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Regulation of Membrane Na+-K+ ATPase

  • Sajal Chakraborti
  • Naranjan S Dhalla

Part of the Advances in Biochemistry in Health and Disease book series (ABHD, volume 15)

Table of contents

  1. Front Matter
    Pages i-xi
  2. Functional and Signaling Aspects

    1. Front Matter
      Pages 1-1
    2. Sajal Chakraborti, Sayed Modinur Rahaman, Md Nur Alam, Amritlal Mandal, Biswarup Ghosh, Kuntal Dey et al.
      Pages 3-30
    3. Moumita Banerjee, Zijian Xie
      Pages 31-50
    4. Marco Túlio C. Pessôa, Vanessa F. Cortes, Leandro A. Barbosa
      Pages 51-61
    5. Gladis Sánchez, Gustavo Blanco
      Pages 77-92
    6. Adalberto Vieyra, Paulo A. Silva, Humberto Muzi-Filho, Claudia F. Dick, André L. Araujo-dos-Santos, Juliana Dias et al.
      Pages 93-112
    7. Milica M. Labudović Borović, Milan M. Obradović, Jelena T. Kostić, Ivan V. Zaletel, Dejan G. Milašinović, Marija T. Stojanović et al.
      Pages 113-144
    8. Bechan Sharma, Shweta Singh, Sunil Kumar Jaiswal, Nikhat Jamal Siddiqi
      Pages 173-183
    9. Kuntal Dey, Haim Garty, Sajal Chakraborti
      Pages 185-193
    10. Yasser A. Mahmmoud
      Pages 223-240
  3. Modulatory and Regulatory Aspects

    1. Front Matter
      Pages 241-241
    2. Sajal Chakraborti, Kuntal Dey, Md Nur Alam, Amritlal Mandal, Jaganmay Sarkar, Tapati Chakraborti
      Pages 243-259
    3. Hansraj Dhayan, Rajender Kumar, Andreas Kukol
      Pages 261-276
    4. Vijayan Elimban, Monika Bartekova, Yan-Jun Xu, Naranjan S. Dhalla
      Pages 311-322
    5. Keyvan Karimi Galougahi, Gemma A. Figtree
      Pages 323-338
    6. Thakur Uttam Singh, Subhashree Parida, Santosh Kumar Mishra
      Pages 339-348
    7. Tatjana G. Momić, Mirjana B. Čolović, Tamara D. Lazarević-Pašti, Vesna M. Vasić
      Pages 389-425
  4. Back Matter
    Pages 427-436

About this book

Introduction

Na+-KATPase 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. Regulation of Na+-KATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-KATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-KATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of α- and β- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembrane domain adjacent to the isoform(s) of α-β subunits of Na+-KATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled “Regulation of Membrane Na+-K+ ATPase” for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease.

Keywords

Membrane Na+-K+ ATPase Cardiac Na+-K+ ATPase Na+/K+-ATPase inhibitors Na+-coupled cotransport Na+-K+ pump

Editors and affiliations

  • Sajal Chakraborti
    • 1
  • Naranjan S Dhalla
    • 2
  1. 1.Biochemistry and BiophysicsUniversity of KalyaniKalyaniIndia
  2. 2.University of ManitobaInstitute of Cardiovascular Science St. Boniface Hospital ResearchWinnipegCanada

Bibliographic information

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