Regulation of Membrane NaK ATPase

Sajal Chakraborti and Naranjan S. Dhalla, "Regulation of Membrane Na-K ATPase"
English | ISBN: 3319247484 | 2016 | 450 pages | PDF | 15 MB
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 alpha- and ss- subunits. At present four different alpha- (alpha-1,alpha-2,alpha-3 and alpha-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 alpha- 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 alpha-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 "" 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.

Title: Regulation of Membrane NaK ATPase
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