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Na+/K+-ATPase
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Na+/K+-ATPase (also known as the Na+/K+ pump, sodium-potassium pump, or simply NAKA, for short) is an enzyme (EC 3.6.3.9 (http://www.expasy.org/cgibin/nicezyme.pl?3.6.3.9)) located in the plasma membrane (specifically an electrogenic transmembrane ATPase). It is found in the human cell and is common to all cellular life.

Contents
1 Function 1.1 Resting potential 1.2 Transport 2 Mechanism 3 Regulation 3.1 Endogenous 3.2 Exogenous 4 Discovery 5 Genes 6 See also 7 References 8 External links

Flow of ions.

Function
The Na+/K+-ATPase helps maintain resting potential, avail transport and regulate cellular volume.
Alpha and beta units.

Resting potential
See also: Resting potential In order to maintain the cell potential, cells must keep a low concentration of sodium ions and high levels of potassium ions within the cell (intracellular). Outside of the cells (extracellular), there are high concentrations of sodium and low concentrations of potassium, so diffusion occurs through ion channels in the plasma membrane. In order to keep the appropriate concentrations, the sodiumpotassium pump pumps sodium out and potassium in through active transport. As the plasma membrane is far less permeable to sodium than it is to potassium ions, an electric potential (negative intracellularly) is the eventual result. The resting potential avails action potentials of nerves and muscles.

Transport
Export of sodium from the cell provides the driving force for several facilitated membrane transport proteins, which import glucose, amino acids and other nutrients into the cell. Translocation of sodium from one side of an epithelium to http://en.wikipedia.org/wiki/NaKATPase

Sodium-potassium pump, E2-Pi state. Calculated hydrocarbon boundaries of the lipid bilayer are shown as blue (intracellular) and red (extracellular) planes

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Na+/K+-ATPase - Wikipedia, the free encyclopedia the other side creates an osmotic gradient that drives the absorption of water.

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Another important task of the Na+-K+ pump is to provide a Na+ gradient that is used by certain carrier processes. In the gut, for example, sodium is transported out of the resorbing cell on the blood side via the Na+-K+ pump, whereas, on the resorbing side, the Na+-Glucose symporter uses the created Na+ gradient as a source of energy to import both Na+ and Glucose, which is far more efficient than simple diffusion. Similar processes are located in the renal tubular system.

Mechanism
The pump, with bound ATP, binds 3 intracellular Na+ ions. ATP is hydrolyzed, leading to phosphorylation of the pump at a highly conserved aspartate residue and subsequent release of ADP. A conformational change in the pump exposes the Na+ ions to the outside. The phosphorylated form of the pump has a low affinity for Na+ ions, so they are released. The pump binds 2 extracellular K+ ions. This causes the dephosphorylation of the pump, reverting it to its previous conformational state, transporting the K+ ions into the cell. The unphosphorylated form of the pump has a higher affinity for Na+ ions than K+ ions, so the two bound K+ ions are released. ATP binds, and the process starts again.

Regulation
Endogenous
The Na+/K+-ATPase is thought to be downregulated by cAMP.[1] Thus, substances causing an increase in cAMP downregulates Na+/K+-ATPase. These include the ligands of the Gscoupled GPCRs. In contrast, substances causing a decrease in cAMP upregulates Na+/K+-ATPase. These include the ligands of the Gicoupled GPCRs. It should be noted that cAMP also acts as a second messenger causing an increase in protein abundance of Na-K-ATPase.

Exogenous
The Na+-K+-ATPase can be pharmacologically modified by administrating drugs exogenously. For instance, Na+-K+-ATPase found in the membrane of heart cells is an important target of cardiac glycosides (for example digoxin and ouabain), inotropic drugs used to improve heart performance by increasing its force of contraction. Contraction of any muscle is dependent on a 100- to 10,000-times higher-than-resting intracellular Ca2+ concentration, which, as soon as it is put back again on its normal level by a carrier enzyme in the plasma membrane, and a calcium pump in sarcoplasmic reticulum, muscle relaxes. http://en.wikipedia.org/wiki/NaKATPase 2/17/2008

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Since this carrier enzyme (Na+-Ca2+ translocator) uses the Na gradient generated by the Na+-K+ pump to remove Ca2+ from the intracellular space, slowing down the Na+-K+ pump results in a permanently-higher Ca2+ level in the muscle, which will eventually lead to stronger contractions.

Discovery
Na+/K+-ATPase was discovered by Jens Christian Skou in 1957 while working as assistant professor at the Department of Physiology, University of Aarhus, Denmark. He published his work in 1957.[2] In 1997, he received one-half of the Nobel Prize in Chemistry "for the first discovery of an ion-transporting enzyme, Na+, K+ -ATPase."[3]

Genes
Alpha: ATP1A1[1] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1A1), ATP1A2[2] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1A2), ATP1A3[3] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1A3), ATP1A4[4] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1A4). #1 predominates in kidney. #2 is also known as "alpha(+)" Beta: ATP1B1[5] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1B1), ATP1B2 (http://www.genenames.org/data/hgnc_data.php?match=ATP1B2), ATP1B3[6] (http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1B3), ATP1B4 (http://www.genenames.org/data/hgnc_data.php?match=ATP1B4)

See also
V-ATPase active transport

References
1. ^ Regulation of Na+-K+-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein (http://ajpcell.physiology.org/cgi/content/full/279/5/C1516) Kinji Kurihara, Nobuo Nakanishi, and Takao Ueha. Departments of 1 Oral Physiology and 2 Biochemistry, School of Dentistry, Meikai University, Sakado, Saitama 350-0283, Japan 2. ^ Skou J (1957). "The influence of some cations on an adenosine triphosphatase from peripheral nerves.". Biochim Biophys Acta 23 (2): 394-401. PMID 13412736 (http://www.ncbi.nlm.nih.gov/pubmed/13412736). 3. ^ http://nobelprize.org/chemistry/laureates/1997/index.html A pdf copy of the paper (reference 1) appears on http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf

External links
MeSH Sodium,+Potassium+ATPase (http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi? mode=&term=Sodium,+Potassium+ATPase) Retrieved from "http://en.wikipedia.org/wiki/Na%2B/K%2B-ATPase" Categories: All articles with unsourced statements | Articles with unsourced statements since February 2008 | EC 3.6.3 | Transport proteins

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This page was last modified on 11 February 2008, at 21:38. All text is available under the terms of the GNU Free Documentation License. (See Copyrights for details.) Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a U.S. registered 501(c)(3) tax-deductible nonprofit charity.

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Na+/K+-ATPase - Wikipedia, the free encyclopedia Shortcut Text NaKATPase navigation search

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lipid bilayer superscript subscript technical limitations enzyme EC 3.6.3.9 plasma membrane transmembrane ATPase human cell life citation needed hide 1 Function 1.1 Resting potential 1.2 Transport 2 Mechanism 3 Regulation 3.1 Endogenous 3.2 Exogenous 4 Discovery 5 Genes 6 See also 7 References 8 External links edit resting potential volume edit sodium potassium intracellular http://en.wikipedia.org/wiki/NaKATPase

Internet Address http://en.wikipedia.org/w/index.php?title=NaKATPase&redire http://en.wikipedia.org/wiki/NaKATPase#column-one http://en.wikipedia.org/wiki/NaKATPase#searchInput http://en.wikipedia.org/wiki/Image:NaKpompe2.jpg http://en.wikipedia.org/wiki/Image:Sodium_Pump.svg http://en.wikipedia.org/wiki/Image:3b8e.gif http://en.wikipedia.org/wiki/Lipid_bilayer http://en.wikipedia.org/wiki/Superscript http://en.wikipedia.org/wiki/Subscript http://en.wikipedia.org/wiki/Wikipedia:Naming_conventions_( #Subscripts_and_superscripts http://en.wikipedia.org/wiki/Enzyme http://en.wikipedia.org/wiki/EC_number http://www.expasy.org/cgi-bin/nicezyme.pl?3.6.3.9 http://en.wikipedia.org/wiki/Plasma_membrane http://en.wikipedia.org/wiki/Transmembrane_ATPase http://en.wikipedia.org/wiki/Human http://en.wikipedia.org/wiki/Cell_(biology) http://en.wikipedia.org/wiki/Life http://en.wikipedia.org/wiki/Wikipedia:Citation_needed javascript:toggleToc() http://en.wikipedia.org/wiki/NaKATPase#Function http://en.wikipedia.org/wiki/NaKATPase#Resting_potential http://en.wikipedia.org/wiki/NaKATPase#Transport http://en.wikipedia.org/wiki/NaKATPase#Mechanism http://en.wikipedia.org/wiki/NaKATPase#Regulation http://en.wikipedia.org/wiki/NaKATPase#Endogenous http://en.wikipedia.org/wiki/NaKATPase#Exogenous http://en.wikipedia.org/wiki/NaKATPase#Discovery http://en.wikipedia.org/wiki/NaKATPase#Genes http://en.wikipedia.org/wiki/NaKATPase#See_also http://en.wikipedia.org/wiki/NaKATPase#References http://en.wikipedia.org/wiki/NaKATPase#External_links http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Resting_potential http://en.wikipedia.org/wiki/Volume http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Sodium http://en.wikipedia.org/wiki/Potassium http://en.wikipedia.org/wiki/Intracellular 2/17/2008

Na+/K+-ATPase - Wikipedia, the free encyclopedia Shortcut Text extracellular diffusion ion channels active transport action potentials nerves muscles edit membrane transport proteins glucose amino acids epithelium gut symporter renal tubular system edit ATP hydrolyzed phosphorylation aspartate ADP dephosphorylation edit edit cAMP [1] Gs Gi edit cardiac glycosides digoxin ouabain inotropic heart Ca sarcoplasmic reticulum edit Jens Christian Skou

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Internet Address http://en.wikipedia.org/wiki/Extracellular http://en.wikipedia.org/wiki/Diffusion http://en.wikipedia.org/wiki/Ion_channel http://en.wikipedia.org/wiki/Active_transport http://en.wikipedia.org/wiki/Action_potential http://en.wikipedia.org/wiki/Nerve http://en.wikipedia.org/wiki/Muscle http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Membrane_transport_protein http://en.wikipedia.org/wiki/Glucose http://en.wikipedia.org/wiki/Amino_acid http://en.wikipedia.org/wiki/Epithelium http://en.wikipedia.org/wiki/Gut http://en.wikipedia.org/wiki/Symporter http://en.wikipedia.org/wiki/Renal_tubular_system http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Image:NaKpompe-cycle.jpg http://en.wikipedia.org/wiki/Adenosine_triphosphate http://en.wikipedia.org/wiki/Hydrolyzed http://en.wikipedia.org/wiki/Phosphorylation http://en.wikipedia.org/wiki/Aspartate http://en.wikipedia.org/wiki/Adenosine_diphosphate http://en.wikipedia.org/wiki/Dephosphorylation http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Cyclic_adenosine_monophosphate http://en.wikipedia.org/wiki/NaKATPase#_note-0 http://en.wikipedia.org/wiki/Gs_alpha_subunit http://en.wikipedia.org/wiki/Gi_alpha_subunit http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Cardiac_glycoside http://en.wikipedia.org/wiki/Digoxin http://en.wikipedia.org/wiki/Ouabain http://en.wikipedia.org/wiki/Inotrope http://en.wikipedia.org/wiki/Heart http://en.wikipedia.org/wiki/Calcium_in_biology http://en.wikipedia.org/wiki/Sarcoplasmic_reticulum http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Jens_Christian_Skou

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Na+/K+-ATPase - Wikipedia, the free encyclopedia Shortcut Text 1957 University of Aarhus Denmark [2] Nobel Prize in Chemistry [3] edit ATP1A1 [1] ATP1A2 [2] ATP1A3 [3] ATP1A4 [4] ATP1B1 [5] ATP1B2 ATP1B3 [6] ATP1B4 edit V-ATPase edit ^ Regulation of Na+-K+-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein ^ PMID 13412736 ^ http://nobelprize.org/chemistry/laureates/1997/index.html http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf edit MeSH Sodium,+Potassium+ATPase hide v d e http://en.wikipedia.org/wiki/NaKATPase

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http://en.wikipedia.org/wiki/1957 http://en.wikipedia.org/wiki/University_of_Aarhus http://en.wikipedia.org/wiki/Denmark http://en.wikipedia.org/wiki/NaKATPase#_note-1 http://en.wikipedia.org/wiki/Nobel_Prize_in_Chemistry http://en.wikipedia.org/wiki/NaKATPase#_note-2 http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/ATP1A1 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://en.wikipedia.org/wiki/ATP1A2 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://en.wikipedia.org/wiki/ATP1A3 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://en.wikipedia.org/wiki/ATP1A4 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://en.wikipedia.org/wiki/ATP1B1 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://www.genenames.org/data/hgnc_data.php?match=ATP1B http://en.wikipedia.org/wiki/ATP1B3 http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1 http://www.genenames.org/data/hgnc_data.php?match=ATP1B http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/V-ATPase http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/NaKATPase#_ref-0 http://ajpcell.physiology.org/cgi/content/full/279/5/C1516

http://en.wikipedia.org/wiki/NaKATPase#_ref-1 http://www.ncbi.nlm.nih.gov/pubmed/13412736 http://en.wikipedia.org/wiki/NaKATPase#_ref-2 http://nobelprize.org/chemistry/laureates/1997/index.html http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATP http://en.wikipedia.org/wiki/Medical_Subject_Headings http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi?mode=&term javascript:collapseTable(0); http://en.wikipedia.org/wiki/Template:ATPases http://en.wikipedia.org/w/index.php?title=Template_talk:ATPa http://en.wikipedia.org/w/index.php?title=Template:ATPases& 2/17/2008

Na+/K+-ATPase - Wikipedia, the free encyclopedia Shortcut Text Acid anhydride hydrolases ATPases Menkes Wilson Ca+ SERCA Plasma membrane H+/K+ ATP synthase H+ (F-type) Dynein Kinesin Myosin hide v d e ion pumps Cotransporter Na+/K+/2ClNa/Pi3 Na+/ClNa/glucose Na+/ICl-/K+ 4 5 Antiporter (exchanger) Na+/H+ Na+/Ca2+ Na+/(Ca2+-K+) Cl-/HCO3- (Band 3) Cl-formate exchanger Cl-oxalate exchanger ATP2A2 Uniporter Halorhodopsin Proton pump http://en.wikipedia.org/wiki/Na%2B/K%2B-ATPase

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Internet Address http://en.wikipedia.org/wiki/Acid_anhydride_hydrolases http://en.wikipedia.org/wiki/ATPase http://en.wikipedia.org/wiki/ATP7A http://en.wikipedia.org/wiki/Wilson_disease_protein http://en.wikipedia.org/wiki/Calcium_ATPase http://en.wikipedia.org/wiki/SERCA http://en.wikipedia.org/wiki/Plasma_membrane_Ca2+_ATPase http://en.wikipedia.org/wiki/Hydrogen_potassium_ATPase http://en.wikipedia.org/wiki/ATP_synthase http://en.wikipedia.org/wiki/F-ATPase http://en.wikipedia.org/wiki/Dynein http://en.wikipedia.org/wiki/Kinesin http://en.wikipedia.org/wiki/Myosin javascript:collapseTable(1); http://en.wikipedia.org/wiki/Template:Ion_pumps http://en.wikipedia.org/w/index.php?title=Template_talk:Ion_p http://en.wikipedia.org/w/index.php?title=Template:Ion_pump http://en.wikipedia.org/wiki/Ion_transporter http://en.wikipedia.org/wiki/Cotransporter http://en.wikipedia.org/wiki/Na-K-2Cl_symporter http://en.wikipedia.org/wiki/Sodium/phosphate_cotransporter http://en.wikipedia.org/wiki/Sodium-chloride_symporter http://en.wikipedia.org/wiki/Sodium-glucose_transport_protein http://en.wikipedia.org/wiki/Sodium-iodide_symporter http://en.wikipedia.org/wiki/Chloride_potassium_symporter http://en.wikipedia.org/wiki/Chloride_potassium_symporter_4 http://en.wikipedia.org/wiki/Chloride_potassium_symporter_5 http://en.wikipedia.org/wiki/Antiporter http://en.wikipedia.org/wiki/Sodium-hydrogen_antiporter http://en.wikipedia.org/wiki/Sodium-calcium_exchanger http://en.wikipedia.org/wiki/Potassium-dependent_sodiumhttp://en.wikipedia.org/wiki/Band_3 http://en.wikipedia.org/wiki/Cl-formate_exchanger http://en.wikipedia.org/wiki/Cl-oxalate_exchanger http://en.wikipedia.org/wiki/ATP2A2 http://en.wikipedia.org/wiki/Uniporter http://en.wikipedia.org/wiki/Halorhodopsin http://en.wikipedia.org/wiki/Proton_pump http://en.wikipedia.org/wiki/Na+/K+-ATPase

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