7.2.2.13: Na+/K+-exchanging ATPase
This is an abbreviated version!
For detailed information about Na+/K+-exchanging ATPase, go to the full flat file.
Word Map on EC 7.2.2.13
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7.2.2.13
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ouabain
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cardiac
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ouabain-sensitive
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basolateral
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tubule
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erythrocyte
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hypertension
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epithelium
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depolarization
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electrogenic
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glycoside
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cotransporter
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reabsorption
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cl
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contractile
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alpha-subunits
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hyperpolarization
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nephron
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medullary
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normotensive
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amiloride
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digoxin
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transepithelial
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voltage
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sarcolemmal
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atpases
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aldosterone
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myocytes
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na+,k+-atpase
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ca-atpase
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rb+
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microelectrodes
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cardiotonic
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sarcoplasmic
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short-circuit
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phosphoenzyme
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vanadate
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digitalis
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furosemide
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inotropic
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mg2+-atpase
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voltage-clamped
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medicine
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electroneutral
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nai
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natriuresis
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aldosterone-producing
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k+-dependent
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amiloride-sensitive
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bumetanide
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henle
- 7.2.2.13
- ouabain
- cardiac
-
ouabain-sensitive
-
basolateral
- tubule
- erythrocyte
- hypertension
- epithelium
-
depolarization
-
electrogenic
- glycoside
-
cotransporter
-
reabsorption
- cl
-
contractile
- alpha-subunits
-
hyperpolarization
- nephron
- medullary
-
normotensive
- amiloride
- digoxin
-
transepithelial
-
voltage
-
sarcolemmal
- atpases
- aldosterone
- myocytes
- na+,k+-atpase
-
ca-atpase
- rb+
-
microelectrodes
-
cardiotonic
- sarcoplasmic
-
short-circuit
- phosphoenzyme
- vanadate
- digitalis
- furosemide
-
inotropic
- mg2+-atpase
-
voltage-clamped
- medicine
-
electroneutral
- nai
-
natriuresis
-
aldosterone-producing
-
k+-dependent
-
amiloride-sensitive
- bumetanide
- henle
Reaction
Synonyms
(Na+ + K+)-activated ATPase, (Na+ + K+)-ATPase, (Na+, K+)-ATPase, (Na+, K+)-dependent ATPase, (Na+,K+)-activated ATPase, (Na+-K+)-ATPase, alpha2Na+/K+-ATPase, ATP1a1, atp1a1a, ATPalpha, EC 3.6.1.3, EC 3.6.1.37, EC 3.6.3.9, Na pump, Na(+)-K(+)-exchanging ATPase, Na+ pump, Na+, K+ -ATPase, Na+, K+-ATPase, Na+,K+ pump, Na+,K+-adenosine triphosphatase, Na+,K+-ATPase, Na+,K+-pump, Na+-K+ ATPase, Na+-K+ pump, Na+-K+ pump alpha1-isoform, Na+-K+ pump alpha2-isoform, Na+-K+-ATPase, Na+-K+-ATPase alpha2-isoform, Na+-K+-pump, Na+/K+ -ATPase, Na+/K+ ATPase, Na+/K+ pump, Na+/K+-ATPase, Na+K+-ATPase, Na+K+ATPase, Na, K-ATPase, Na,K pump, Na,K-activated ATPase, Na,K-adenosine triphosphatase, Na,K-ATPase, Na,K-Pump, Na-K-ATPase, Na/K pump, Na/K-ATPase, NKA, Nkaalpha protein, nkaalpha1, nkaalpha3a, nkaalpha3b, renal sodium-potassium pump, SNaK1, sodium potassium adenosinetriphosphatase, sodium pump, sodium-potassium pump, sodium/potassium ATPase
ECTree
7.2.2.13 Na+/K+-exchanging ATPaseAdvanced search results
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Source Tissue on EC 7.2.2.13 - Na+/K+-exchanging ATPase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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glioblastoma cells, A172 cells overexpress Na/K-ATPase alpha1 isoform in the caveolar structure
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muscle cell line, A-769662 inhibits the Na+-K+-ATPase cell surface abundance in L6 cells by decreasing the phosphorylation of the alpha-subunit
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enzyme activity is well-maintained in the dissociated neostriatal neurons
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differential distribution of enzyme alpha subunit isoforms in subicular interneurones and pyramidal cells. While ATP1A3-isoforms regulate sodium and potassium homeostasis in subicular interneurones, ATPA1-isoforms assume this function in pyramidal cells
additional information
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electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
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little changes in enzyme alpha subunit isoform composition between summer and winter. Exposure to anoxia does not affect the activity of Na+K+-ATPase, but there is a 150fold extension in brain anoxia tolerance by seasonal changes in energy supply-demand ratio. Enzyme shows 10times lower catalytic activity in winter than in summer
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rodent cancer cells lack discernable expression of the alpha3 subunit Na,K-ATPase isoform
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acclimation to dilute seawater induces increased expression of Na+K+-ATPase and enzyme activity, with the increase being less in juveniles than in larger crabs. Juveniles maintain osmotic and ionic homeostasis by the expression and utilization of extremely high levels of gill Na+K+ATPase, in posterior, as well in anterior, gills
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following acclimation in dilute seawater, specific activity of Na+K+-ATPase is progressively increased up to 3.9fold. Increased enzyme activity may be modulated by the changed proportion of fatty acids in the purified membranes of posterior gills. Long-term acclimation to dilute seawater results in increase in metallothionein content in posterior gill
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in the apical region of the epithelial pillar cells,
and throughout the pillar cell bodies
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neither osmotic pressure, Na+K+-ATPase activity, nor free amino acids are affected by diets rich/low in highly unsaturated fatty acids. Higher water content in gills of shrimp exposed to low salinty is counteracted by increased content in highly unsaturated fatty acids
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Na+K+-ATPase activity is positively regulated via an N-terminal phosphorylation site that is necessary for correct heart morphogenesis to occur, and maintenance of Zonula occludens-1 junction belts requires ion pump activity
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differential distribution of enzyme alpha subunit isoforms in subicular interneurones and pyramidal cells. While ATP1A3-isoforms regulate sodium and potassium homeostasis in subicular interneurones, ATPA1-isoforms assume this function in pyramidal cells
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light microscopic immunocytochemistry detects Na+/K+-ATPase along the renal tubules and collecting ducts. Na+/K+-ATPase is distributed on the basal infoldings of first and second segments of the proximal tubule, and distal tube cells. The distal tube and collecting duct cells show more intense Na+/K+-ATPase immunoreaction in freshwater eel than in seawater-acclimated eel
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from normotensive patients who have unilateral nephrectomy because of renal carcinoma or trauma
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study on enzyme isoforms in muscle in three consecutive days of exercise followed by 3 days of recovery. Increases in subunit isoforms alpha1, alpha2, alpha3 by 46%, 42%, and 31% are observed at recovery day 1, respectively. Subunit isoforms beta1 and beta2 increase by 19% and 28% at recovery day 1, whereas isoform beta3 increase by 18% at recovery day 2. with exception of isoforms alpha 2 and alpha 3, the increases persisted at recovery day 3. The increases in subunit expression are not accompanied by increases in the maximal catalytic activity
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ventricular myocyte. Patchy presence of subunit isoform alpha1 in the transverse tubules and surface sarcolemma, isoform alpha2 is distributed continously in the tramsverse tubules alone. Isoform alpha3 is expressed prominently in the intercalated discs. Subunit isoform beta1 is located in the transverse tubules and surface sarcolemma, and isoform beta2 is mainly located in the intercalated disc. Subunit isoform alpha1 and alpha2 form heterodimers with subunit isoform beta1 and alpha3 with beta2
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ventricular myocyte. Patchy presence of subunit isoform alpha1 in the transverse tubules and surface sarcolemma, isoform alpha2 is distributed continuously in the transverse tubules alone. Isoform alpha3 is expressed slightly. Subunit isoform beta1 is located in the transverse tubules and surface sarcolemma, and isoform beta2 is mainly located in the intercalated disc. Subunit isoform alpha1 and alpha2 form heterodimers with subunit isoform beta1 and alpha3 with beta2
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ventricular myocyte. Subunit isoform alpha 2 accounts for 29.5% of the cation current, and the low-affinity subunit isoform alpha 1 accounts for 70.5% of current. The functional density of the enzyme is significantly higher in t-tubules compared to external sarcolemma. Subunit isoform alpha2 is enriched in t-tubules, while isoform alpha1 is almost uniformly distributed between the t-tubules and external sarcolemma
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oubain-resistant mutant Na+/K+-ATPase is expressed in Xenopus oocytes by microinjection of mRNA coding for the alpha-subunit and the beta-subunit of the protein
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oubain-resistant mutant Na+/K+-ATPase is expressed in Xenopus oocytes by microinjection of mRNA coding for the alpha-subunit and the beta-subunit of the protein
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existence of at least two isoforms of the pump in the horizontal cells
additional information
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enzyme is not detected in skeletal muscle or the dorsal vessel
additional information
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method for histochemical localization of the enzyme
additional information
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method for histochemical localization of the enzyme
additional information
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method for histochemical localization of the enzyme
