Regulation of Membrane Na+-K+ ATPase

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 t...

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Λεπτομέρειες βιβλιογραφικής εγγραφής
Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
Άλλοι συγγραφείς: Chakraborti, Sajal (Επιμελητής έκδοσης), Dhalla, Naranjan S. (Επιμελητής έκδοσης)
Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
Γλώσσα:English
Έκδοση: Cham : Springer International Publishing : Imprint: Springer, 2016.
Σειρά:Advances in Biochemistry in Health and Disease ; 15
Θέματα:
Διαθέσιμο Online:Full Text via HEAL-Link
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245 1 0 |a Regulation of Membrane Na+-K+ ATPase  |h [electronic resource] /  |c edited by Sajal Chakraborti, Naranjan S Dhalla. 
264 1 |a Cham :  |b Springer International Publishing :  |b Imprint: Springer,  |c 2016. 
300 |a XI, 436 p. 100 illus., 44 illus. in color.  |b online resource. 
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490 1 |a Advances in Biochemistry in Health and Disease ;  |v 15 
505 0 |a 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 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 Reference 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. 
520 |a 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. 
650 0 |a Life sciences. 
650 0 |a Molecular biology. 
650 0 |a Proteins. 
650 0 |a Cell membranes. 
650 0 |a Atomic structure. 
650 0 |a Molecular structure. 
650 0 |a Spectra. 
650 1 4 |a Life Sciences. 
650 2 4 |a Protein Structure. 
650 2 4 |a Membrane Biology. 
650 2 4 |a Protein Science. 
650 2 4 |a Atomic/Molecular Structure and Spectra. 
650 2 4 |a Molecular Medicine. 
700 1 |a Chakraborti, Sajal.  |e editor. 
700 1 |a Dhalla, Naranjan S.  |e editor. 
710 2 |a SpringerLink (Online service) 
773 0 |t Springer eBooks 
776 0 8 |i Printed edition:  |z 9783319247489 
830 0 |a Advances in Biochemistry in Health and Disease ;  |v 15 
856 4 0 |u http://dx.doi.org/10.1007/978-3-319-24750-2  |z Full Text via HEAL-Link 
912 |a ZDB-2-SBL 
950 |a Biomedical and Life Sciences (Springer-11642)