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Na
+
/K
+
-ATPase
From Wikipedia, the free encyclopedia
(Redirected from NaKATPase)
Na
+
/K
+
-ATPase
(also known as the
Na
+
/K
+
pump
,
sodium-potassium pump
, orsimply
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 anelectrogenic transmembrane ATPase). It is found in the human cell and is commonto all cellular life.
Function
The Na
+
/K
+
-ATPase helps maintain resting potential, avail transport and regulatecellular volume.
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 andlow concentrations of potassium, so diffusion occurs through ion channels in theplasma membrane. In order to keep the appropriate concentrations, the sodium-potassium pump pumps sodium out and potassium in through active transport. Asthe 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 facilitatedmembrane transport proteins, which import glucose, amino acids and othernutrients into the cell. Translocation of sodium from one side of an epithelium to
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.Alpha and beta units.Sodium-potassium pump, E2-Pistate. Calculated hydrocarbonboundaries of the lipid bilayer areshown as blue (intracellular) andred (extracellular) planes
Page 1 of 10Na+/K+-ATPase - Wikipedia, the free encyclopedia2/17/2008http://en.wikipedia.org/wiki/NaKATPase
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 thegut, for example, sodium is transported out of the resorbing cell on the blood side via the Na
+
-K
+
pump, whereas, onthe 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 tubularsystem.
Mechanism
The pump, with bound ATP, binds 3intracellular Na
+
ions.
ATP is hydrolyzed, leading tophosphorylation of the pump at a highlyconserved aspartate residue and subsequentrelease of ADP.
A conformational change in the pumpexposes the Na
+
ions to the outside. Thephosphorylated form of the pump has a lowaffinity for Na
+
ions, so they are released.
The pump binds 2 extracellular K
+
ions. Thiscauses the dephosphorylation of the pump,reverting it to its previous conformationalstate, transporting the K
+
ions into the cell.
The unphosphorylated form of the pump hasa higher affinity for Na
+
ions than K
+
ions, so the two bound K
+
ions are released. ATP binds, and the processstarts 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 G
s
-coupled GPCRs.In contrast, substances causing a decrease in cAMP upregulates Na
+
/K
+
-ATPase. These include the ligands of the G
i
-coupled GPCRs. It should be noted that cAMP also acts as a second messenger causing an increase in proteinabundance 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 (forexample 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 Ca
2+
concentration,which, as soon as it is put back again on its normal level by a carrier enzyme in the plasma membrane, and a calciumpump in sarcoplasmic reticulum, muscle relaxes.Page 2 of 10Na+/K+-ATPase - Wikipedia, the free encyclopedia2/17/2008http://en.wikipedia.org/wiki/NaKATPase
Since this carrier enzyme (Na
+
-Ca
2+
translocator) uses the Na gradient generated by the Na
+
-K
+
pump to remove Ca
2+
from the intracellular space, slowing down the Na
+
-K
+
pump results in a permanently-higher Ca
2+
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 Departmentof 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 alsoknown 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 anchoringprotein (http://ajpcell.physiology.org/cgi/content/full/279/5/C1516) Kinji Kurihara, Nobuo Nakanishi, and TakaoUeha. Departments of 1 Oral Physiology and 2 Biochemistry, School of Dentistry, Meikai University, Sakado,Saitama 350-0283, Japan2.
^
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.htmlA 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 proteinsPage 3 of 10Na+/K+-ATPase - Wikipedia, the free encyclopedia2/17/2008http://en.wikipedia.org/wiki/NaKATPase
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