Search Results - "VASILETS, L. A"

Phosphorylation of Na,K-ATPase alpha-subunits in microsomes and in homogenates of Xenopus oocytes resulting from the stimulation of protein kinase A and protein kinase C by CHIBALIN, A. V, VASILETS, L. A, HENNEKES, H, PRALONG, D, GEERING, K

“…The phosphorylation of the alpha-subunit of Na+/K(+)-transporting ATPase (Na,K-ATPase) by cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was…”
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Down-regulation of GABA-transporter function by hippocampal translation products: its possible role in epilepsy by Fueta, Y, Vasilets, L A, Takeda, K, Kawamura, M, Schwarz, W

“…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…”
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A negative slope in the current-voltage relationship of the Na+/K+ pump in Xenopus oocytes produced by reduction of external [K+] by RAKOWSKI, R. F, VASILETS, L. A, LATONA, J, SCHWARZ, W

“…To investigate the voltage dependence of the Na+/K+ pump, current-voltage relations were determined in prophase-arrested oocytes of Xenopus laevis. All…”
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Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K+-ATPase in oocytes of Xenopus laevis by VASILETS, L. A, SCHMALZING, G, MÄDEFESSEL, K, HAASE, W, SCHWARZ, W

“…Full-grown prophase-arrested oocytes of Xenopus laevis were treated with 50 nM phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C, or with…”
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Stimulation of the Na+/K+ pump by external [K+] is regulated by voltage-dependent gating by VASILETS, L. A, OMAY, H. S, OHTA, T, NOGUCHI, S, KAWAMURA, M, SCHWARZ, W

“…Wild-type and mutants with alpha-subunits truncated at the N terminus of Na+/K+ pumps of Torpedo electroplax were expressed in Xenopus oocytes by injection of…”
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RNA from heart of young and old rats leads to the expression of protein(s) in Xenopus oocytes that alter the transport activity of rat Na+,K+-ATPases differently by Vasilets, L A, Darmer, D, Isenberg, G, Schwarz, W

“…To address the question of whether the function of Na+,K+-ATPases differs in the heart of young and old rats, enzymes formed from the alpha1 or alpha2 isoform…”
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Regulation of endogenous and expressed Na+/K+ pumps in Xenopus oocytes by membrane potential and stimulation of protein kinases by VASILETS, L. A, SCHWARZ, W

“…Modulation of the current generated by the Na+/K+ pump by membrane potential and protein kinases was investigated in oocytes of Xenopus laevis. In addition to…”
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Phosphorylation of the Na,K-ATPase by Ca, phospholipid-dependent and cAMP-dependent protein kinases. Mapping of the region phosphorylated by Ca, phospholipid-dependent protein kinase by CHIBALIN, A. V, LOPINA, O. D, PETUKHOV, S. P, VASILETS, L. A

“…Ca,phospholipid-dependent (PKC) and cAMP-dependent (PKA) protein kinases phosphorylate the alpha-subunit of the Na,K-ATPase from duck salt gland with the…”
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Voltage-dependent inhibition of the sodium pump by external sodium : species differences and possible role of the N-terminus of the α-subunit by VASILETS, L. A, OHTA, T, NOGUCHI, S, KAWAMURA, M, SCHWARZ, W

“…Currents generated by the Na+/K+ ATPase were measured under voltage clamp in oocytes of Xenopus laevis. The dependence of pump current on external [Na+] was…”
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Structure-function relationships of cation binding in the Na+/K(+)-ATPase by Vasilets, L A, Schwarz, W

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Extracellular pH modulates kinetics of the Na+,K+-ATPase by Salonikidis, Petrus S., Kirichenko, Svetlana N., Tatjanenko, Lilia V., Schwarz, Wolfgang, Vasilets, Larisa A.

“…To investigate effects of pH on the Na+,K+-ATPase, we used the Xenopus oocytes to measure transient charge movements in the absence of extracellular K+, and…”
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Voltage-dependent inhibition of the Na +,K + pump by tetraethylammonium by Eckstein-Ludwig, Ursula, Rettinger, Jürgen, Vasilets, Larisa A., Schwarz, Wolfgang

“…Tetraethylammonium (TEA +) is an effective inhibitor of a variety of K + channels, and has been widely used to reduce K +-sensitive background conductances in…”
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Inhibition of the Na+,K+ pump by the epileptogenic pentylenetetrazole by Dubberke, R, Vasilets, L A, Schwarz, W

“…Pentylenetetrazole (PTZ) is a convulsant drug used in animal experiments to induce epileptic activity. It is known to interact with a variety of channels and…”
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Phosphorylation of the α‐subunits of the Na+/K+‐ATPase from mammalian kidneys and Xenopus oocytes by cGMP‐dependent protein kinase results in stimulation of ATPase activity by Fotis, Heike, Tatjanenko, Liliya V., Vasilets, Larisa A.

“…Phosphorylation of Na+/K+‐ATPase by cGMP‐dependent protein kinase (PKG) has been studied in enzymes purified from pig, dog, sheep and rat kidneys, and in…”
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The Na+,K+‐ATPase carrying the carboxy‐terminal Ca2+/calmodulin binding domain of the Ca2+ pump has 2Na+,2K+ stoichiometry and lost charge movement in Na+/Na+ exchange by Yoshimura, Shige H, Vasilets, Larisa A, Ishii, Toshiaki, Takeyasu, Kunio, Schwarz, Wolfgang

“…An altered ion‐transport stoichiometry from 3Na+,2K+ to 2Na+,2K+ is observed in a chimeric Na+,K+‐ATPase, which carries the Ca2+/calmodulin binding domain…”
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Structure-function relationships of Na+/K(+)-pumps expressed in Xenopus oocytes by Schwarz, W, Vasilets, L A

“…During the last years we have examined structure-function relationships in the Na+/K(+)-ATPase with respect to interactions of the external cations with the…”
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The Ca2+/calmodulin binding domain of the Ca2+‐ATPase linked to the Na+,K+‐ATPase alters transport stoichiometry by Zhao, Jianxing, Vasilets, Larisa A., Yoshimura, Shige H., Gu, Quanbao, Ishii, Toshiaki, Takeyasu, Kunio, Schwarz, Wolfgang

“…Using Xenopus oocytes as an expression system, we have investigated ion‐transport and ouabain‐binding properties of a chimeric ATPase (α1‐CBD; Ishii and…”
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Modification of the PKC phosphorylation site Ser-23 of the rat alpha1 subunit by Vasilets, L A, Spielmann, A, Schwarz, W

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Modification of the PKC Phosphorylation Site Ser-23 of the Rat α1 Subunit by VASILETS, L. A., SPIELMANN, A., SCHWARZ, W.

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Action of burn serum on electrical and contractile activity of the homoiothermic myocardium by Vasilets, L. A.

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