Sodium-Potassium Pump On Wikipedia (Landscape)

Na+/K+-ATPase - Wikipedia, the free encyclopedia Page 1 of 12
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/cgi-bin/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
Flow of ions.
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
Function
The Na+/K+-ATPase helps maintain resting potential, avail transport and regulate cellular volume.
Resting potential Alpha and beta units.
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 sodium-potassium 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.
http://en.wikipedia.org/wiki/NaKATPase 2/17/2008
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 the other side creates an osmotic gradient that drives the absorption of
water.
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 Gs-coupled GPCRs.
In contrast, substances causing a decrease in cAMP upregulates Na+/K+-ATPase. These include the ligands of the Gi-coupled 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.
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
This page was last modified on 11 February 2008, at 21:38.

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enzyme http://en.wikipedia.org/wiki/Enzyme
EC http://en.wikipedia.org/wiki/EC_number
3.6.3.9 http://www.expasy.org/cgi-bin/nicezyme.pl?3.6.3.9
plasma membrane http://en.wikipedia.org/wiki/Plasma_membrane
transmembrane ATPase http://en.wikipedia.org/wiki/Transmembrane_ATPase
human http://en.wikipedia.org/wiki/Human
cell http://en.wikipedia.org/wiki/Cell_(biology)
life http://en.wikipedia.org/wiki/Life
citation needed http://en.wikipedia.org/wiki/Wikipedia:Citation_needed
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1 Function http://en.wikipedia.org/wiki/NaKATPase#Function
1.1 Resting potential http://en.wikipedia.org/wiki/NaKATPase#Resting_potential
1.2 Transport http://en.wikipedia.org/wiki/NaKATPase#Transport
2 Mechanism http://en.wikipedia.org/wiki/NaKATPase#Mechanism
3 Regulation http://en.wikipedia.org/wiki/NaKATPase#Regulation
3.1 Endogenous http://en.wikipedia.org/wiki/NaKATPase#Endogenous
3.2 Exogenous http://en.wikipedia.org/wiki/NaKATPase#Exogenous
4 Discovery http://en.wikipedia.org/wiki/NaKATPase#Discovery
5 Genes http://en.wikipedia.org/wiki/NaKATPase#Genes

6 See also http://en.wikipedia.org/wiki/NaKATPase#See_also
7 References http://en.wikipedia.org/wiki/NaKATPase#References
8 External links http://en.wikipedia.org/wiki/NaKATPase#External_links
edit http://en.wikipedia.org/w/index.php?title=Na%2B/K%2B-ATPase&action=edit§ion=1
resting potential http://en.wikipedia.org/wiki/Resting_potential
volume http://en.wikipedia.org/wiki/Volume
sodium http://en.wikipedia.org/wiki/Sodium
potassium http://en.wikipedia.org/wiki/Potassium
intracellular http://en.wikipedia.org/wiki/Intracellular
extracellular http://en.wikipedia.org/wiki/Extracellular
diffusion http://en.wikipedia.org/wiki/Diffusion
ion channels http://en.wikipedia.org/wiki/Ion_channel
active transport http://en.wikipedia.org/wiki/Active_transport
action potentials http://en.wikipedia.org/wiki/Action_potential
nerves http://en.wikipedia.org/wiki/Nerve
muscles http://en.wikipedia.org/wiki/Muscle
membrane transport proteins http://en.wikipedia.org/wiki/Membrane_transport_protein
glucose http://en.wikipedia.org/wiki/Glucose
amino acids http://en.wikipedia.org/wiki/Amino_acid
epithelium http://en.wikipedia.org/wiki/Epithelium
gut http://en.wikipedia.org/wiki/Gut
symporter http://en.wikipedia.org/wiki/Symporter
renal tubular system http://en.wikipedia.org/wiki/Renal_tubular_system
http://en.wikipedia.org/wiki/Image:NaKpompe-cycle.jpg
ATP http://en.wikipedia.org/wiki/Adenosine_triphosphate
hydrolyzed http://en.wikipedia.org/wiki/Hydrolyzed

phosphorylation http://en.wikipedia.org/wiki/Phosphorylation
aspartate http://en.wikipedia.org/wiki/Aspartate
ADP http://en.wikipedia.org/wiki/Adenosine_diphosphate
dephosphorylation http://en.wikipedia.org/wiki/Dephosphorylation
cAMP http://en.wikipedia.org/wiki/Cyclic_adenosine_monophosphate
[1] http://en.wikipedia.org/wiki/NaKATPase#_note-0
Gs http://en.wikipedia.org/wiki/Gs_alpha_subunit
Gi http://en.wikipedia.org/wiki/Gi_alpha_subunit
cardiac glycosides http://en.wikipedia.org/wiki/Cardiac_glycoside
digoxin http://en.wikipedia.org/wiki/Digoxin
ouabain http://en.wikipedia.org/wiki/Ouabain
inotropic http://en.wikipedia.org/wiki/Inotrope
heart http://en.wikipedia.org/wiki/Heart
Ca http://en.wikipedia.org/wiki/Calcium_in_biology
sarcoplasmic reticulum http://en.wikipedia.org/wiki/Sarcoplasmic_reticulum
Jens Christian Skou http://en.wikipedia.org/wiki/Jens_Christian_Skou
1957 http://en.wikipedia.org/wiki/1957
University of Aarhus http://en.wikipedia.org/wiki/University_of_Aarhus
Denmark http://en.wikipedia.org/wiki/Denmark
Nobel Prize in Chemistry http://en.wikipedia.org/wiki/Nobel_Prize_in_Chemistry
ATP1A1 http://en.wikipedia.org/wiki/ATP1A1
[1] http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1A1

ATP1B1 http://en.wikipedia.org/wiki/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 http://en.wikipedia.org/wiki/ATP1B3
[6] http://www.genenames.org/data/hgnc_data.php?hgnc_id=ATP1B3
ATP1B4 http://www.genenames.org/data/hgnc_data.php?match=ATP1B4
V-ATPase http://en.wikipedia.org/wiki/V-ATPase
^ http://en.wikipedia.org/wiki/NaKATPase#_ref-0
Regulation of Na+-K+-ATPase by cAMP-dependent
protein kinase anchored on membrane via its anchoring http://ajpcell.physiology.org/cgi/content/full/279/5/C1516
protein
PMID 13412736 http://www.ncbi.nlm.nih.gov/pubmed/13412736
http://nobelprize.org/chemistry/laureates/1997/index.html http://nobelprize.org/chemistry/laureates/1997/index.html
http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf
MeSH http://en.wikipedia.org/wiki/Medical_Subject_Headings
Sodium,+Potassium+ATPase http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi?mode=&term=Sodium,+Potassium+ATPase
hide javascript:collapseTable(0);
v http://en.wikipedia.org/wiki/Template:ATPases
d http://en.wikipedia.org/w/index.php?title=Template_talk:ATPases&action=edit

e http://en.wikipedia.org/w/index.php?title=Template:ATPases&action=edit
Acid anhydride hydrolases http://en.wikipedia.org/wiki/Acid_anhydride_hydrolases
ATPases http://en.wikipedia.org/wiki/ATPase
Menkes http://en.wikipedia.org/wiki/ATP7A
Wilson http://en.wikipedia.org/wiki/Wilson_disease_protein
Ca+ http://en.wikipedia.org/wiki/Calcium_ATPase
SERCA http://en.wikipedia.org/wiki/SERCA
Plasma membrane http://en.wikipedia.org/wiki/Plasma_membrane_Ca2+_ATPase
H+/K+ http://en.wikipedia.org/wiki/Hydrogen_potassium_ATPase
ATP synthase http://en.wikipedia.org/wiki/ATP_synthase
H+ (F-type) http://en.wikipedia.org/wiki/F-ATPase
Dynein http://en.wikipedia.org/wiki/Dynein
Kinesin http://en.wikipedia.org/wiki/Kinesin
Myosin http://en.wikipedia.org/wiki/Myosin
hide javascript:collapseTable(1);
v http://en.wikipedia.org/wiki/Template:Ion_pumps
d http://en.wikipedia.org/w/index.php?title=Template_talk:Ion_pumps&action=edit
e http://en.wikipedia.org/w/index.php?title=Template:Ion_pumps&action=edit
ion pumps http://en.wikipedia.org/wiki/Ion_transporter
Cotransporter http://en.wikipedia.org/wiki/Cotransporter
Na+/K+/2Cl- http://en.wikipedia.org/wiki/Na-K-2Cl_symporter
Na/Pi3 http://en.wikipedia.org/wiki/Sodium/phosphate_cotransporter
Na+/Cl- http://en.wikipedia.org/wiki/Sodium-chloride_symporter
Na/glucose http://en.wikipedia.org/wiki/Sodium-glucose_transport_proteins
Na+/I- http://en.wikipedia.org/wiki/Sodium-iodide_symporter
Cl-/K+ http://en.wikipedia.org/wiki/Chloride_potassium_symporter
4 http://en.wikipedia.org/wiki/Chloride_potassium_symporter_4
5 http://en.wikipedia.org/wiki/Chloride_potassium_symporter_5
Antiporter (exchanger) http://en.wikipedia.org/wiki/Antiporter

Na+/H+ http://en.wikipedia.org/wiki/Sodium-hydrogen_antiporter
Na+/Ca2+ http://en.wikipedia.org/wiki/Sodium-calcium_exchanger
Na+/(Ca2+-K+) http://en.wikipedia.org/wiki/Potassium-dependent_sodium-calcium_exchanger
Cl-/HCO3- (Band 3) http://en.wikipedia.org/wiki/Band_3
Cl-formate exchanger http://en.wikipedia.org/wiki/Cl-formate_exchanger
Cl-oxalate exchanger http://en.wikipedia.org/wiki/Cl-oxalate_exchanger
Uniporter http://en.wikipedia.org/wiki/Uniporter
Halorhodopsin http://en.wikipedia.org/wiki/Halorhodopsin
Proton pump http://en.wikipedia.org/wiki/Proton_pump
http://en.wikipedia.org/wiki/Na%2B/K%2B-ATPase http://en.wikipedia.org/wiki/Na+/K+-ATPase
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Na+/K+-ATPase - Wikipedia, the free encyclopedia Page 1 of 12

Resting potential Alpha and beta units.

See also: Resting potential

The resting potential avails action potentials of nerves and muscles.

The Na+/K+-ATPase is thought to be downregulated by cAMP.[1]

The Na+-K+-ATPase can be pharmacologically modified by administrating drugs exogenously.

A pdf copy of the paper (reference 1) appears on http://jasn.asnjournals.org/cgi/reprint/9/11/2170.pdf

Retrieved from "http://en.wikipedia.org/wiki/Na%2B/K%2B-ATPase"

This page was last modified on 11 February 2008, at 21:38.

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