|
|
|
|
LEADER |
05653nam a22005535i 4500 |
001 |
978-3-319-24750-2 |
003 |
DE-He213 |
005 |
20170518122442.0 |
007 |
cr nn 008mamaa |
008 |
151215s2016 gw | s |||| 0|eng d |
020 |
|
|
|a 9783319247502
|9 978-3-319-24750-2
|
024 |
7 |
|
|a 10.1007/978-3-319-24750-2
|2 doi
|
040 |
|
|
|d GrThAP
|
050 |
|
4 |
|a QD431-431.7
|
072 |
|
7 |
|a PSBC
|2 bicssc
|
072 |
|
7 |
|a SCI007000
|2 bisacsh
|
082 |
0 |
4 |
|a 572.633
|2 23
|
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.
|
336 |
|
|
|a text
|b txt
|2 rdacontent
|
337 |
|
|
|a computer
|b c
|2 rdamedia
|
338 |
|
|
|a online resource
|b cr
|2 rdacarrier
|
347 |
|
|
|a text file
|b PDF
|2 rda
|
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)
|