Pumps Na+/K+ ATPase:

History:

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 that year.
In 1997, he received one-half of the Nobel Prize in Chemistry "for the first discovery of an ion-transporting enzyme, Na+/ K+-ATPase."

Function: 

Export of sodium from the cell provides the driving force for several secondary active transporters , which import glucose, amino acids, and other nutrients into the cell by use of the sodium gradient.

 Failure of the Na+-K+ pumps can result in swelling of the cell. A cell's osmolarity is the sum of the concentrations of the various ion species and many proteins and other organic compounds inside the cell. When this is higher than the osmolarity outside of the cell, water flows into the cell through osmosis. This can cause the cell to swell up and die (the lyse). The Na+-K+ pump helps to maintain the right concentrations of ions. Furthermore, when the cell begins to swell, this automatically activates the Na+-K+ pump.

http://www.asso-etud.unige.ch/aecb/articles/notes_cours/1ere/biolobarja2011.pdf

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Aquaporins:

     1) Historical:

   These aquaporins have been discovered in 1992 by an american biologist named Peter Agre during a studying about red blood cells: it was during an experience about an injection of a "copy" of DNA (or RNAm) of a protein in an amphibian's egg. In 2003, the biologist was rewarded by the Nobel Prize of Chemistry.


     2) What is the aquaporin?

   At the human's body, aquaporins are really important for the operation of the kidneys. Cellulars have a plasma membrane which no accept the pass of the water. However, they have aquaporins which can pass the water easier through the cellular. In fact, thanks to hydrogen bonds (chemestry bond between  oxygen atoms and hydrogen atoms) and proteins' charges, that the water travel in the plasma membrane.

http://www.proteine.wikibis.com/aquaporine.php

===> More details in this video (1'53''). 

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