Table of Contents
Metal-Based Drugs
Volume 7, Issue 6, Pages 357-364

Li+ Influx and Binding, and Li+/Mg2+ Competition in Bovine Chromaffin Cell Suspensions as Studied by 7Li NMR and Fluorescence Spectroscopy

1Department of Biochemistry, University of Coimbra, P.O. Box 3126, Coimbra 3000, Portugal
2Center for Neuroscience, University of Coimbra, P.O. Box 3126, Coimbra 3000, Portugal
3Chemistry Department, Loyola University of Chicago, Chicago 60626, IL, USA

Received 21 February 2001; Accepted 28 February 2001

Copyright © 2000 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Li+ influx by bovine chromaffin cells, obtained from bovine adrenal medulla, was studied in intact cell suspensions using 7Li NMR spectroscopy with the shift reagent [Tm(HDOTP)]4-. The influx rate constants, ki, were determined in the absence and in the presence of two Na+ membrane transport inhibitors. The values obtained indicate that both voltage sensitive Na+ channels and (Na+/K+)-ATPase play an important role in Li+ uptake by these cells. 7Li NMR T1 and T2 relaxation times for intracellular Li+ in bovine chromaffin cells provided a T1/T2 ratio of 305, showing that Li+ is highly, immobilized due to strong binding to intracellular structures. Using fluorescence spectroscopy and the Mg2+ fluorescent probe, furaptra, the free intracellular Mg2+ concentration in the bovine chromaffin cells incubated with 15 mM LiCl was found to increase by about mM after the intracellular Li+ concentration reached a steady state. Therefore, once inside the cell, Li+ is able to displace Mg2+ from its binding sites.