1.

Record Nr.

UNINA9910253874703321

Titolo

Regulation of Membrane Na+-K+ ATPase / / edited by Sajal Chakraborti, Naranjan S Dhalla

Pubbl/distr/stampa

Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016

ISBN

3-319-24750-6

Edizione

[1st ed. 2016.]

Descrizione fisica

1 online resource (434 p.)

Collana

Advances in Biochemistry in Health and Disease, , 2512-2150 ; ; 15

Disciplina

570

Soggetti

Proteins

Biological transport

Cell membranes

Atomic structure 

Molecular structure

Medicine - Research

Biology - Research

Membrane Trafficking

Protein Biochemistry

Atomic and Molecular Structure and Properties

Biomedical Research

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di bibliografia

Includes bibliographical references at the end of each chapters and index.

Nota di contenuto

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.

Sommario/riassunto

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.