Glut3: Difference between revisions

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 <StructureSection load='5c65' size='340' side='right' caption='GLUT3=''>
 == Function ==
-GLUT3 is one of fourteen facilitative sugar transporters, which use the glucose diffusion gradient to move across various plasma membranes to display various specificities, kinetics and tissue expression profiles <ref name="three">Long, W., & Cheeseman, C. I. (2015). Structure of, and functional insight into the GLUT family of membrane transporters. Cell Health and Cytoskeleton, 7, 167-183. doi:10.2147/CHC.S60484</ref>. Glucose transporters are approximately 500 amino acids in length and part of a growing superfamily of integral membrane glycoproteins that have 12 transmembrane (TM) helices. The transmembrane regions presumably create channels through which glucose can move<ref name="four">Kipmen-Korgun, D., Bilmen-Sarikcioglu, S., Altunbas, H., Demir, R., & Korgun, E. T. (2009). Type-2 diabetes down-regulates glucose transporter proteins and genes of the human blood leukocytes.Scandinavian Journal of Clinical and Laboratory Investigation, 69(3), 350-358.
+GLUT3 is one of 14 facilitative sugar transporters, which use the glucose diffusion gradient to move across various plasma membranes to display various specificities, kinetics and tissue expression profiles <ref name="three">Long, W., & Cheeseman, C. I. (2015). Structure of, and functional insight into the GLUT family of membrane transporters. Cell Health and Cytoskeleton, 7, 167-183. doi:10.2147/CHC.S60484</ref>. Glucose transporters are approximately 500 amino acids in length and part of a growing superfamily of integral membrane glycoproteins that have 12 transmembrane (TM) helices. The transmembrane regions presumably create channels through which glucose can move<ref name="four">Kipmen-Korgun, D., Bilmen-Sarikcioglu, S., Altunbas, H., Demir, R., & Korgun, E. T. (2009). Type-2 diabetes down-regulates glucose transporter proteins and genes of the human blood leukocytes.Scandinavian Journal of Clinical and Laboratory Investigation, 69(3), 350-358.
 doi:10.1080/00365510802632163</ref>. GLUT3 is categorized as a Class I transporter due to its protein sequence and structural similarity to other glucose transporters grouped in Class I<ref name="three"/>. GLUT3 displays the highest affinity for glucose of all of the Class I glucose transporters and has a transport capacity five times greater than that of GLUT1 and GLUT4<ref name="five"> 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. doi:10.1152/ajpendo.90388.2008</ref>. In humans, GLUT3 is found predominantly in brain tissue, highly and specifically expressed by neurons, and has some expression in peripheral tissues. For this reason GLUT3 is commonly known as the “neuronal glucose transporter”<ref name="five"/><ref name="six">Maher, F., Vannucci, S. J., & Simpson, I. A. (1994). Glucose transporter proteins in brain. FASEB Journal, 8(13), 1003-1011.</ref>.  GLUT3 has a more restricted expression pathway, which represents specialized functions for the protein<ref name="seven">Xu, J., Lu, C., Wang, J., Zhang, R., Qian, X., & Zhu, H. (2015). Regulation of human trophoblast GLUT3 glucose transporter by mammalian target of rapamycin signaling. International Journal of Molecular Sciences, 16(6), 13815-13828. doi:10.3390/ijms160613815</ref>. GLUT3 has been found to play an important role in gestational development and maintaining the brain's structure. Defects in GLUT3 can cause fetal death as well as neurodegeneration, which can lead to diseases like Alzheimer’s<ref name="eight">Liu, Y., Liu, F., Iqbal, K., Grundke-Iqbal, I., & Gong, C. -. (2008). Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in alzheimer disease. FEBS Letters, 582(2), 359-364. doi:10.1016/j.febslet.2007.12.035</ref>.