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DIFFERENTIAL EFFECTS OF OUABAIN ON NA⁺,K⁺-ATPASE FUNCTION: A KINETIC AND ACTIVITY STUDY
Eka Nozadzeand 8 co-authors
Ivane Beritashvili Center of Experimental Biomedicine
FENS Forum 2026 (2026)
Barcelona, Spain
Board PS06-09PM-248
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Date TBA
Board: PS06-09PM-248
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Poster Board
PS06-09PM-248
Poster
View posterAbstract
Differential Effects of Ouabain on Na⁺,K⁺-ATPase Function: A Kinetic and Activity Study
E. Nozadze1, L. Shioshvili1, N. Arutinova1, M. Leladze1, S. Dzneladze1,2, M. Javakhishvili1, L. Tsakadze1, N. Metreveli1, G. Chkadua1,2
1Ivane Beritashvili Center of Experimental Biomedicine, Membranology, Tbilisi, Georgia.
2Georgian National University, Tbilisi, Georgia.
Keywords: Na,K-ATPase, enzyme kinetics, ouabain
The Na⁺,K⁺-ATPase is a ubiquitous membrane enzyme that plays a fundamental role in maintaining ionic gradients across the plasma membrane, thereby regulating cellular excitability, osmotic balance, and secondary active transport. Beyond its classical pumping function, Na⁺,K⁺-ATPase also acts as a signaling molecule, interacting with intracellular pathways that influence cell survival, metabolism, and gene expression. Ouabain, a specific ligand of Na⁺,K⁺-ATPase, has been shown to exert dual effects on the enzyme: at pharmacological concentrations it inhibits ion transport, whereas at low physiological concentrations it activates signaling cascades without complete pump inhibition.
In the present study, we investigated the effects of different physiological and pharmacological concentrations of ouabain on Na⁺,K⁺-ATPase activity. We analyzed how ouabain modulates enzyme kinetics and functional activity, with particular attention to concentration-dependent regulatory mechanisms. Our findings provide further insight into the complex role of ouabain as both an inhibitor and a regulator of Na⁺,K⁺-ATPase function.
This work was supported by the Shota Rustaveli National Science Foundation of Georgia (Project No FR-24-940)
E. Nozadze1, L. Shioshvili1, N. Arutinova1, M. Leladze1, S. Dzneladze1,2, M. Javakhishvili1, L. Tsakadze1, N. Metreveli1, G. Chkadua1,2
1Ivane Beritashvili Center of Experimental Biomedicine, Membranology, Tbilisi, Georgia.
2Georgian National University, Tbilisi, Georgia.
Keywords: Na,K-ATPase, enzyme kinetics, ouabain
The Na⁺,K⁺-ATPase is a ubiquitous membrane enzyme that plays a fundamental role in maintaining ionic gradients across the plasma membrane, thereby regulating cellular excitability, osmotic balance, and secondary active transport. Beyond its classical pumping function, Na⁺,K⁺-ATPase also acts as a signaling molecule, interacting with intracellular pathways that influence cell survival, metabolism, and gene expression. Ouabain, a specific ligand of Na⁺,K⁺-ATPase, has been shown to exert dual effects on the enzyme: at pharmacological concentrations it inhibits ion transport, whereas at low physiological concentrations it activates signaling cascades without complete pump inhibition.
In the present study, we investigated the effects of different physiological and pharmacological concentrations of ouabain on Na⁺,K⁺-ATPase activity. We analyzed how ouabain modulates enzyme kinetics and functional activity, with particular attention to concentration-dependent regulatory mechanisms. Our findings provide further insight into the complex role of ouabain as both an inhibitor and a regulator of Na⁺,K⁺-ATPase function.
This work was supported by the Shota Rustaveli National Science Foundation of Georgia (Project No FR-24-940)
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