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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 it's ?- 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 common signature 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 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.