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The Sodium Pump

Structure Mechanism, Hormonal Control and its Role in Disease

  • Book
  • © 1994

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Editors:
  1. Ernst Bamberg

    1. Max-Planck-Institut für Biophysik, Frankfurt, Germany

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  2. Wilhelm Schoner

    1. Institut für Biochemie, Universität Gießen, Gießen, Germany

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Table of contents (167 chapters)

  1. Front Matter

    Pages I-XIX
    Download chapter PDF

  2. Gene organization, analysis of the sodium pump by molecular biology

    1. Transcription factors regulating the Na+/K+-ATPase genes

      • K. Kawakami, Y. Suzuki-Yagawa, Y. Watanabe, K. Ikeda, K. Nagano
      Pages 1-10

    2. Expression of Functional Na+/K+-ATPase in Yeast

      • Robert A. Farley, Kurt A. Eakle, Georgios Scheiner-Bobis, Kena Wang
      Pages 11-20

    3. Expression of Functional Na+/K+-ATPase in Insect Cells Using Baculovirus

      • R. W. Mercer, G. Blanco, A. W. De Tomaso, J. C. Koster, Z. J. Xie
      Pages 21-32

    4. Sp1 and an E-Box Binding Protein Regulate Na+/K+-ATPase α2-Subunit Gene

      • K. Ikeda, K. Nagano, K. Kawakami
      Pages 33-36

    5. Cloning and Analysis of the 5’-Flanking Region of the Rabbit Na+/K+-ATPase α2 Subunit Gene

      • Trine Kjærsig, Peter L. Jørgensen, Li-Mei Meng
      Pages 37-40

    6. Positive and Negative Transcriptional Elements in the Chicken Na+/K+-ATPase α1-Subunit Gene

      • Hui-Ying Yu, Kunio Takeyasu
      Pages 41-44

    7. Transcriptional Regulation of Na+/K+-ATPase α1 Gene Expression by 8-Bromo-Cyclic AMP in Renal Cells

      • M. Ahmad, L. Olliff, N. Weisberg, R. M. Medford
      Pages 45-48

    8. Cloning of the Dog Na+/K+-ATPase α1-Subunit

      • Z. J. Xie, H. Li, Q. Liu, Y. Wang, A. Askari, R. W. Mercer
      Pages 49-52

    9. Cloning and Characterization of a New Member of the Family of Na+/K+-ATPase Genes

      • Karl Lücking, Peter L. Jørgensen, Li-Mei Meng
      Pages 53-56

    10. The Cloning of Homologous Na+/K+-ATPase Genes from New Species

      • C. P. Cutler, I. L. Sanders, G. A. Luke, N. Hazon, G. Cramb
      Pages 57-60

    11. Functional expression of the gastric H,K-ATPase in Xenopus oocytes

      • P. M. Mathews, D. Claeys, F. Jaisser, K. Geering, J.-P. Kraehenbuhl, B. C. Rossier
      Pages 61-65

    12. Over-expression of the peptide containing the ATP-binding site in Na/K-ATPase α-subunit

      • T. Ohta, M. Kuroda, M. Yoshii, H. Hayashi
      Pages 66-69

    13. Expression of Na+,K+-ATPase in Saccharomyces cerevisiae

      • Per Amstrup Pedersen, Vibeke Foersom, Peter Leth Jørgensen
      Pages 70-73

    14. Regulation of Na+/K+-ATPase α1 and ß1 Expression in Epithelial Cells

      • K. K. Grindstaff, G. Blanco, R. W. Mercer
      Pages 74-77

    15. The α-Subunit of the Na+/K+-ATPase has Catalytic Activity Independent of the ß-subunit

      • G. Blanco, A. W. De Tomaso, J. C. Koster, Z. J. Xie, R. W. Mercer
      Pages 78-81

    16. Functional Expression of Na+/K+-ATPase α and β Isoforms

      • G. Blanco, Z. J. Xie, R. W. Mercer
      Pages 82-85

    17. Ca2+/Calmodulin-Sensitive Na+/K+-ATPase Activity Expressed in Chimeric Molecules between the Plasma Membrane Ca2+-ATPase and the Na+/K+-ATPase α-Subunit

      • Toshiaki Ishii, Kunio Takeyasu
      Pages 86-89

    18. Expression of Na+/K+-ATPase and H+/K+-ATPase fusion proteins in Sf-9 insect cells

      • J. C. Koster, M. A. Reuben, G. Sachs, R. W. Mercer
      Pages 90-93

    19. In Vitro Synthesis of H+/K+-ATPase Polypeptides in Insect Cells Using the Baculovirus Expression System

      • C. H. W. Klaassen, M. P. De Moel, H. G. P. Swarts, J. J. H. H. M. De Pont
      Pages 94-97
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Keywords

About this book

The sodium of animal cell membranes converts the chemical energy obtained from the hydrolysis of adenosine 5' -triphosphate into a movement of the cations Na + and K + against an electrochemical gradient. The gradient is used subse­ quently as an energy source to drive the uptake of metabolic substrates in polar epithelial cells and to use it for purposes of communications in excitable cells. The biological importance of the sodium pump is evident from the fact that be­ tween 20-70% of the cell's metabolic energy is consumed for the pumping pro­ cess. Moreover, the sodium pump is an important biological system involved in regulatory processes like the maintenance of the cells' and organism's water me­ tabolism. It is therefore understandable that special cellular demands are han­ dled better by special isoforms of the sodium pump, that the expression of the sodium pump and their isoforms is regulated by hormones as is the activity of the sodium pump via hormone-regulated protein kinases. Additionally, the sodium pump itself seems to be a receptor for a putative new group of hormones, the endogenous digitalis-like substances, which still have to be defined in most cases in their structure. This group of substances has its chemically well known coun­ terpart in steroids from plant and toad origin which are generally known as "car­ diac glycosides". They are in medical use since at least 200 years in medicine in the treatment of heart diseases.

Editors and Affiliations

  • Max-Planck-Institut für Biophysik, Frankfurt, Germany

    Ernst Bamberg

  • Institut für Biochemie, Universität Gießen, Gießen, Germany

    Wilhelm Schoner

Bibliographic Information

  • Book Title: The Sodium Pump

  • Book Subtitle: Structure Mechanism, Hormonal Control and its Role in Disease

  • Editors: Ernst Bamberg, Wilhelm Schoner

  • DOI: https://doi.org/10.1007/978-3-642-72511-1

  • Publisher: Steinkopff Heidelberg

  • eBook Packages: Springer Book Archive

  • Copyright Information: Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994

  • Softcover ISBN: 978-3-642-72513-5Published: 14 February 2012

  • eBook ISBN: 978-3-642-72511-1Published: 06 December 2012

  • Edition Number: 1

  • Number of Pages: XX, 906

  • Topics: Human Physiology, Biochemistry, general, Cardiology

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