Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives
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The previously reported class of potent inorganic inhibitors of Na,K-ATPase, named MCS factors, was shown to inhibit not only Na,K-ATPase but several P-type ATPases with high potency in the sub-micromolar range. These MCS factors were found to bind to the intracellular side of the Na, K-ATPase. The inhibition is not competitive with ouabain binding, thus excluding its role as cardiac-steroid-like inhibitor of the Na,K-ATPase. The mechanism of inhibition of Na,K-ATPase was investigated with the fluorescent styryl dye RH421, a dye known to report changes of local electric fields in the membrane dielectric. MCS factors interact with the Na,K-ATPase in the E1 conformation of the ion pump and induce a conformational rearrangement that causes a change of the equilibrium dissociation constant for one of the first two intracellular cation binding sites. The MCS-inhibited state was found to have bound one cation (H+, Na+ or K+) in one of the two unspecific binding sites, and at high Na+ concentrations another Na+ ion was bound to the highly Na+-selective ion-binding site.
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STIMAC, Robert, Franz KEREK, Hans-Jürgen APELL, 2005. Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives. In: The Journal of Membrane Biology. 2005, 205(2), pp. 89-101. ISSN 0022-2631. eISSN 1432-1424. Available under: doi: 10.1007/s00232-005-0767-2BibTex
@article{Stimac2005Mecha-8615, year={2005}, doi={10.1007/s00232-005-0767-2}, title={Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives}, number={2}, volume={205}, issn={0022-2631}, journal={The Journal of Membrane Biology}, pages={89--101}, author={Stimac, Robert and Kerek, Franz and Apell, Hans-Jürgen} }
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