NDLI: Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators

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Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators

Content Provider	Taylor & Francis Online
Author	Krstić, Danijela Krinulović, Katarina Vasić, Vesna
Abstract	Kinetics and inhibition of Na+/K+-ATPase and Mg2+-ATPase activity from rat synaptic plasma membrane (SPM), by separate and simultaneous exposure to transition (Cu2+, Zn2+, Fe2+ and.Co2+) and heavy metals (Hg2+and Pb2+) ions were studied. All investigated metals produced a larger maximum inhibition of Na+/K+-ATPase than Mg2+-ATPase activity. The free concentrations of the key species (inhibitor, MgATP2 − , MeATP2 − ) in the medium assay were calculated and discussed. Simultaneous exposure to the combinations Cu2+/Fe2+ or Hg2+/Pb2+caused additive inhibition, while Cu2+/Zn2+ or Fe2+/Zn2+ inhibited Na+/K+-ATPase activity synergistically (i.e., greater than the sum metal-induced inhibition assayed separately). Simultaneous exposure to Cu2+/Fe2+ or Cu2+/Zn2+ inhibited Mg2+-ATPase activity synergistically, while Hg2+/Pb2+ or Fe2+/Zn2+ induced antagonistic inhibition of this enzyme. Kinetic analysis showed that all investigated metals inhibited Na+/K+-ATPase activity by reducing the maximum velocities (Vmax) rather than the apparent affinity (Km) for substrate MgATP2-, implying the noncompetitive nature of the inhibition. The incomplete inhibition of Mg2+-ATPase activity by Zn2+, Fe2+ and Co2+ as well as kinetic analysis indicated two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATP2 − concentration. EDTA, L-cysteine and gluthathione (GSH) prevented metal ion-induced inhibition of Na+/K+-ATPase with various potencies. Furthermore, these ligands also reversed Na+/K+-ATPase activity inhibited by transition metals in a concentration-dependent manner, but a recovery effect by any ligand on Hg2+-induced inhibition was not obtained.
Starting Page	469
Ending Page	476
Page Count	8
File Format	PDF HTM / HTML
ISSN	14756366 14756374
DOI	10.1080/14756360500213280
Journal	Journal of Enzyme Inhibition and Medicinal Chemistry
Volume Number	20
Issue Number	5
Language	English
Publisher	Taylor & Francis
Publisher Date	2008-10-04
Access Restriction	Open
Subject Keyword	Transition and heavy metals Na+/K+-ATPase Mg2+-ATPase Kinetics Inhibition
Content Type	Text
Resource Type	Article
Subject	Drug Discovery Medicine Pharmacology

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