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Tuesday, July 21, 2020 | History

2 edition of Na,K-ATPase found in the catalog.

Na,K-ATPase

Jean-Daniel Horisberger

Na,K-ATPase

structure-function relationship

by Jean-Daniel Horisberger

  • 379 Want to read
  • 18 Currently reading

Published by R.G. Landes, CRC Press [distributor] in Austin, Boca Raton, FL .
Written in English

    Subjects:
  • Sodium/potassium ATPase.

  • Edition Notes

    Includes bibliographical references and index.

    StatementJean-Daniel Horisberger.
    SeriesMolecular biology intelligence unit, Molecular biology intelligence unit (Unnumbered)
    Classifications
    LC ClassificationsQP609.S63 H67 1994
    The Physical Object
    Paginationvii, 130 p. :
    Number of Pages130
    ID Numbers
    Open LibraryOL1079571M
    ISBN 101570590303
    LC Control Number94002908

      The MCAT wants you to know that it is the action of the Na+/K+ ATPase Pump and the K+ Leak (slow) channels that maintain the RMP (resting membrane potential). When K+ leaks out (down its gradient), the cell becomes less positive on the inside.   The Na⁺/K⁺-ATPase is The Membrane Aldosterone Receptor, and it works independently of ATP. This is highlighted by Dostanic-Larson when she states: "The α1 isoform was converted to a high affinity subunit by introducing RL and DN amino acid substitutions, which enhanced binding of cardiac glycosides ≈fold without altering.

    Using the cut-off value of Na +,K + -ATPase and dynein ATPase, we found that the low level Na +,K + -ATPase and dynein ATPase correlated with the low embryo development quality (p, respectively).Author: Silvia W. Lestari, Aucky Hinting, Hamdani Lunardi, Debby Aditya, Dessy Noor Miati, Meidika Dara Rizk. The sensitivity of Na/K-ATPase to MBG was enhanced at the level of high-affinity binding sites (IC 50, vs nmol/L, PCited by:

    This article contains a translation of Na+/K+-ATPase from dia. Book Reviews; Editorials; MBoC 20th Anniversary Favorites; MBoC Perspectives on Cell Biology and Human Health; MBoC Technical Perspectives; Meeting Reviews; Obituaries; Perspectives and Essays; Resources; Retrospectives; MBoC Career Perspectives; Collections. Selected MBoC Articles on Stem Cells; ASCB Resources. ASCB Career Resources; CBE.


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Na,K-ATPase by Jean-Daniel Horisberger Download PDF EPUB FB2

Scott J. Schurman, Steven J. Scheinman, in Genetics of Bone Biology and Skeletal Disease (Second Edition), Role of Kir in Kidney. In the DCT, basolateral Na + /K +-ATPase transports sodium to the interstitium and potassium to the intracellular compartment against chemical teral potassium channels recycle potassium to the interstitium.

S.M. Lamothe, S. Zhang, in Progress in Molecular Biology and Translational Science, Na + /K + ATPase. Na + /K + ATPase (sodium-potassium adenosine triphosphatase), also known as the sodium potassium pump (Na + /K + pump) is a plasma membrane transporter.

It transports sodium out of the cell and potassium into the cell against their concentration gradients. The Na+ K+ pump is an electrogenic transmembrane ATPase first discovered in and situated in the outer plasma membrane of the cells; on the cytosolic side.[1][2] The Na+ K+ ATPase pumps 3 Na+ out of the cell and 2K+ that into the cell, for every single ATP consumed.

The plasma membrane is a lipid bilayer that arranged asymmetrically, containing cholesterol, Author: Yasaman Pirahanchi, Narothama R.

Aeddula. Na+,K+-ATPase is an ATP-powered ion pump that establishes concentration gradients for Na+ and K+ ions across the plasma membrane in all animal cells by pumping Na+ from the cytoplasm and K+ from the extracellular medium. This heterodimeric enzyme, a member of P-type ATPases, is composed of a catalytic α-subunit with ten transmembrane domains and a heavily Cited by: 1.

Na +-K + ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s α- and β- subunits.

At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Na/K-ATPase inhibition and CTS-regulated natriuresis.

The Na/K-ATPase was discovered in by Jens Skou through his studies on crab nerves, and is a member of the P-type ATPase family responsible for the exchange of Na and K ions across cell membranes via the hydyolysis of ATP [].Its structure and function has since been extensively by: 1.

Na + /K +-ATPase is an enzyme found in the plasma is sodium-potassium adenosine triphosphatase, also known as the 'Na + /K + pump', 'sodium-potassium pump', or simply 'sodium pump', for short.

It was first discovered by Jens Christian Skou who won a Nobel Prize in Chemistry in The enzyme moves Na + ions out of the cell and replaces them. The β subunit of Na +,K +-ATPase is required for assembly and delivery to the plasma membrane of [16,17], and thus availability of β subunits is a critical determinant of the cell's capacity to maintain low intracellular Na + under a wide range of conditions [7,34].Cited by:   Introduction.

The Na + /K +-ATPase maintains Na + and K + gradients across the plasma membrane, which are crucial for various cell functions such as regulation of cell volume, pH, Na +-coupled secondary transport of molecules and neurotransmitters, maintenance of the resting membrane potential (RMP) of most cells, and the excitability of muscle and neuronal Cited by:   Abstract.

The Na + /K +-ATPase (also known as the “sodium–potassium pump” or just “sodium pump”) is a ubiquitous and critically important protein complex in the human the brain, between 40 and 70% of all energy is spent maintaining its ionic transport activity [1,2,3]. This energy is used for the active exchange of cytosolic sodium for extracellular potassium in a Cited by: 9.

We propose that the activation of ERK, AKT, and NFκB, resulting from ECS-Na +, K +-ATPase interaction, modifies neuronal activity and neurotransmission which, in turn, participate in the regulation of behavior and BD. These observations suggest Na +, K +-ATPase-mediated signaling is a potential target for drug development for the treatment of by: 6.

Book August The cellular energy is generated essentially by a complex molecu lar machine located at its periphery: the Na,K-ATPase system (NKA), called also sodium pump. It includes a proposal that Na/K-ATPase plays a role as a tranducer of signal transduction, and, amongst other topics, covers the oligomericity of the enzyme, the site directed mutagenesis of P-type ATPases and the role of g-subunit.

The book will serve as an important resouce, not only for work on Na/K-ATPase, but also for the investigation of. The Na +, K + -ATPase generates and maintains the cell membrane potential and the inward Na + gradient thus generated is utilized by other Na + dependent transport systems for uptake of.

Na, K-ATPase, structure and kinetics: proceedings of the 2nd International Conference on the Properties and Functions of Na, K-ATPase, held at Sandbjerg Castle, Sønderborg, Denmark, Septemberby K-ATPase International Conference on the Properties and Functions of Na (Book).

Cardiac glycosides (CGs) are selective inhibitors of sodium-potassium adenosine triphosphatase (Na + /K +-ATPase or Na + /K +-pump or NKA) s of the cardiac glycoside family share a similar Cited by: 3.

- [Voiceover] What I hope to do in this video is give ourselves an appreciation for the sodium-potassium pump, and as the name implies, it pumps sodium and potassium, but it does it in different directions. So this little depiction right over here, this is my drawing, my rendition of the sodium-potassium pump, it's a trans-membrane, I guess you.

Because Na + /K + ATPase is the primary transporter maintaining the electrochemical gradient for Na + across syncytiotrophoblast plasma membranes, the decreased Na + /K + ATPase activity in MVM in association with IUGR may impair placental nutrient uptake and proton elimination.

As a consequence, these changes could indirectly affect nutrient Cited by: In recent years, Na/K-ATPase signaling has been implicated in different physiological and pathophysiological conditions, including cardiac hypertrophy and uremic cardiomyopathy.

Cardiotonic steroids (CTS), specific ligands of Na/K-ATPase, regulate its enzymatic activity (at higher concentrations) and signaling function (at lower concentrations without significantly Author: Jiang Liu, Ying Nie, Muhammad Chaudhry, Fang Bai, Justin Chuang, Komal Sodhi, Joseph I.

Shapiro. During hypoxia, ROS activate PKCζ, which in turn phosphorylates Na,K-ATPase α 1 subunit at Ser, leading to the endocytosis of Na,K-ATPase from the plasma membrane.

The endocytosis of Na,K-ATPase results in decreased Na,K-ATPase activity and can be prevented by : Guofei Zhou, Laura A. Dada, Jacob I.

Sznajder. The Na+/K+-ATPase (NKA) is a P-type ATPase originally discovered by Skou [1] and responsible for the export of three sodium ions to the outside of the cell and the import of two potassium ions. This ion transport against the concentration gradient is driven by the hydrolysis of ATP. The ion gradient established by NKA is essential.Previous studies provide evidence for a genetic component for susceptibility to bipolar affective disorder (BPAD) in the old-order Amish population.

El-Mallakh and Wyatt [ Biol Psychiatry ] have suggested that the Na(+),K(+)-ATPase may be a candidate gene for BPAD. This study examines the relationship between BPAD in the old-order Amish cohort and the Na(+),K(+) Cited by: 9.Na +,K +-ATPase is affected by changes in intracellular calcium.

It is also sensitive to ouabain and inhibited by vanadate, and (in vitro) by SPAI-1, a peptide isolated from porcine duodenum. It has been reported to be regulated by phosphorylation by protein kinase A (PKA).