Übersicht			Auf mobile öffnen

Lieferstatus:	Auf Bestellung (Lieferzeit unbekannt)
Veröffentlichung:	Dezember 2015
Genre:	Naturwissensch., Medizin, Technik
	Atomic and Molecular Structure and Properties / Atomic structure / Atomic/Molecular Structure and Spectra / B / biochemistry / Biomedical and Life Sciences / Biomedical Research / Cell membranes / Cellular biology (cytology) / Life Sciences / Medical research / Membrane Biology / Membrane Trafficking / molecular biology / Molecular Medicine / Molecular structure / Nuclear physics / Protein Science / Protein Structure / proteins
ISBN:	9783319247489
EAN-Code:	9783319247489
Verlag:	Springer Nature EN
Einband:	Gebunden
Sprache:	English
Serie:	#15 - Advances in Biochemistry in Health and Disease
Dimensionen:	H 235 mm / B 155 mm / D
Gewicht:	7922 gr
Seiten:	436
Illustration:	XI, 436 p. 100 illus., 44 illus. in color., schwarz-weiss Illustrationen, farbige Illustrationen
Bewertung:	Titel bewerten / Meinung schreiben

Inhalt:

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 transmembrane 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.