Sandbox Reserved 1358

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{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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==Discussion 1==
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==GLUT3 / SLC2A3==
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<StructureSection load='1bna' size='340' side='right' caption='Structure of DNA' scene=''>
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<StructureSection load='5c65' size='340' side='right' caption='Structure of DNA' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==
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The GLUT3 protein, encoded by the SLC2A3 gene in humans, found in mammalian cells, allows for the transport of the glucose molecule across the plasma membrane. It is especially prevalent in the axons of nerve cells in brain tissue. In neurons themselves, GLUT3 is the main glucose transporter that is utilized. In the human body, of the first four glucose transporters discovered (GLUT1, GLUT2, GLUT3, and GLUT4), GLUT3 has a higher glucose affinity and transport capacity, which facilitates its use in glucose transport in neurons. This is significant because the glucose levels surrounding the neuron are five times lower than those found in serum (blood). GLUT3 is also present in sperm, embryos, white blood cells and carcinoma cell lines.
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== Structure ==
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GLUT3 transport protein is composed of 481 amino acids, <scene name='77/777678/Two_protein_chains/1'>two alpha helical protein chains</scene>, and two different ligands, ligand <scene name='77/777678/Ligand_y01/1'>Y01</scene> and ligand <scene name='77/777678/Ligand_37x/1'>37X</scene>. On the protein, one ligand Y01, known as Cholesterol hemisuccinate, is attached to chain a, and one to chain b. Ligand 37X is called Octyl Glucose Neopentyl Glycol, and there are 6 of these ligands on chain a and 3 on chain b.
== Disease ==
== Disease ==
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Correlations between low levels of glucose transport proteins and abnormal hyperphosphorylation of tau in Alzheimer Disease. Individuals with Alzheimer Disease have decreased levels of GLUT3 and GLUT1 in their brain.
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== Relevance ==
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</StructureSection>
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== References ==
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Kayano, T., Fukumoto, H., Eddy, R. L., Fan, Y. S., Byers, M. G., Shows, T. B., & Bell, G. I. (n.d.). Cell Glucose Transport and Glucose Handling During Fetal and Neonatal Development. Retrieved from Journal of Biological Chemistry website: http://www.jbc.org/content/263/30/15245.short
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== Structural highlights ==
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Liu, Y., Liu, F., Iqbal, K., Grundke-Iqbal, I., & Gong, C.-X. (2008). Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer disease. FEBS Letters, 582(2), 359–364. http://doi.org/10.1016/j.febslet.2007.12.035
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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Simmons, R. A. (2017). Cell Glucose Transport and Glucose Handling During Fetal and Neonatal Development. Retrieved from Science Direct website: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/glut3
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</StructureSection>
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Simpson, I. A., Dwyer, D., Malide, D., Moley, K. H., Travis, A., & Vannucci, S. J. (2008). The facilitative glucose transporter GLUT3: 20 years of distinction. American Journal of Physiology - Endocrinology and Metabolism, 295(2), E242–E253. http://doi.org/10.1152/ajpendo.90388.2008
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== References ==
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<references/>
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Current revision

This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

GLUT3 / SLC2A3

Structure of DNA

Drag the structure with the mouse to rotate

References

Kayano, T., Fukumoto, H., Eddy, R. L., Fan, Y. S., Byers, M. G., Shows, T. B., & Bell, G. I. (n.d.). Cell Glucose Transport and Glucose Handling During Fetal and Neonatal Development. Retrieved from Journal of Biological Chemistry website: http://www.jbc.org/content/263/30/15245.short

Liu, Y., Liu, F., Iqbal, K., Grundke-Iqbal, I., & Gong, C.-X. (2008). Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer disease. FEBS Letters, 582(2), 359–364. http://doi.org/10.1016/j.febslet.2007.12.035

Simmons, R. A. (2017). Cell Glucose Transport and Glucose Handling During Fetal and Neonatal Development. Retrieved from Science Direct website: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/glut3

Simpson, I. A., Dwyer, D., Malide, D., Moley, K. H., Travis, A., & Vannucci, S. J. (2008). The facilitative glucose transporter GLUT3: 20 years of distinction. American Journal of Physiology - Endocrinology and Metabolism, 295(2), E242–E253. http://doi.org/10.1152/ajpendo.90388.2008

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