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Regulation of Membrane Na+-K+ ATPase
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Na+-K+ATPase or Na-pump ATPase, a member of P-type ATPase superfamily, is characterized by association of multiple isoforms mainly of its - and - subunits. At present four different - (-1,-2,-3 and -4) and three - (-1, -2, and -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 - and - 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 commonsignature sequence encompassing the transmembra ne domain adjacent to the isoform(s) of - 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 entitledRegulation of Membrane Na+-K+ATPasefor 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.
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