Chakraborti / Dhalla Regulation of Membrane Na+-K+ ATPase

1. Auflage 2016
ISBN: 978-3-319-24750-2
Verlag: Springer International Publishing
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 15, 436 Seiten, eBook

Reihe: Advances in Biochemistry in Health and Disease

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 a- and ß- subunits. At present four different a- (a-1,a-2,a-3 and a-4) and three ß- (ß-1, ß-2, and ß-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na + -K +  ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na + -K +  ATPase 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 + -K +  ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of a- and ß- 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 transmembra ne domain adjacent to the isoform(s) of a-ß subunits of Na + -K +  ATPase. 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.

Zielgruppe

Research

Autoren/Hrsg.

Chakraborti, Sajal

Dhalla, Naranjan S

Inhaltsverzeichnis

Part A.- 1 Na+/K+-ATPase: A Perspective.- 2 Na+/K+-ATPase and Its Role in Signal Transduction.- 3 Na+ K+-ATPase Cell Signaling Pathways and Cancer.- 4 Calcium Controls the P2-ATPase Mediated Homeostasis: Essential Role of NaAF.- 5 Na+/K+-ATPase a4: An Isoform Dedicated to Sperm Function.- 6 The Role of the 2nd Na+ Pump in Mammals and Parasites.- 7 Myocardial Na+/K+-ATPase and SERCA: Clinical and Pathological Significance from a Cytological perspective.- 8 Understanding the Dysfunction of Na+/K+-ATPase in Rapid-Onset Dystonia- Parkinsonism and Amyotrophic Lateral Sclerosis.- 9 Activity of Membrane ATPases in Human Erythrocytes Under the Influence ofHighly Hydroxylated Fullerenol.- 10 Xenobiotics-mediated Modulation of ATPases and Biomedical Implications.- 11 Emerging Role of Dysadherin in Metastasis.- 12 The Astrocytic Na+/K+-ATPase - Stimulation by Increased Extracellular K+, ß-Adrenergic Activation, Ouabain-mediated Signaling, and Interaction with the Transporter NKCC1.- 13 Uncoupling of P-type ATPases.- 14 Phospholemman: A Brief Overview.- 15 Regulation of the Cardiac Na+/K+-ATPase by Phospholemman.- 16 Regulation of Brain Na+/K+- ATPase Activity by Noradrenaline with ParticularReference to Normal and Altered Rapid Eye Movement Sleep.- 17 Regulation Na+/K+-ATPase Activity in the Nervous System.- 18 Regulation of Membrane Na+/K+ ATPase in Health and Disease.- 19 Redox Regulation of the Na+/K+ ATPase in the Cardiovascular System.- 20 Regulation of Na+/K+-ATPase in Pulmonary Vasculature.- 21 Exercise-induced Regulation of the Na, K-pump in Skeletal Muscles.- 22 Advances in the Understanding of Renal Proximal Tubular Na+/K+-ATPase Regulation by Parathyroid Hormone and Dopamine.- 23 Regulation of Na+/ K+-ATPase in Epithelial-Mesenchymal Transition and Cancer.- 24 Metal Based Compounds, Modulators of Na+/K+-ATPase with Anticancer Activity.