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|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||Authors:||Srinivasan, Chandra
Freitas, Duarte Mota de
Geraldes, Carlos F. G. C.
|Keywords:||lithium; human red blood cell membranes; cytoskeleton; multiple-quantum-filtered 23Na NMR; 7Li relaxation times||Issue Date:||1999||Citation:||Journal of Magnetic Resonance. 140:1 (1999) 206-217||Abstract:||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.||URI:||http://hdl.handle.net/10316/3897||Rights:||openAccess|
|Appears in Collections:||FCTUC Ciências da Vida - Artigos em Revistas Internacionais|
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