Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Larisa A. Vasilets"'
Publikováno v:
Neuroscience. 118:371-378
The genetically epileptic mouse strain (El) is used as a model for human temporal lobe epilepsy. To address the question of whether altered function of the neuronal GABA transporter GAT1 is involved in the pathology of epilepsy of El mice, we express
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1609:55-62
The N-terminus of the Na(+),K(+)-ATPase alpha-subunit shows some homology to that of Shaker-B K(+) channels; the latter has been shown to mediate the N-type channel inactivation in a ball-and-chain mechanism. When the Torpedo Na(+),K(+)-ATPase is exp
Autor:
Christoph Böhmer, Iwan Setiawan, Yuxi Feng, Florian Lang, Wolfgang Schwarz, Larisa A. Vasilets, Guido Henke
Publikováno v:
Pflügers Archiv. 444:426-431
The serum and glucocorticoid-dependent kinase-1 (sgk1) is expressed in a wide variety of tissues including renal epithelial cells. As it is up-regulated by aldosterone, it is considered to participate in the regulation of renal Na(+) reabsorption. In
Publikováno v:
Cell Biochemistry and Biophysics. 37:083-096
The protein kinase C (PKC)-mediated phosphorylation of the Na+/K+-ATPase α-subunit has been shown to play an important role in regulation of the Na+/K+-ATPase activity. In the rat α1-subunit, phosphorylation occurs at Ser-23 and results in inhibiti
Publikováno v:
FEBS Letters. 455:8-12
The Na+/K+-ATPase is a target protein for protein kinase C (PKC). The PKC-mediated phosphorylation of the rat alpha1 subunit at Ser-23 results in the inhibition of its transport function. To understand the molecular basis of the inhibition by PKC, th
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1372:289-300
Tetraethylammonium (TEA+) is an effective inhibitor of a variety of K+ channels, and has been widely used to reduce K+-sensitive background conductances in electrophysiological investigations of the Na+,K+-ATPase. Here we demonstrate by combination o
Autor:
Larisa A. Vasilets
Publikováno v:
Cellular Physiology and Biochemistry. 7:1-18
Protein-kinase-mediated phosphorylation of the Na+/K+-ATPase has been studied in enzymes purified from pig, dog, sheep, and rat kidneys and in Xenopus oocytes.
Autor:
Wolfgang Schwarz, Larisa A. Vasilets
Publikováno v:
Cellular Physiology and Biochemistry. 4:81-95
Major, functionally relevant features of Na+/K+-ATPase are located on the α-subunit of the αβ-heterodimer. They include the binding sites for the transported cations, the binding pocket and phosporylation site for ATP as well as regulatory phospho
Autor:
Wolfgang Schwarz, Larisa A. Vasilets
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes. 1154:201-222
Publikováno v:
The Journal of Membrane Biology. 121:177-187
To investigate the voltage dependence of the Na+/K+ pump, current-voltage relations were determined in prophase-arrested oocytes of Xenopus laevis. All solutions contained 5 mM Ba2+ and 20 mM tetraethylammonium (TEA) to block K+ channels. If, in addi