Expression of functional (Na++ K+)-ATPase from cloned cDNAs
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O-13: Na+/K+-ATPase Alpha1 Isoform Mediates Ouabain-Induced Expression of Cyclin D1 and Proliferation of Rat Sertoli Cells
Background: Novel roles for the interaction of cardiotonic steroids to Na+/K+-ATPase have been established in recent years. The aim of the present study was to investigate the intracellular signaling events downstream the action of ouabain on Na+/K+-ATPase in Sertoli cell obtained from immature rats. Treatment of Sertoli cells with ouabain (1 μM) induced a rapid and transient increase in the ex...
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متن کاملSpecialized Functional Diversity and Interactions of the Na,K-ATPase
Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions with molecular environment. Studies over the last decades clearly demonstrated complex and isofo...
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Associated proteins are important for the correct functioning of nicotinic acetylcholine receptors (nAChRs). In the present study, a neonicotinoid-agarose affinity column was used to isolate related proteins from a solubilized membrane preparation from the nervous system of Locusta migratoria manilensis (Meyen). 1530 peptides were identified and most of them were involved in the membranous stru...
متن کاملMolecular activity of Na+/K+-ATPase
species in a predictable manner. For example, it is several-fold greater in endothermic than in ectothermic vertebrate species when measured at the same body temperature. This difference in metabolic activity appears to be primarily a cellular phenomenon, and it has recently been proposed that it is related to differences in membrane composition (Hulbert and Else, 1999, 2000). A substantial pro...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1987
ISSN: 0014-5793
DOI: 10.1016/0014-5793(87)81125-0