Details

Regulation of Membrane Na+-K+ ATPase

Advances in Biochemistry in Health and Disease, Band 15

von: Sajal Chakraborti, Naranjan S Dhalla
CHF 177.00
Verlag:	Springer
Format:	PDF
Veröffentl.:	16.12.2015
ISBN/EAN:	9783319247502
Sprache:	englisch

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Beschreibungen

Titelbeschreibung

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. 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 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+-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.

Inhaltsverzeichnis

<div>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 α4: 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 of</div><div>Highly 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+, β-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 Particular</div><div>Reference to Normal and Altered Rapid Eye </div>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.</div>

Back cover copy

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. 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 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+-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.

Sonderbeitrag

A comprehensive investigation into the ATPase regulation of Membrane Na+-K+ ATPase Explores the specific inhibitors and molecular probes for membrane ATPases to improve the therapy of various diseases An informative resource to improve diverse ATPase therapeutic approaches of life threatening diseases