the total ionic strength was higher than 40 mM. This is a consequence of ionic strength effects on the conformation of the cytoskeleton, in particular on the dimer-tetramer equilibrium of spectrin. The determinant involvement of the cytoskeleton in the anisotropy of Na+ motion at the membrane surface was demonstrated by the isotropy of the DQF spectra of csdRBC membranes even at high ionic strength. Li+ addition initially quenched the isotropic signal the most, indicating preferential Li+/Na+ competition for the isotropic membrane sites. High ionic strength also increased the intensity of the anisotropic signal, due to its effect on the restructuring of the membrane cytoskeleton. Further Li+ addition competed with Na+ for those sites, quenching the anisotropic signal.
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10316/3897
http://hdl.handle.net/10316/3897
https://doi.org/10.1006/jmre.1999.1813
url http://hdl.handle.net/10316/3897
https://doi.org/10.1006/jmre.1999.1813
dc.language.iso.fl_str_mv eng
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dc.relation.none.fl_str_mv Journal of Magnetic Resonance. 140:1 (1999) 206-217
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eu_rights_str_mv openAccess
dc.format.none.fl_str_mv aplication/PDF
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