Article
Plant Sciences
Magda F. El-Adl, Taha M. El-Katony, Reham M. Nada
Summary: The study found that the specific ion effects of Na+ and K+ were different on the growth of Ulva lactuca. Ulva lactuca showed better growth with high concentrations of NaCl, while KCl might have adverse effects on photosynthesis and cell wall. Transcription of PM H+-ATPase was induced specifically by high concentrations of Na+, while the induction of PM-Na+/K+-ATPase-like alone could not improve the growth of KCl-treated Ulva lactuca.
PLANT PHYSIOLOGY AND BIOCHEMISTRY
(2021)
Article
Multidisciplinary Sciences
Ryuta Kanai, Flemming Cornelius, Bente Vilsen, Chikashi Toyoshima
Summary: Cryo-electron microscopy was used to study the structure of Na+, K+-ATPase and its variations. The results showed that different reaction states exhibited different biochemical characteristics, and the presence of Mg2+ ions in the transmembrane cation binding sites played a crucial role in the reactions. The binding mechanism of the new-generation cardiotonic steroids (CTSs) did not significantly affect the structure of NKA, and the phospholipid molecules were better resolved in the electron microscopy maps compared to X-ray structures.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Biochemistry & Molecular Biology
Santiago E. Faraj, Wanda M. Valsecchi, Mariela Ferreira-Gomes, Mercedes Centeno, Elina Malen Saint Martin, Natalya U. Fedosova, Juan Pablo FC. Rossi, Monica R. Montes, Rolando C. Rossi
Summary: The Na+/K+-ATPase is a plasma membrane glycoprotein that exchanges intracellular Na+ for extracellular K+ by hydrolyzing ATP. The asymmetric distribution of Na+ and K+ is essential for cellular life. Current research indicates that Na+ becomes spontaneously occluded in the E1 dephosphorylated form of the Na+/K+-ATPase, showing positive interactions between binding sites. Adding ATP does not increase Na+ occlusion.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2023)
Article
Multidisciplinary Sciences
Ryuta Kanai, Flemming Cornelius, Haruo Ogawa, Kanna Motoyama, Bente Vilsen, Chikashi Toyoshima
Summary: The sodium pump (Na+, K+-ATPase, NKA) is crucial for maintaining ion gradients across cell membranes, with cardiotonic steroids (CTSs) acting as specific inhibitors. Different structural features of CTSs result in diverse inhibitory properties, with crystal structures providing insights into their mechanism of action and potential for isoform specific targeting.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Multidisciplinary Sciences
Victoria C. Young, Hanayo Nakanishi, Dylan J. Meyer, Tomohiro Nishizawa, Atsunori Oshima, Pablo Artigas, Kazuhiro Abe
Summary: This study investigates ion transport mechanisms by introducing mutations to convert an electroneutral proton/potassium pump into a prototypical electrogenic sodium/potassium pump, explaining their selectivity and phosphorylation mechanisms.
NATURE COMMUNICATIONS
(2022)
Article
Biochemistry & Molecular Biology
Shreya T. Mukherji, Luca Brambilla, Kailey B. Stuart, Isabella Mayes, Laura C. Kutz, Yiliang Chen, Leandro A. Barbosa, Ibrahim Elmadbouh, Jeff P. McDermott, Steven T. Haller, Michael F. Romero, Manoocher Soleimani, Jiang Liu, Joseph I. Shapiro, Gustavo V. Blanco, Zijian Xie, Sandrine V. Pierre
Summary: Through ATP-dependent ion pumping, basolateral Na/K-ATPase (NKA) generates a Na+ gradient that drives apical Na+ reabsorption in the renal proximal tubule (RPT), while NKA signaling function triggers cellular redistribution and decreases Na+ reabsorption. Knockdown of RPT NKA leads to increased membrane NHE3 and NBCe1A, resulting in decreased urine output and Na+ excretion, elevated blood pressure, and increased RPT Na+ reabsorption. NKA signaling plays an important role in regulating Na+ reabsorption in RPT, functioning dominantly over NKA ion pumping.
Article
Chemistry, Applied
Yan-ping Li, Xue-hua Zhang, Fei Lu, Zhuang-Li Kang
Summary: The study found that substituting sodium bicarbonate for sodium chloride led to an increase in pH and the absolute values of Zeta potential, active sulfhydryl, and surface hydrophobicity of myofibrillar protein solution, while decreasing turbidity, particle size, and Ca2+-ATPase activity. Additionally, Mg(2+)ATPase activity was not significantly affected by sodium bicarbonate, implying that it does not impact actin, but may induce protein denaturation.
Article
Cell Biology
Samantha Edenfield, Abigail M. Sims, Constance Porretta, Harry J. Gould, Dennis Paul
Summary: This study demonstrated that the expression of VGSCs doubles during the preparation phase of cell division, while the expression of Na+,K+-ATPase only increases by 1.5 times. This finding has important implications for understanding the role of sodium in cell cycle control and the variability of treatments targeting these components of the Na+ handling system.
Review
Cell Biology
Kelath Murali Manoj, Daniel A. A. Gideon, Nikolai M. M. Bazhin, Hirohisa Tamagawa, Vijay Nirusimhan, Mahendra Kavdia, Laurent Jaeken
Summary: The redox metabolic paradigm emphasizes the importance of diffusible reactive species (DRS), particularly oxygen-centric radicals, in physiology. This article focuses on the membrane protein Na,K-ATPase (NKA) and its role in neuro-cardio-musculo electrophysiology. Through analyzing diffusion, NKA's structural features, ion transport mechanisms, and inhibitory effects of various substances, a minimalist murburn model is proposed to explain the physiological inhibitory effects of different substances on cells.
JOURNAL OF CELLULAR PHYSIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Sofia Ygberg, Evgeny E. Akkuratov, Rebecca J. Howard, Fulya Taylan, Daniel C. Jans, Dhani R. Mahato, Adriana Katz, Paula F. Kinoshita, Benjamin Portal, Inger Nennesmo, Maria Lindskog, Steven J. D. Karlish, Magnus Andersson, Anna Lindstrand, Hjalmar Brismar, Anita Aperia
Summary: The Trp931Arg mutation of the Na+,K+-ATPase catalytic alpha 1 subunit described in this study led to reduced membrane expression of the mutant protein, loss of ion pumping activity, and formation of water-filled pores in the plasma membrane. This resulted in depolarization of neurons, a lowered threshold for epileptic seizures, and destabilization of the ion-binding sites. These findings suggest that Na+,K+-ATPase plays a significant role in diseases associated with epilepsy and loss of plasma membrane integrity.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Article
Cell Biology
Wei Chen, Lei Wang, Pengfei Liang, Jason Mast, Clausell Mathis, Catherine Y. Liu, Jin Wei, Jie Zhang, Liying Fu, Luis A. Juncos, Jacentha Buggs, Ruisheng Liu
Summary: This study demonstrates the potential therapeutic effect of using a synchronization modulation electric field to activate Na/K pumps and maintain cellular functions during renal ischemia-reperfusion injury.
SCIENCE TRANSLATIONAL MEDICINE
(2022)
Article
Plant Sciences
Qi Chen, Kai Xu, Yan Xu, Dehua Ji, Changsheng Chen, Chaotian Xie, Wenlei Wang
Summary: This study analyzed the function of Na+/K+-ATPase in the response of Neoporphyra haitanensis to salt stress and found that it played a crucial role in maintaining the K+/Na+ homeostasis in the algae. The inhibitor ouabain caused Na+ accumulation and K+ leakage in the cells, disrupting the K+/Na+ balance and leading to decreased photosynthesis and oxidative damage in the algae.
FRONTIERS IN PLANT SCIENCE
(2023)
Article
Biochemistry & Molecular Biology
Marlene U. Fruergaard, Ingrid Dach, Jacob L. Andersen, Mette Ozol, Azadeh Shahsavar, Esben M. Quistgaard, Hanne Poulsen, Natalya U. Fedosova, Poul Nissen
Summary: In this study, the crystal structure and functional properties of the E2-BeFx complex of pig kidney Na+,K+-ATPase are investigated. The complex resembles the E2P intermediate and is able to bind ADP/ATP and Na+. The results suggest a relation between E2-BeFx and the E*P intermediate in the functional cycle of Na+, K+-ATPase.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Ryuta Kanai, Bente Vilsen, Flemming Cornelius, Chikashi Toyoshima
Summary: Na+,K+-ATPase (NKA) plays a crucial role in establishing electrochemical gradients for Na+ and K+ across the cell membrane. This study presents two crystal structures of NKA in different states, providing insight into its reaction cycle and functional roles. The findings demonstrate how NKA converts between different forms and utilizes the lipid bilayer for gating the ion pathway.
Article
Biochemistry & Molecular Biology
Ryuta Kanai, Flemming Cornelius, Bente Vilsen, Chikashi Toyoshima
Summary: In this study, the 3.3 angstrom resolution structure of Na+,K+-ATPase (NKA) in the E2·2K(+) state was resolved using cryo-electron microscopy. The transition from the E2P state to the E2·2K(+) state involves the closure and locking of the extracellular ion pathway, as well as events at the phosphorylation site over 50 angstrom away. Furthermore, the binding of ATP to NKA in the E2·2K(+) state was found to relax the gating machinery and greatly accelerate the release of K+ into the cytoplasm.