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ADP + phosphate + 3 Na+/out
ATP + 3 Na+/in
-
in the absence of K+ and in the presence of ATP and ADP without net ATP hydrolysis
transphosphorylation of ATP/ADP
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
ATP + H2O
ADP + phosphate
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
ATP + H2O + 3 Na+[side 1] + 2 K+[side 2]
ADP + phosphate + 3 Na+[side 2] + 2 K+[side 1]
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
ATP + H2O + Na+/in + Rb+/out
ADP + phosphate + Na+/out + Rb+/in
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
ATP + H2O + Na+[side 1] + Rb+[side 2]
ADP + phosphate + Na+[side 2] + Rb+[side 1]
-
-
-
-
?
ATP + Na+/in
ADP + phosphate + Na+/out
beta-(2-furyl)acryloyl phosphate + H2O
?
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
additional information
?
-
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
r
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
r
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
reaction obeys Michaelis-Menten kinetics
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
enzyme has a high- and a low-affinity ATP hydrolizing site
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
Pareledone sp.
-
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
-
-
-
-
?
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
-
-
-
-
?
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
r
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
formation of a phosphorylated intermediate
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
a continous Na+ influx exists across the plasma membrane in the presence of external Na+. When Na+ is removed from both external and internal solutions, a transient outward pump current is observed by adding K+ to the external solution, thus indicating that the transient pump current is activated by the residual intracellular Na+
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme does not show a distinct voltage dependency either with or without extracellular Na+. In presence of extracellular Na+ a steady Na+-K+ pump current exists even in absence of internal Na+. A steady Na+-K+ pump current is observed with 10 mM intracellular Na+
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
dogfish
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
Frog
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
246952, 246960, 246962, 246966, 246968, 246973, 711156, 711774, 712134, 712538, 712805, 713011, 734675 -
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme plays a crucial role in cellular ion homeostasis
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
may not play a significant role in adaption in freshwater crustaceans
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
for each ATP molecule hydrolyzed three Na+ ions are transported out of and two K+ ions into the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
creation of a electrochemical gradient of Na+ ions into and K+ ions out of the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
246950, 246954, 246958, 246959, 246962, 246964, 246966, 246969, 246972, 695469, 695495, 710811, 712134, 712794, 713007, 713111, 713119, 733517, 734325, 734529, 734530, 734538, 735119, 735146, 735302 -
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
modelling of enzyme function in neurons in absence or presence of ethanol, overview
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
shark
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + Rb+/out
ADP + phosphate + Na+/out + Rb+/in
-
measurement of enzyme activity by ouabain-sensitive 86Rb+ uptake
-
-
?
ATP + H2O + Na+/in + Rb+/out
ADP + phosphate + Na+/out + Rb+/in
-
measurement of enzyme activity by ouabain-sensitive Rb+ uptake
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + Na+/in
ADP + phosphate + Na+/out
-
-
-
-
?
ATP + Na+/in
ADP + phosphate + Na+/out
-
under saturating Mg2+, Na+, and K+ conditions, enzyme exhibits two well-defined ATP hydrolyzing sites. At the high-affinity sites, K0.5 value is 63.8 nmol per l, at the low-affinity sites, hydrolysis follows Michaelis-Menten kinetics
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
additional information
?
-
-
Na+K+-ATPase actively participates in the regulation of endosomal pH value and endocytosed membrane traffic
-
-
?
additional information
?
-
-
the enzyme also catalyzes: 1. uncoupled Na+ efflux in presence of Na+/in, Mg2+ and ATP, 2. Na+-dependent ADP/ATP exchange, 3. K+-dependent enzyme phosphorylation by phosphate
-
-
?
additional information
?
-
-
assay using solid-supported membrane, overview
-
-
?
additional information
?
-
-
electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
-
-
?
additional information
?
-
-
subunit isoform alpha2 abundance is higher in the t-tubules than in the surface sarcolemma. The isoform is functinally coupled to the Na+/Ca2+-exchanger and can regulate Ca2+ handling without changing global concentration of Na+
-
-
?
additional information
?
-
-
K+-dependent ATPase activity in absence of Na+ at acid pH, protons can be transported by the sodium pump in place of Na+
-
-
?
additional information
?
-
-
the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor. ND1 as a Src-interacting domain from the Na/K-ATPase alpha1 subunit, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
ATP + H2O + 3 Na+[side 1] + 2 K+[side 2]
ADP + phosphate + 3 Na+[side 2] + 2 K+[side 1]
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
additional information
?
-
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
r
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
-
-
-
-
?
ATP + H2O + 3 Na+/in + 2 K+/out
ADP + phosphate + 3 Na+/out + 2 K+/in
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
r
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme plays a crucial role in cellular ion homeostasis
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
may not play a significant role in adaption in freshwater crustaceans
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
creation of a electrochemical gradient of Na+ ions into and K+ ions out of the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
710811, 712134, 712794, 713007, 713111, 733517, 734325, 734529, 734530, 734538, 735119, 735146, 735302 -
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
modelling of enzyme function in neurons in absence or presence of ethanol, overview
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + Na+[side 1] + K+[side 2]
ADP + phosphate + Na+[side 2] + K+[side 1]
-
-
-
-
?
additional information
?
-
-
Na+K+-ATPase actively participates in the regulation of endosomal pH value and endocytosed membrane traffic
-
-
?
additional information
?
-
-
electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
-
-
?
additional information
?
-
-
subunit isoform alpha2 abundance is higher in the t-tubules than in the surface sarcolemma. The isoform is functinally coupled to the Na+/Ca2+-exchanger and can regulate Ca2+ handling without changing global concentration of Na+
-
-
?
additional information
?
-
-
the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor. ND1 as a Src-interacting domain from the Na/K-ATPase alpha1 subunit, overview
-
-
?
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(12beta,20R)-12-hydroxy-20,25-epoxydammarane-3,6-dione
-
(1R,2R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-2,3a,11,11a-tetrahydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,2R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)-2-(2-oxopropanoyl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-13a-formyl-3a,11a-dihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-11-yl beta-D-glucopyranoside
-
-
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1S,3aR,3bR,12aR,14R)-10-fluoro-14-hydroxy-3a,3b,6,6,12a-pentamethyl-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
-
(1S,3aR,3bR,12aR,14R)-14-hydroxy-3a,3b,6,6,12a-pentamethyl-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
-
(1S,3aR,3bR,12aR,14R)-14-hydroxy-3a,3b,6,6,12a-pentamethyl-10-(trifluoromethoxy)-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
-
(20R)-20,25-epoxydammarane-3,6,12-trione
-
(3beta,12beta,20R)-12-hydroxy-3-phenoxy-20,25-epoxydammaran-6-one
-
(3beta,12beta,20R)-12-hydroxy-3-[(5-oxo-4,5-dihydro-1,2,4-oxadiazol-3-yl)oxy]-20,25-epoxydammaran-6-one
-
(3beta,12beta,20R)-12-hydroxy-3-[4-(trifluoromethoxy)phenoxy]-20,25-epoxydammaran-6-one
-
(3beta,12beta,20R)-3-(ethenyloxy)-12-hydroxy-20,25-epoxydammaran-6-one
-
(3beta,12beta,20R)-3-ethoxy-12-hydroxy-20,25-epoxydammaran-6-one
-
(3E,5beta,15beta,16beta)-16-(acetyloxy)-3-(hydroxyimino)-8-methyl-14,15-epoxybufa-20,22-dienolide
-
-
(3E,5beta,15beta,16beta)-16-(acetyloxy)-3-(methoxyimino)-8-methyl-14,15-epoxybufa-20,22-dienolide
-
-
(3E,5beta,15beta,16beta)-16-(acetyloxy)-3-[(2-aminoethoxy)imino]-8-methyl-14,15-epoxybufa-20,22-dienolide
-
most potent inhibitor
(5aR,7R,8S,10aR,10bR)-7-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]hexadecahydrocyclopenta[5,6]naphtho[2,1-c]azepine-3,12-dione
-
(5aR,8S,10aR,10bR,12R)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
-
(5aR,8S,10aR,10bR,12S)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
-
(6alpha,12beta,20R)-12-hydroxy-6-[(prop-2-en-1-yl)oxy]-20,25-epoxydammaran-3-one
-
(6alpha,12beta,20R)-6,12-bis(benzyloxy)-20,25-epoxydammaran-3-one
-
(6alpha,12beta,20R)-6,12-bis[(prop-2-en-1-yl)oxy]-20,25-epoxydammaran-3-one
-
(6alpha,12beta,20R)-6-(benzyloxy)-12-hydroxy-20,25-epoxydammaran-3-one
-
(6alpha,20R)-6-hydroxy-20,25-epoxydammarane-3,12-dione
-
1,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
i.e. wedelolactone, inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
1-chloro-2,4-dinitrobenzene
-
inhibition of the transport activity of the Na-K pump
12,20-dihydroxydammar-24-en-3-yl 2-O-D-glucopyranosyl-D-glucopyranoside
-
-
12,20-dihydroxydammar-24-en-3-yl D-glucopyranoside
-
-
19-hydroxy-2''-oxovoruscharin
-
i.e. UNBS1450, a trans-trans-cis cardiotonic steroid
1H-[1,2,4]oxadiazole[4,3-a]quinoxalin-1-one
-
ODQ, inhibition of SNP-induced pump stimulation
2,3-dihydroxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2,9-dihydroxy-3,8-dimethoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2-aminoethyl-methanethiosulfonate
-
inhibition of mutants F323C, P333C, E334C, G335C, I322C, G326C and A330C
3,8,9-trihydroxy-2-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
3-[(2-O-D-glucopyranosyl-D-glucopyranosyl)oxy]-12-hydroxydammar-24-en-20-yl D-glucopyranoside
-
-
3-[(3S,3aS,4R,5aR,6S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoic acid
-
4,7-diacetoxy-14-hydroxydolast-1(15),8-diene
-
-
4-acetoxy-9,14-dihydroxydolast-1(15),7-diene
-
-
4-[(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-13a-(hydroxymethyl)-9,15a-dimethylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
5-hydroxydecanoate
-
presence of 5 mM ATP, inhibitory above 1 mM. Presence of 0.05 mM ATP, inhibitory above 0.25 mM. No effect on ouabain-sensitiviy of the enzyme
8-methoxycoumestrol
-
inhibits the isozyme alpha1beta1 Na,K-ATPase, mechanism, overview
A-769662
-
inhibits the Na+-K+-ATPase transport activity and cell surface abundance in L6 cells, which is independent of AMP kinase activation, overview
alpha2-adrenergic agonists
-
negative modulator
-
astragaloside III
-
from dried roots of Astragalus membraneceus or var. mongholicus
ATP
-
competitive inhibitor of K+-phosphatase activity
benzyltriethylammonium chloride
-
inhibition of pump current is dependent on membrane potential
bradykinin
-
negative modulator
cholic acid
-
from dried bile of Ursus arctos or Selenarctos thibetanus
cinobufotalin
-
27.5% inhibition at 0.01 mM
cyclosporin A
-
diminishs induction of alpha1 protein in activated lymphocytes
dammar-24-ene-3,12,20-triol
-
-
dammar-24-ene-3,6,12,20-tetrol
-
-
dansylcysteinyl-mercuric chloride
-
-
diphenyl diselenide
-
activity is restored by DTT
dopamine
-
negative modulator
endothelin
-
negative modulator
-
epicatechin-3-gallate
-
solubilization of the Na+,K+-ATPase with a nonionic detergent reduces sensitivity to epigallocatechin-3-gallate
epigallocatechin-3-gallate
-
noncompetitive with respect to ATP, reduces the affinity for vanadate, shifts the equilibrium of E1P and E2P toward E1P, and reduces the rate of the E1P to E2P transition
epinephrine
-
0.5 mM epinephrine added for 20 min, decreases the activity of the enzyme by around 50%. Treatment with Rp-cAMP, indomethacin, PP2, SB202190, and PD98059 completely abrogate the effect of epinephrine
ethylester of glutathione
-
inhibition of the transport activity of the Na-K pump
ethylmercurithiosalicylate
-
-
fenoldopam
-
induces inhibition of Na+ ?K+-ATPase activity in HK-2 cells. Ouabain protects against the cyclic adenosine monophosphate accumulation and Na+ ?K+-ATPase inhibition induced by the D1 receptor agonist fenoldopam in HK-2 cells. Chronic ouabain treatment decreases the protein and mRNA expression levels of the D1 receptor and increases the basal phosphorylation of the D1 receptor in HK-2 cells
genistein
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
ginsenoside Rh2
-
from dried roots of Panax ginseng or Panax notoginseng
glyburide
-
presence of 5 mM ATP, slightly stimulating up to 1 mM, inhibitory above. Presence of 0.05 mM ATP, stimulating at least up to 3 mM
glycyrrhizin
-
from roots of Glycyrrhiza uralensis , Glycyrrhiza inflata, or Glycyrrhiza glabra
herbimycin A
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
isovaleric acid
-
isovaleric acid injection significantly inhibits Na+,K+-ATPase activity by 25% in cerebral cortex of rats 2 or 24 h after administration, while pre-treatment of rats with creatine completely prevents the inhibitory effects of isovaleric acid on Na+,K+-ATPase
jujuboside B
-
from mature seeds of Ziziphus jujube var. spinosa
L-homocysteine
-
inhibitory effect is reversed by alanine
lauric acid
-
presence of 5 mM ATP, inhibitory above 0.25 mM. Presence of 0.05 mM ATP, stimulating up to 0.3 mM, inhibitory above
lavendustin A
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
Lyn kinase
-
Lyn kinase directly binds to the Na+,K+-ATPase alpha3 subunit for regulation of activity
-
m-trifluoromethyl-diphenyl diselenide
-
i.e. (m-CF3C6H4Se)2, activity is restored by DTT
methyl 3-[(3S,3aS,4R,5aR,6R,7R,9aR,9bS)-4-hydroxy-7-(2-hydroxypropan-2-yl)-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
-
methyl 3-[(3S,3aS,4R,5aR,6R,7S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-7-(prop-2-en-1-yl)-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
-
methyl 3-[(3S,3aS,4R,5aR,6S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
-
monosodium glutamate
-
selenofuranoside therapy is able to prevent the inhibition of the enzyme activity in the hippocampus but not in the brain cortex
MTSET
-
[2-(trimethylammonium)ethyl]methanethiosulphonate bromide, inhibits mutants G803C, V805C
Na+
-
25% inhibition at 80 mmol/l
Na/K ATPase-alpha1-specific siRNA A1
-
Na/K ATPase-alpha1-specific siRNA A2
-
Na/K ATPase-alpha1-specific siRNA A3
-
Na/K ATPase-alpha1-specific siRNA A4
-
O-[(3beta,12beta,20R)-12-hydroxy-6-oxo-20,25-epoxydammaran-3-yl] O-methyl 2-imidothiodicarbonate
-
odoroside A
-
i.e. 3beta-O-(beta-D-diginosyl)-14-hydroxy-5beta,14beta-card-20(22)-enolide, isolated from the stems and twigs of Nerum oleander, inhibits the enzyme's ATPase activity
Omeprazole
-
inhibit mutants G803C, T804C, V805C
p-chloro-diphenyl diselenide
-
i.e. (p-ClC6H4Se)2, activity is restored by DTT
p-methoxyl-diphenyl diselenide
-
i.e. (p-CH3OC6H4Se)2, activity is restored by DTT
Pb2+
-
inhibitory effect of Pb2+ on the transport cycle of the Na+,K+-ATPase, overview. Pb2+ inhibits cycling of the enzyme, but it does not affect cytoplasmic Na+ binding and release of Na+ ions at the extracellular side at concentrations below 0.010 mM
polygalacic acid
-
from dried roots of Platycodon grandiflorum
PP1
-
Src kinase inhibitor
Prostaglandins
-
negative modulator
-
reduced glutathione
-
extracellular and, or intracellular, inhibition of the transport activity of the Na-K pump
saikosaponin A
-
from dried roots of Bupleurum chinense or Bupleurum scorzonerifolium
sarsasapogenin
-
from dried roots of Anemarrhena asphodeloides
suramin
-
potent inhibitor, acts on the inside surface of the sodium pump
tetraethylammonium chloride
-
inhibition of pump current is independent on membrane potential
Tumor necrosis factor alpha
-
TNF-alpha, TNF-alpha affects the Na+-K+ pump via PGE2-dependent pathways
-
ursolic acid
-
from whole plant of Prunella vulgaris with dried flowers
Yes kinase
-
regulator of the Na+,K+-ATPase activity
-
[Au(2,2'-bipyridine)Cl2]+
-
-
[Au(dimethylsulfoxide)2Cl2]+
-
-
[PdCl(dien)]+
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
[PdCl(Me4dien)]+
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
-
[PdCl4]2-
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
BAY-K8644
-
a calcium channel agonist, the effect is blocked by a phosphatidylinositol-3 kinase inhibitor wortmannin
BAY-K8644
-
a calcium channel agonist, the effect is blocked by a phosphatidylinositol-3 kinase inhibitor wortmannin
bufalin
-
inhibition of the enzyme, enhancement of the acidification of the late endosome, alteration in membrane traffic
bufalin
-
from dried venom of Bufo gargarizans or Bufo bufo melanostictus
Ca2+
-
CaCl2 up to 300 microM does not affect Na+/K+-ATPase activity, but CaCl2 above 1 mM inhibits the activity
Ca2+
-
enzyme from anterior intestine is 5-fold more sensitive than enzymes from pyloric caeca and posterior intestine
digitoxigenin
-
-
digoxin
-
-
Ethacrynic acid
-
-
ethanol
-
-
ethanol
-
inhibits the enzyme in Golgi membranes of cerebellar neurons leading to potentiation of GABAergic transmission at Golgi cell-to-granule cell synapses throughan increase in Golgi cell excitability
Mg2+
-
considerable inhibition of enzyme activity is seen above 5 mM Mg2+
Mg2+
-
IC50: 0.0008 mM; IC50: 0.0012 mM; IC50: 0.012 mM
Na/K ATPase-alpha1-specific siRNA A1
-
0% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A1
-
-
-
Na/K ATPase-alpha1-specific siRNA A2
-
20% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A2
-
-
-
Na/K ATPase-alpha1-specific siRNA A3
-
20% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A3
-
-
-
Na/K ATPase-alpha1-specific siRNA A4
-
40% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A4
-
-
-
oleandrin
-
-
oleandrin
-
oleandrin treatment results in selective inhibition of human cancer cell growth but not rodent cell proliferation, which corresponds to the relative level of Na,K-ATPase alpha3 subunit protein expression. A correlation is observed between the ratio of alpha3 to alpha1 isoforms and the level of oleandrin uptake during inhibition of cell growth and initiation of cell death, the higher the alpha3 expression relative to alpha1 expression, the more sensitive the cell is to treatment with oleandrin
oleandrin
-
oleandrin treatment results in selective inhibition of human cancer cell growth but not rodent cell proliferation, which corresponds to the relative level of Na,K-ATPase alpha3 subunit protein expression. A correlation is observed between the ratio of alpha3 to alpha1 isoforms and the level of oleandrin uptake during inhibition of cell growth and initiation of cell death, the higher the alpha3 expression relative to alpha1 expression, the more sensitive the cell is to treatment with oleandrin
oleanolic acid
-
-
oleanolic acid
-
from whole plant of Prunella vulgaris with dried flowers
oligomycin
-
inhibits (Na+,K+)-ATPase reaction and Na+-ATPase reaction, has little effect on the K+-phosphatase reaction and can stimulate the ADP/ATP exchange reaction
oligomycin
-
not completely inhibits but decreases the rate of turnover of transport and of the hydrolysis reaction. Oligomycin affects the extracellular side of the system, Na+ on the cytoplasmic side of the system is necessary for the effect, oligomycin decreases the rate of transition from the Na+ form to the K+ form of the enzyme, but has no effect on the rate of the reverse reaction
orthovanadate
-
up to 87% inhibition
orthovanadate
-
increasing orthovanadate concentrations from 0.0001 mM to 1 mM inhibit total ATPase activity by around 75%
orthovanadate
-
up to 67% inhibition in absence of NH4+
orthovanadate
-
up to 75% inhibition at 0.05 mM
orthovanadate
-
about 44% inhibition at 3 mM
Ouabain
-
ouabain up to 1 mM decreases silkworm ATPase activity to 42% of the maximal ATPase activity in presence of 10 mM NaCl and 30 mM KCl
Ouabain
-
up to 87% inhibition
Ouabain
-
76.4% residual activity at 3 mM
Ouabain
-
up to 67% inhibition in absence of NH4+
Ouabain
-
about 70% inhibition at 3 mM
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy. Ouabain produces in the cat at 25 nM a 43% decrease in cell viability due to apoptosis and necrosis
Ouabain
-
inhibition of enzyme, enhancement of the acidification of the late endosome
Ouabain
-
ouabain does not affect TNF-alpha-induced mRNA expression but inhibits TNF-alpha-induced protein expression
Ouabain
-
specific inhibitor
Ouabain
-
73% inhibition at 3 mM
Ouabain
-
interaction is dependent on the conformation and phosphorylation state of the protein
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis.The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy
Ouabain
-
complete inhibition at 0.001 mM
Ouabain
-
-
671274, 673231, 675717, 675725, 695469, 695856, 696017, 699696, 700430, 701003, 710811
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy. Ouabain produces in the rat at 0.002 mM a 43% decrease in cell viability due to apoptosis and necrosis
Ouabain
-
55% inhibition at 0.02 mM
Ouabain
-
6.1% inhibition at 0.01 mM
Ouabain
-
about 30% inhibition at 2 mM
Ouabain
-
specific inhibitor
Ouabain
-
enzyme from anterior intestine is ten-fold more sensitive than enzymes from pyloric caeca and posterior intestine
Ouabain
a cardiac glycoside derived from Strophanthus gratus, ouabain is deeply inserted into the transmembrane domain with the lactone ring very close to the bound K+. Low-affinity ouabain-bound state due to antagonism between ouabain and K+. The closure of the binding cavity confers a high affinity, homology model for the high affinity state, structures, overview. Binding of sugar moiety and steroid core, overveiw
Ouabain
-
specific inhibitor
Ouabain
-
Na+/K+-ATPase specific inhibitor
Ouabain
-
about 50% inhibition at 3 mM, ouabain inhibition increases about 80% in the presence of NH4+ with a 3fold lower KI value
oubain
-
-
oubain
-
two apparently different oubain binding sites
oubain
-
the IC50 value is higher in neonates than in children
oubain
-
K+ completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes
oubain
-
K+ protects against inhibition, probably due to phosphorylating effect
oubain
-
quantitative aspects of the interaction between oubain and the enzyme in vitro
oubain
-
half-maximal inhibition at 0.1 mM
palytoxin
-
-
palytoxin
-
mild, non-toxic, exposures to the Na+/K+-ATPase inhibitor palytoxin synergistically sensitizes the vulnerability of neurons to normally non-toxic concentrations of domoic acid, leaving NMDA receptor-mediated excitotoxic response unaltered. Palytoxin causes a voltage-sensitive Na+ channel-independent increase in intracellular Na+. Enhancement of the excitotoxic response to domoic acid by palytoxin is time-dependent and is not affected by gene expression inhibitors
perillyl alcohol
-
a monoterpene, inhibits Na/K-ATPase, non-competitive inhibition for Na+ and K+ and an uncompetitive inhibition for ATP in brain and kidney
perillyl alcohol
-
a monoterpene, inhibits Na/K-ATPase showing a noncompetitive inhibition profile to Na+ and K+ and an uncompetitive inhibition towards ATP. The generated electrochemical gradient is essential for a number of other cellular functions
prostaglandin E2
-
-
putrescine
-
-
putrescine
-
putrescine inhibits (Na+, K+)-ATPase phosphorylation and activity in juvenile and adult shrimp gill
spermidine
-
-
spermidine
-
spermidine inhibits (Na+, K+)-ATPase phosphorylation and activity in juvenile and adult shrimp gill
strophanthidin
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
strophanthidin
-
29.6% inhibition at 0.01 mM
vanadate
-
-
vanadate
-
20fold less sensitive to vanadate than alpha1 and 3; 20 times more sensitive to vanadate than alpha2
vanadate
-
epigallocatechin-3-gallate reduces the affinity for vanadate, shifts the equilibrium of E1P and E2P toward E1P, and reduces the rate of the E1P to E2P transition
additional information
-
not inhibitory: NH4+. At elevated concentrations of NH4+, enzyme is fully active and K+ cannot displace NH4+ from its exclusive binding sites
-
additional information
-
odoroside A and ouabain potently reduce NF-kappaB-inducible de novo protein synthesis, largely due to its ability to block Na+-dependent transport of amino acids across the plasma membrane, but not to interfering with the translation machinery
-
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum
-
additional information
-
inhibitory potencies of cardenolide glycosides, isolated from the roots of Pergularia tomentosa, on Na+,K+-ATPase activity
-
additional information
-
spermine has a negligible effect (less than 10%) on enzyme activity
-
additional information
-
enzyme activity is inhibited by excess ATP
-
additional information
-
decrease in extracellular pH inhibits Na+-K+ pump activity
-
additional information
-
physical training is effective against Na+,K+-ATPase enzyme activity inhibition, while fluid percussion injury induces a decrease in Na+,K+-ATPase activity in the ipsilateral cerebral cortex of sedentary animals
-
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum
-
additional information
cardiac glycosides are efficient inhibitors of the Na+,K+-ATPase
-
additional information
-
molecular docking and modelling, and inhibitory potencies of steroid-like compounds from Chinese medicinal products, used for promoting the blood circulation, with Na+,K+-ATPase, overview
-
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0.00081
(12beta,20R)-12-hydroxy-20,25-epoxydammarane-3,6-dione
Sus scrofa
pH and temperature not specified in the publication
0.0017
(1R,2R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-2,3a,11,11a-tetrahydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0012
(1R,2R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)-2-(2-oxopropanoyl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0005
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-13a-formyl-3a,11a-dihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-11-yl beta-D-glucopyranoside
Homo sapiens
-
pH 7.8, 37°C
0.0004
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0005
(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.000091
(1S,3aR,3bR,12aR,14R)-10-fluoro-14-hydroxy-3a,3b,6,6,12a-pentamethyl-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
Sus scrofa
pH and temperature not specified in the publication
0.00077
(1S,3aR,3bR,12aR,14R)-14-hydroxy-3a,3b,6,6,12a-pentamethyl-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
Sus scrofa
pH and temperature not specified in the publication
0.00036
(1S,3aR,3bR,12aR,14R)-14-hydroxy-3a,3b,6,6,12a-pentamethyl-10-(trifluoromethoxy)-1-[(2R)-2,6,6-trimethyloxan-2-yl]-2,3,3a,3b,4,5a,6,7,12,12a,12b,13,14,14a-tetradecahydrocyclopenta[5,6]naphtho[2,1-b]carbazol-5(1H)-one
Sus scrofa
pH and temperature not specified in the publication
0.00076
(20R)-20,25-epoxydammarane-3,6,12-trione
Sus scrofa
pH and temperature not specified in the publication
0.0003
(3beta,12beta,20R)-12-hydroxy-3-phenoxy-20,25-epoxydammaran-6-one
Sus scrofa
pH and temperature not specified in the publication
0.00096
(3beta,12beta,20R)-12-hydroxy-3-[(5-oxo-4,5-dihydro-1,2,4-oxadiazol-3-yl)oxy]-20,25-epoxydammaran-6-one
Sus scrofa
pH and temperature not specified in the publication
0.00045
(3beta,12beta,20R)-12-hydroxy-3-[4-(trifluoromethoxy)phenoxy]-20,25-epoxydammaran-6-one
Sus scrofa
pH and temperature not specified in the publication
0.00105
(3beta,12beta,20R)-3-(ethenyloxy)-12-hydroxy-20,25-epoxydammaran-6-one
Sus scrofa
pH and temperature not specified in the publication
0.00114
(3beta,12beta,20R)-3-ethoxy-12-hydroxy-20,25-epoxydammaran-6-one
Sus scrofa
pH and temperature not specified in the publication
0.00041
(5aR,7R,8S,10aR,10bR)-7-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]hexadecahydrocyclopenta[5,6]naphtho[2,1-c]azepine-3,12-dione
Sus scrofa
pH and temperature not specified in the publication
0.00123
(5aR,8S,10aR,10bR,12R)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
Sus scrofa
pH and temperature not specified in the publication
0.00113 - 0.00118
(5aR,8S,10aR,10bR,12S)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
0.00091
(6alpha,12beta,20R)-12-hydroxy-6-[(prop-2-en-1-yl)oxy]-20,25-epoxydammaran-3-one
Sus scrofa
pH and temperature not specified in the publication
0.00087
(6alpha,12beta,20R)-6,12-bis(benzyloxy)-20,25-epoxydammaran-3-one
Sus scrofa
pH and temperature not specified in the publication
0.00075
(6alpha,12beta,20R)-6,12-bis[(prop-2-en-1-yl)oxy]-20,25-epoxydammaran-3-one
Sus scrofa
pH and temperature not specified in the publication
0.00033
(6alpha,12beta,20R)-6-(benzyloxy)-12-hydroxy-20,25-epoxydammaran-3-one
Sus scrofa
pH and temperature not specified in the publication
0.0007
(6alpha,20R)-6-hydroxy-20,25-epoxydammarane-3,12-dione
Sus scrofa
pH and temperature not specified in the publication
0.0007
1,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.055
12,20-dihydroxydammar-24-en-3-yl D-glucopyranoside
Sus scrofa
-
-
0.003
2,3-dihydroxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.0007
2,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.006
2,9-dihydroxy-3,8-dimethoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.003
3,8,9-trihydroxy-2-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.00114
3-oxo-panaxatriol
Sus scrofa
pH and temperature not specified in the publication
0.00054
3-[(3S,3aS,4R,5aR,6S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoic acid
Sus scrofa
pH and temperature not specified in the publication
0.171
4,7-diacetoxy-14-hydroxydolast-1(15),8-diene
Cavia porcellus
-
enzym preparation from kidney
0.0007
4-[(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-13a-(hydroxymethyl)-9,15a-dimethylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
0.0004
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
0.0003
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
0.00118
6-oxo-panaxatriol
Sus scrofa
pH and temperature not specified in the publication
0.00009
8-methoxycoumestrol
Homo sapiens
-
isozyme alpha1beta1 Na,K-ATPase, pH 7.4, 30°C
0.000575
AuCl4-
Sus scrofa
-
at pH 7.4 and 37°C
0.000587
beta-acetyldigoxin
Homo sapiens
-
isozyme alpha1beta1 Na,K-ATPase, pH 7.4, 30°C
0.003
bufalin
Homo sapiens
-
-
0.000287
digitoxin
Homo sapiens
-
isozyme alpha1beta1 Na,K-ATPase, pH 7.4, 30°C
0.00027 - 0.000409
digoxin
0.031
diphenyl diselenide
Rattus norvegicus
-
pH 7.4, 37°C
0.2
epicatechin
Sus scrofa
-
pH 7.0, 37°C
0.0008
epicatechin-3-gallate
Sus scrofa
-
pH 7.0, 37°C
0.001
epigallocatechin-3-gallate
Sus scrofa
-
pH 7.0, 37°C
0.006
m-trifluoromethyl-diphenyl diselenide
Rattus norvegicus
-
pH 7.4, 37°C
0.00026
methyl 3-[(3S,3aS,4R,5aR,6R,7R,9aR,9bS)-4-hydroxy-7-(2-hydroxypropan-2-yl)-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
Sus scrofa
pH and temperature not specified in the publication
0.00109
methyl 3-[(3S,3aS,4R,5aR,6R,7S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-7-(prop-2-en-1-yl)-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
Sus scrofa
pH and temperature not specified in the publication
0.00041
methyl 3-[(3S,3aS,4R,5aR,6S,9aR,9bS)-4-hydroxy-6,9a,9b-trimethyl-8-oxo-3-[(2R)-2,6,6-trimethyloxan-2-yl]dodecahydro-1H-cyclopenta[a]naphthalen-6-yl]propanoate
Sus scrofa
pH and temperature not specified in the publication
0.000282
methyldigoxin
Homo sapiens
-
isozyme alpha1beta1 Na,K-ATPase, pH 7.4, 30°C
0.00138
O-[(3beta,12beta,20R)-12-hydroxy-6-oxo-20,25-epoxydammaran-3-yl] O-methyl 2-imidothiodicarbonate
Sus scrofa
pH and temperature not specified in the publication
0.0012
odoroside A
Homo sapiens
-
pH 7.0, 37°C
0.115
oleic acid
Cavia porcellus
-
enzym preparation from kidney
0.006
p-chloro-diphenyl diselenide
Rattus norvegicus
-
pH 7.4, 37°C
0.045
p-methoxyl-diphenyl diselenide
Rattus norvegicus
-
pH 7.4, 37°C
0.00109
panaxatriol
Sus scrofa
pH and temperature not specified in the publication
0.0398
[Au(2,2'-bipyridine)Cl2]+
Sus scrofa
-
at pH 7.4 and 37°C
0.0055
[Au(dimethylsulfoxide)2Cl2]+
Sus scrofa
-
at pH 7.4 and 37°C
0.0121
[PdCl(dien)]+
Sus scrofa
-
pH 7.4, 37°C
0.0236
[PdCl(Me4dien)]+
Sus scrofa
-
pH 7.4, 37°C
-
0.0225
[PdCl4]2-
Sus scrofa
-
pH 7.4, 37°C
0.00113
(5aR,8S,10aR,10bR,12S)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
Sus scrofa
pH and temperature not specified in the publication
0.00118
(5aR,8S,10aR,10bR,12S)-12-hydroxy-1,1,5a,10a,10b-pentamethyl-8-[(2R)-2,6,6-trimethyloxan-2-yl]tetradecahydro-1H-cyclopenta[5,6]naphtho[2,1-c]oxepine-3,7-dione
Sus scrofa
pH and temperature not specified in the publication
0.00027
digoxin
Sus scrofa
pH and temperature not specified in the publication
0.000409
digoxin
Homo sapiens
-
isozyme alpha1beta1 Na,K-ATPase, pH 7.4, 30°C
0.0008
Mg2+
Rattus norvegicus
-
IC50: 0.0008 mM
0.0012
Mg2+
Rattus norvegicus
-
IC50: 0.0012 mM
0.012
Mg2+
Rattus norvegicus
-
IC50: 0.012 mM
0.0001
Ouabain
Homo sapiens
-
-
0.00045
Ouabain
Sus scrofa
-
-
0.0016
Ouabain
Homo sapiens
-
pH 7.0, 37°C
0.0016
Ouabain
Cavia porcellus
-
enzym preparation from kidney
0.4
Ouabain
Callinectes sapidus
-
pH 7.4
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malfunction
-
depletion of subunit ATP1a1 reduces the level of active Rab27a in melanocytes and ist targeting to melanosomes
malfunction
-
knockdown causes a significant depolarization of the resting membrane potential in slow-twitch fibers of skeletal muscles. Abrupt mechanosensory responses are observed in alpha2Na+/K+-ATPase-deficient embryos, possibly linked to a postsynaptic defect. The enzyme deficiency reduces the heart rate and causes a loss of left-right asymmetry in the heart tube
malfunction
-
knocking down of catalytic subunit ATPalpha, but not alpha-like, in the entire Johnston's organ results in complete deafness. Knocking down beta subunit nrv2 in scolopale cells reduces ATPalpha expression in scolopale cells and causes almost complete deafness
metabolism
-
in vivo administration of isovaleric acid inhibits the citric acid cycle probably through the enzyme citrate synthase, as well as Na+,K+-ATPase, a crucial enzyme responsible for maintaining the basal potential membrane necessary for a normal neurotransmission, inhibition of these activities may be involved in the pathophysiology of the neurological dysfunction of isovaleric academic patients. Isovaleric acidemia is an autosomal recessive inherited metabolic disorder of leucine metabolism caused by a deficiency of isovaleryl-CoA dehydrogenase
metabolism
-
the enzyme is tightly coupled to glycolysis with undetectable flux of ATP between mitochondria and the enzyme
physiological function
-
inactivation of Na+, K+-ATPase leads to partial membrane depolarization allowing excessive Ca2+ entry inside neurons with resultant toxic events such as excitotoxicity
physiological function
-
Na+, K+-ATPase plays a role in regulating electrolyte concentration in the lens, contributing to lens transparency, and is involved in cataract formation caused by prolonged use of glucocorticoids, that suppress the Na+,K+-ATPase in the lens, overview
physiological function
-
Na+, K+-ATPase plays an important role in pulmonary inflammation
physiological function
Na+,K+-ATPase is responsible for establishing Na+ and K+ concentration gradients across the plasma membrane and therefore plays an essential role in, for instance, generating action potentials
physiological function
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Na/K-ATPase is a plasma membrane protein complex transferring the stored energy of ATP to the active transport of Na+ and K+ ions across the cell membrane. Na/K-ATPase alpha1 isoform modulates signaling mechanisms leading to apoptosis, cell migration, and cell proliferation
physiological function
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Na/K-ATPase is a plasma membrane protein complex transferring the stored energy of ATP to the active transport of Na+ and K+ ions across the cell membrane. The generated electrochemical gradient is essential for a number of other cellular functions
physiological function
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Klotho is a transmembrane protein with particularly strong expression in kidney, parathyroid glands and choroid plexus. Expression of Klotho in Xenopus oocytes increases the Na+/K+ ATPase pump current. Treatment of Xenopus oocytes with Klotho protein similarly increases the pump current
physiological function
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Klotho is a transmembrane protein with particularly strong expression in kidney, parathyroid glands and choroid plexus. Klotho-hypomorphic mice suffer from renal salt wasting and hypovolemia despite hyperaldosteronism. Na+/K+ ATPase protein abundance in isolated collecting ducts is lower in Klothohm mice than in their wild type littermates
physiological function
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the degree of activation of Na+/K+-ATPase at physiological Na+-concentrations differs between oxidative and glycolytic muscles and between subcellular membrane domains with different isoform compositions
physiological function
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alpha2Na+/K+-ATPase is important for skeletal and heart muscle function
physiological function
function of Na+,K+ ATPase Atp1a1 in the elongation of the zebrafish heart tube. Embryos lacking Atp1a1 function exhibit abnormal migration behavior of cardiac precursors, defects in the elongation of the heart tube, and a severe reduction in extracellular matrix/fibronectin deposition around the myocardium. Atp1a1 is expressed in an extraembryonic tissue, the yolk syncytial layer, at earlier stages. Knockdown of Atp1a1 activity specifically in the yolk syncytial layer produces heart tube elongation defects like those found in atp1a1 mutants
physiological function
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in addition to its role as a sodium pump regulating sperm motility, Na+/K+-ATPase is also involved as a signalling molecule during sperm capacitation
physiological function
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Na+,K+-ATPase functionally interacts with the plasma membrane Na+,Ca2+ exchanger to prevent Ca2+ overload and neuronal apoptosis in excitotoxic stress
physiological function
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nuclear Na+/K+-ATPase plays an active role in nucleoplasmic Ca2+ homeostasis
physiological function
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subunit ATP1a1 plays an essential role in Rab27a-dependent melanosome transport. The subunit is essential for targeting and activation of Rab27a to melanosomes
physiological function
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the beta subunits of the enzyme play a role in tissues during development and osmoregulation with beta1 subunits involved in the adaptation to hyperosmotic conditions and beta3 subunits to hypoosmotic environments
physiological function
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the catalytic subunit ATPalpha is required for hearing
physiological function
the enzyme maintains intracellular Na+ and K+ homeostasis and clears extracellular K+ after electric organe discharge
physiological function
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the Na+/K+-ATPase-alpha1 isoform is specifically involved in detection of extracellular Na+ concentration
physiological function
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the Na+K+-ATPase vascular functional activity is greater in male than femals rats
physiological function
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the neuronal glycine transporter GlyT2 function is strictly coupled to the sodium electrochemical gradient actively generated by the Na/K-ATPase
physiological function
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main enzyme responsible for Na+ reabsorption through the renal epithelium
physiological function
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main enzyme responsible for Na+ reabsorption through the renal epithelium
physiological function
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the enzyme is involved in cellular homeostasis in response to heavy metal exposure
additional information
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crucial role for Na+/K+-ATPase activity in determining neuronal vulnerability to domoic acid-mediated excitotoxicity. The enzyme inhibitor palytoxin enhances vulnerability of cultured cerebellar neurons to domoic acid via sodium-dependent mechanisms, overview
additional information
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ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum. The inhibitory effect is abolished by chelator of intracellular-free calcium BAPTA-AM, Ca2+ channel blocker nicardipine, inositol 1,4,5-trisphosphate receptor blocker 2-aminoethyl diphenyl borate, and PI3 kinase inhibitor wortmannin, overview
additional information
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ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum. The inhibitory effect is abolished by chelator of intracellular-free calcium BAPTA-AM, Ca2+ channel blocker nicardipine, inositol 1,4,5-trisphosphate receptor blocker 2-aminoethyl diphenyl borate, and PI3 kinase inhibitor wortmannin, overview
additional information
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ethanol-induced Na+,K+-ATPase inhibition leads to cerebellar dysfunction causing motor coordination impairments and cognitive deficits, and may also contribute to neuronal function alterations in other brain regions, overview. Ethanol increases firing frequency and regularity of spontaneous firing in presence of neurotransmitter receptor antagonists, ethanol increases spontaneous firing frequency and depolarizes the membrane potential, overview
additional information
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inhibition of proliferation of Panc-1 cells by oleandrin is significantly reduced when the relative expression of subunit alpha3 is decreased or when the expression of the alpha1 isoform is increased
additional information
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Na+, K+-ATPase inhibition by cardiotonic steroids increases COX-2 expression in A-549 cells, overview
additional information
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Na+,K+-ATPase alpha1 subunit is one of the targets for reactive oxygen species and is directly involved in oxidative stress. alpha1 Subunit level decrease after fluid percussion injury inducing traumatic brain injury in rats, overview. Physical training is effective against Na+,K+-ATPase enzyme activity inhibition, while fluid percussion injury induces a decrease in Na+,K+-ATPase activity in the ipsilateral cerebral cortex of sedentary animals
additional information
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Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
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Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
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Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
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odoroside A and ouabain potently reduce NF-kappaB-inducible de novo protein synthesis, largely due to its ability to block Na+-dependent transport of amino acids across the plasma membrane, but not to interfering with the translation machinery
additional information
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the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor complex and antagonizing ouabain-induced protein kinase cascades in rat cardiomyocytes, molecular mechanism of Na/KATPase-mediated Src regulation, overview. NaKtide does not directly affect the ERK and protein kinase C family of kinases. It inhibits Lyn with a much lower potency with IC50 of 0.0025 mM
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D409E
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phosphorylation site of alpha-subunit, inactive pump
R669Q
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ATP binding site of alpha-subunit, inactive pump
F785L
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mutation associated with familial rapid-onset dystonia parkinsonism, leads to functionally altered, but active, Na+K+-pumps with reduced apparent affinity for cytoplasmic Na+. Defect in the interaction of the E1 form of enzyme with Na+, and the E1-E2 equilibrium is not displaced. K+ interaction at the external activating sites of E2P phosphoenzyme is normal. The affinity for ouabain is significantly reduced
F785L/L786F
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aromatic function of F785 is critical for Na+ and ouabain binding
F785Y
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aromatic function of F785 is critical for Na+ and ouabain binding
T618M
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mutation associated with familial rapid-onset dystonia parkinsonism, leads to functionally altered, but active, Na+K+-pumps with reduced apparent affinity for cytoplasmic Na+. The Na+-affinity is reduced because of displacement of the conformational equilibrium in favor of the K+-occluded E2 form. K+ interaction at the external activating sites of E2P phosphoenzyme is normal
C911S/C964A/Q111R/N122D
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alpha-subunit: mutant without extracellularly exposed cysteine residues (911, 964) and with reduced ouabain sensitivity (111, 122)
C911S/C964S/Q111R/N122D
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alpha1-subunit mutant without extracellularly exposed cysteine residues (911, 964), and with reduced ouabain sensitivity (111, 122)
D714A
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insensitive to palytoxin
D714E
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the IC50 of the palytoxin-induced K+ efflux is 4fold higher than in cells expressing the wild-type enzyme
D714R
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insensitive to palytoxin
E779A
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15fold increase in K+ concentration that half-maximally activates Na,K-pump current at 0 mV in extracellular Na+-free solutions
G848F
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
G848W
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
K691A
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insensitive to palytoxin
K691D
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insensitive to palytoxin
K691R
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the EC50 of the palytoxin-induced K+ efflux is 7fold higher than in cells expressing the wild-type enzyme
N122D
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membrane potential and K+ dependence similar to wild-type Na,K-ATPase
Q111R
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membrane potential and K+ dependence similar to wild-type Na,K-ATPase
Q849G
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
Q849H
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
Q849W
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
S62C/N158Q/N193Q/N265Q
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beta-subunit: mutation for site-directed fluorescence labeling without impairing enzyme function (62) and mutations in all N-glycosylation sites of the beta1-ectodomain (158, 193, 265)
S62C/Y39F/Y43F
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beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with a shift of the conformational equilibrium (39,43)
S62C/Y39S/Y43S
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beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with a shift of the conformational equilibrium (39,43)
S62C/Y39W/Y43W
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beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with changed apparent rate constant for reverse binding of extracellular Na+ (39, 43)
S775A
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155fold increase in K+ concentration that half-maximally activates Na,K-pump current at 0 mV in extracellular Na+-free solutions
Y847W
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alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
D928A
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the mutant exhibits a modest reduction of the apparent Na+ affinity to 5fold relative to the wild type enzyme
D928E
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the mutant exhibits a modest reduction of the apparent Na+ affinity to 4fold relative to the wild type enzyme
D928H
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the mutant exhibits a modest reduction of the apparent Na+ affinity to 7fold relative to the wild type enzyme
D928L
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the mutant exhibits a modest reduction of the apparent Na+ affinity to 10fold relative to the wild type enzyme
D928N
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the mutant exhibits a dramatic reduction of the apparent Na+ affinity to 78fold and slight 1.5fold increase of apparent K+ affinity relative to the wild type enzyme
E314D
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the mutant exhibits an 3.2fold increase of the apparent Na+ affinity and 1.7fold increase of apparent K+ affinity relative to the wild type enzyme
E314D/D928A
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the mutant exhibits an 1.2fold increase of the apparent Na+ affinity and slight 1.7fold decrease of apparent K+ affinity relative to the wild type enzyme
E314D/D928N
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the mutant exhibits a modest 8.1fold decrease of the apparent Na+ affinity and slight 1.5fold increase of apparent K+ affinity relative to the wild type enzyme
G803C
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the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
L337C
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K+ induced current, I_K in nA, lower (negative) than control - ouabain-sensitive current, I_ouab in nA, lower (negative) than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
L802C
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the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
P801C
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the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
T339C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower control
T341C
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K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, similar to control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
T804C
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the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
V342C
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K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
V805C
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the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
D813C
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decrease in cation/anion selectivity, which is grossly impaired after treatment with 2-trimethylammonium-ethyl-methanethiosulphonate
D817C
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highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
E321C
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reaction with 2-trimethylammonium-ethyl-methanethiosulphonate does not decrease cation current
E336C
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decrease in cation/anion selectivity, which is transformed from cation-selective to anoin-selective after treatment with 2-trimethylammonium-ethyl-methanethiosulphonate
E788C
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highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
G805C
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reaction with 2-trimethylammonium-ethyl-methanethiosulphonate or with 2-aminocarbonyl-ethyl-methanethiosulphonate does not decrease cation current
N785C
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highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
T806C
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cation current is diminished after reaction with 2-trimethylammonium-ethyl-methanethiosulphonat and 7fold decreased after reaction with 2-aminocarbonyl-ethyl-methanethiosulphonate
S62C
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beta-subunit: mutation for site-directed fluorescence labeling without impairing enzyme function
S62C
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beta1-subunit mutant with Cys for site-directed fluorescence labeling
A330C
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difference between K+-induced and ouabain-sensitive I/V curve especially in the negative voltage range, negative slope of the I/V curve of the ouabain-sensitive current in the low and positive membrane potential range
A330C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
A338C
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difference between K+-induced and ouabain-sensitive I/V curve especially in the negative voltage range
A338C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
C111S
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little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
E334C
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negative slope of the I/V curve of the ouabain-sensitive current in the low and positive membrane potential range, K+-activated current with an amplitude half of the oubain-sensitive current in the high negative membrane potential range
E334C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
F323C
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small ouabain-sensitive current over the whole membrane potential range, significant K+-induced inward curve mostly at negative membrane potential range
F323C
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K+ induced current, I_K in nA, lower than control(negativ) - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
G326C
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inhibition by 2-aminoethyl-methanethiosulfonate
G326C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
G335C
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identical and strongly voltage-dependent I/V relationship of the K+-induced and ouabain sensitive currents
G335C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
I322C
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little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
I322C
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K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
I325C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
I325C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
I327C
-
difference between K+-induced and ouabain-sensitive I/V curve especially in the negative voltage range
I327C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
I328C
-
negative slope of the I/V curve of the ouabain-sensitive current in the low and positive membrane potential range
I328C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
L324C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
L324C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, similar to control
L336C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
L336C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
L344C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
L344C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
N331C
-
difference between K+-induced and ouabain-sensitive I/V curve especially in the negative voltage range
N331C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, similar to control
P333C
-
inhibition by 2-aminoethyl-methanethiosulfonate
P333C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
V321C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
V321C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, similar to control
V329C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
V329C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, similar to control
V332C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
V332C
-
K+ induced current, I_K in nA, similar to control - ouabain-sensitive current, I_ouab in nA, similar to control - membrane conductance induced by palytoxin, G_PTX in mikroS, similar to control
V340C
-
little voltage dependence in the low membrane voltage range and a slight voltage dependence in the high negative membrane voltage range
V340C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
additional information
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knockdown of alpha3 isoform expression by alpha3 siRNA, and increasing alpha1 isoform expression by transient transfection of alpha1 cDNA in Panc-1 cells
additional information
-
reduction of Na+, K+-ATPase alpha1 subunit expression by siRNA transfection
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