Aquaporin By Ryan Osgood and Mackenzie Blinn. What they are Aquaporin is a protein embedded in the...
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Transcript of Aquaporin By Ryan Osgood and Mackenzie Blinn. What they are Aquaporin is a protein embedded in the...
![Page 1: Aquaporin By Ryan Osgood and Mackenzie Blinn. What they are Aquaporin is a protein embedded in the cell membrane in order to regulate the flow of water.](https://reader035.fdocuments.us/reader035/viewer/2022062500/56649e7e5503460f94b80cda/html5/thumbnails/1.jpg)
AquaporinBy Ryan Osgood and Mackenzie Blinn
![Page 2: Aquaporin By Ryan Osgood and Mackenzie Blinn. What they are Aquaporin is a protein embedded in the cell membrane in order to regulate the flow of water.](https://reader035.fdocuments.us/reader035/viewer/2022062500/56649e7e5503460f94b80cda/html5/thumbnails/2.jpg)
What they are
• Aquaporin is a protein embedded in the cell membrane in order to regulate the flow of water
• Water needs to move in and out of a cell, and this is facilitated by aquaporins (water channels)
• The presence of these water channels increases the permeability to water of the cell membrane
• These channels are allocated in all kingdoms of life including bacteria, plants, and mammals
• 13 in mammals, 6 in kidney
• In plants- 4 families
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Used for
• Industrial water treatment
• Regulates flow of water in organisms, particularly in the kidney.
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Who discovered them• In 1992 Peter Agre at John
Hopkins University reported his unintentional discovery of aquaporin, he earned a Nobel Prize for his discovery in 2003 .
• In 2000 Stroud’s lab at UCSF succeeded in solving the first high resolution structure of an aquaporin by using x-ray crystallography
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Primary Structure
• Used for water reabsorption
• Found in kidney
• We can see its primary structure because of the amino acid linear sequence
• Simple proteins- AQP monomer has 6x helical domains
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Secondary Structure
• 6 trans membrane helices in a RH Bundle- it forms a tetrameter
• Early evolutionary event
• Used for water reabsorption in response to ADH (a hormone)
• We can see its secondary structure because of the alpha-helices
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Tertiary Structure
• Found in kidney and medullary collecting duct
• Used for water reabsorption and glycerol permeability
• We can see its tertiary because of the tightness of the helixes folded in one compact globule.
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Quaternary Structure
• Used for water reabsorption
• Found in kidney
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More on that…
• Some membranes are more permeable than others. RBC’s, kidney tubules
• AQP 1 was reported in 1992.
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Diseases
• Several diseases such as congenital cataracts and nephrogenic diabetes insipidus are relate to mutations in aquaporins, also fluid transport, brain swelling, strokes, meningities, multiple sclerosis.
• A small number of people are found with a deficiency of aquaporins and they generally seem healthy, but they have a defect in the ability to concentrate solutes in urine and to conserve water when deprived of drinking water
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Bibliography
• http://www.ks.uiuc.edu/Research/aquaporins/
• http://www.bionaid.us/research.htm
• http://www.aquaporins.org/disease.htm
• http://www.hopkinsmedicine.org/press/2003/october/031008a.htm
• http://en.wikipedia.org/wiki/Aquaporin